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P00918 (CAH2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbonic anhydrase 2

EC=4.2.1.1
Alternative name(s):
Carbonate dehydratase II
Carbonic anhydrase C
Short name=CAC
Carbonic anhydrase II
Short name=CA-II
Gene names
Name:CA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for bone resorption and osteoclast differentiation By similarity. Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6. Ref.13 Ref.50 Ref.58

Catalytic activity

H2CO3 = CO2 + H2O.

Cofactor

Zinc. Can also use cobalt(II) with lower efficiency, but not copper(II), nickel(II) and manganese(II). Ref.105

Enzyme regulation

Activated by X-ray, histamine, L-adrenaline, L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-Ala-His (carnosine). Competitively inhibited by saccharin, thioxolone, coumarins, 667-coumate, celecoxib (Celebrex), valdecoxib (Bextra), SC-125, SC-560, diclofenac, acetate, azide, bromide, sulfonamide derivatives such as acetazolamide (AZA), methazolamide (MZA), ethoxzolamide (EZA), dichlorophenamide (DCP), brinzolamide, dansylamide, thiabendazole-5-sulfonamide, trifluoromethane sulfonamide and N-hydroxysulfamide, fructose-based sugar sulfamate RWJ-37497, and Foscarnet (phosphonoformate trisodium salt). Repressed strongly by hydrogen sulfide(HS) and weakly by nitrate (NO3). Esterase activity weakly reduced by cyanamide. N-hydroxyurea interfers with zinc binding and inhibit activity. Ref.14 Ref.15 Ref.22 Ref.23 Ref.46 Ref.55 Ref.62 Ref.66 Ref.71 Ref.72 Ref.74 Ref.77 Ref.81 Ref.84 Ref.87 Ref.88 Ref.91 Ref.93 Ref.94 Ref.95 Ref.97 Ref.102 Ref.104 Ref.106 Ref.107 Ref.111 Ref.112

Subunit structure

Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity. Interacts with SLC26A6 isoform 4(via C-terminus cytoplasmic domain). Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasm. Cell membrane. Note: Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells. Ref.13

Involvement in disease

Osteopetrosis, autosomal recessive 3 (OPTB3) [MIM:259730]: A rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Recessive osteopetrosis commonly manifests in early infancy with macrocephaly, feeding difficulties, evolving blindness and deafness, bone marrow failure, severe anemia, and hepatosplenomegaly. Deafness and blindness are generally thought to represent effects of pressure on nerves. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.115 Ref.116 Ref.117 Ref.118 Ref.119

Miscellaneous

Target of drugs used in treatments against glaucoma disorder and breast cancer.

Sequence similarities

Belongs to the alpha-carbonic anhydrase family.

Biophysicochemical properties

Absorption:

Abs(max)=550 nm Ref.15 Ref.20 Ref.22 Ref.31 Ref.42 Ref.47 Ref.50 Ref.64 Ref.83 Ref.92

At pH 7.0. Shows a second maximum at 618 nm.

Kinetic parameters:

KM=10 mM for CO2

KM=82 mM for H2CO3

KM=3 mM for 4-nitrophenyl acetate

pH dependence:

Optimum pH is 6-8.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Osteopetrosis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin-activated signaling pathway

Inferred from direct assay Ref.13. Source: UniProtKB

bicarbonate transport

Traceable author statement. Source: Reactome

carbon dioxide transport

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelium

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

one-carbon metabolic process

Inferred from electronic annotation. Source: InterPro

positive regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

positive regulation of cellular pH reduction

Inferred from electronic annotation. Source: Ensembl

positive regulation of dipeptide transmembrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of anion transport

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of intracellular pH

Inferred from sequence or structural similarity. Source: UniProtKB

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to pH

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

secretion

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 14675051. Source: UniProtKB

axon

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 114507Ref.13. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

microvillus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.13. Source: UniProtKB

   Molecular_functioncarbonate dehydratase activity

Traceable author statement Ref.115. Source: ProtInc

zinc ion binding

Inferred from direct assay Ref.19. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8
Chain2 – 260259Carbonic anhydrase 2
PRO_0000077418

Regions

Region198 – 1992Substrate binding

Sites

Active site641
Active site671
Active site1271
Metal binding941Zinc; catalytic Ref.17
Metal binding961Zinc; catalytic
Metal binding1191Zinc; catalytic
Binding site621Activator
Binding site671Activator
Binding site921Activator

Amino acid modifications

Modified residue21N-acetylserine Ref.8

Natural variations

Natural variant181K → E in Jogjakarta. Ref.113
VAR_001380
Natural variant921Q → P in OPTB3; in Czechoslovakia. Ref.118 Ref.119
VAR_001381
Natural variant941H → Y in OPTB3; partial loss of activity. Ref.119
VAR_021009
Natural variant1071H → Y in OPTB3; frequent mutation. Ref.115 Ref.116 Ref.117 Ref.119
VAR_001382
Natural variant1441G → R in OPTB3; complete loss of activity. Ref.119
VAR_021010
Natural variant2361P → H in Melbourne. Ref.114
VAR_001383
Natural variant2521N → D.
Corresponds to variant rs2228063 [ dbSNP | Ensembl ].
VAR_001384

Experimental info

Mutagenesis51W → A: Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with W-64. Ref.89
Mutagenesis71Y → F: Enhanced activity. Ref.57 Ref.83
Mutagenesis71Y → H: Reduced proton transfer rate. Ref.57 Ref.83
Mutagenesis621N → A: Reduced activity. Ref.64 Ref.83 Ref.92
Mutagenesis621N → D: Strongly reduced activity. Ref.64 Ref.83 Ref.92
Mutagenesis621N → H: Reduced proton transfer; when associated with A-64. Ref.64 Ref.83 Ref.92
Mutagenesis621N → L: Reduced activity. Ref.64 Ref.83 Ref.92
Mutagenesis621N → T: Reduced activity. Ref.64 Ref.83 Ref.92
Mutagenesis621N → V: Reduced activity. Ref.64 Ref.83 Ref.92
Mutagenesis641H → A: Reduced CO(2) hydrase activity, rescued by 4-methylimidazole (4-MI). Reduced proton transfer; when associated with H-62. Enhanced proton transfer; when associated with H-67. Enhanced proton transfer capacity; when associated with H-99. Ref.53 Ref.64 Ref.68 Ref.89
Mutagenesis641H → G: Impaired activity, not rescued by 4-methylimidazole (4-MI). Ref.53 Ref.64 Ref.68 Ref.89
Mutagenesis641H → W: Impaired activity, rescued by 4-methylimidazole (4-MI). Impaired activity, not rescued by 4-methylimidazole (4-MI); when associated with A-5. Ref.53 Ref.64 Ref.68 Ref.89
Mutagenesis651A → F: Reduced activity. Ref.104
Mutagenesis651A → H, L or S: Normal activity. Ref.104
Mutagenesis671N → H: Enhanced proton transfer; when associated with A-64. Ref.64 Ref.83 Ref.104
Mutagenesis671N → L: Reduced activity. Ref.64 Ref.83 Ref.104
Mutagenesis671N → Q: Normal activity. Ref.64 Ref.83 Ref.104
Mutagenesis941H → C, D, E, N or Q: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities, impaired stability of zinc binding. Ref.26 Ref.47
Mutagenesis1061E → A or Q: Strongly reduced CO(2) hydrase activity. Ref.34 Ref.36
Mutagenesis1061E → D: Normal CO(2) hydrase activity. Ref.34 Ref.36
Mutagenesis1171E → Q: Strongly reduced activity and sulfonamide affinity. Ref.43
Mutagenesis1191H → D, N or Q: Reduced activity. Ref.47
Mutagenesis1191H → E: Strongly reduced activity. Ref.47
Mutagenesis1211V → A, G, I, L or S: Reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. Ref.22
Mutagenesis1211V → K or R: Strongly reduced CO(2) hydrase and p-nitrophenyl acetate esterase activities. Ref.22
Mutagenesis1421V → F or Y: Strongly impaired activity. Ref.21
Mutagenesis1421V → G: Weakly impaired activity. Ref.21
Mutagenesis1421V → H: Impaired activity. Ref.21
Mutagenesis1971L → A: Reduced CO(2) hydrase activity. Ref.27
Mutagenesis1971L → E, H or R: Strongly reduced CO(2) hydrase activity. Ref.27
Mutagenesis1971L → F: Normal activity. Ref.27
Mutagenesis1981T → A, C, H or P: Strongly reduced activity. Ref.28 Ref.31 Ref.34 Ref.42 Ref.56
Mutagenesis1981T → D or E: Strongly reduced activity, but enhanced zinc affinity. Ref.28 Ref.31 Ref.34 Ref.42 Ref.56
Mutagenesis1981T → S or V: Reduced activity. Ref.28 Ref.31 Ref.34 Ref.42 Ref.56
Mutagenesis1991T → H: Higher affinity for bicarbonate. Enhanced proton transfer capacity; when associated with A-64. Ref.20 Ref.33 Ref.68
Mutagenesis1991T → S: Enhanced p-nitrophenyl acetate esterase activity, but normal CO(2) hydrase activity. Ref.20 Ref.33 Ref.68
Mutagenesis2011P → A: Normal CO(2) hydrase activity, but impaired stability. Ref.29
Sequence conflict179 – 1802DP → AA in AAH11949. Ref.6

Secondary structure

.......................................................... 260
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00918 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2EC2BB7548F10558

FASTA26029,246
        10         20         30         40         50         60 
MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL 

        70         80         90        100        110        120 
NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL 

       130        140        150        160        170        180 
VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP 

       190        200        210        220        230        240 
RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM 

       250        260 
VDNWRPAQPL KNRQIKASFK 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of human liver carbonic anhydrase II cDNA."
Montgomery J.C., Venta P.J., Tashian R.E., Hewett-Emmett D.
Nucleic Acids Res. 15:4687-4687(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II."
Murakami H., Marelich G.P., Grubb J.H., Kyle J.W., Sly W.S.
Genomics 1:159-166(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Urinary bladder.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[7]"Human carbonic anhydrases. XII. The complete primary structure of the C isozyme."
Lin K.-T.D., Deutsch H.F.
J. Biol. Chem. 249:2329-2337(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-260.
[8]"Primary structure of human carbonic anhydrase C."
Henderson L.E., Henriksson D., Nyman P.O.
J. Biol. Chem. 251:5457-5463(1976) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-260.
[9]"Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements."
Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E.
Biochim. Biophys. Acta 826:195-201(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
[10]"Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter."
Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.
Biochemistry 42:12321-12329(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC4A4.
[11]"Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase II and PKA."
Loiselle F.B., Morgan P.E., Alvarez B.V., Casey J.R.
Am. J. Physiol. 286:C1423-C1433(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC4A7.
[12]"Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal tubule cells."
Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I., Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.
J. Physiol. (Lond.) 559:55-65(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC4A4.
[13]"Metabolon disruption: a mechanism that regulates bicarbonate transport."
Alvarez B.V., Vilas G.L., Casey J.R.
EMBO J. 24:2499-2511(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SLC26A6, SUBCELLULAR LOCATION.
[14]"Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[15]"Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Crystal structure of human carbonic anhydrase C."
Liljas A., Kannan K.K., Bergsten P.-C., Waara I., Fridborg K., Strandberg B., Carlbom U., Jaerup L., Loevgren S., Petef M.
Nature New Biol. 235:131-137(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[18]"Refined structure of human carbonic anhydrase II at 2.0-A resolution."
Eriksson A.E., Jones T.A., Liljas A.
Proteins 4:274-282(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC ION.
[19]"Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN-ion to the zinc at high pH."
Eriksson A.E., Kylsten P.M., Jones T.A., Liljas A.
Proteins 4:283-293(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
[20]"Conformational mobility of His-64 in the Thr-200TO: human carbonic anhydrase II."
Krebs J.F., Fierke C.A., Alexander R.S., Christianson D.W.
Biochemistry 30:9153-9160(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT SER-199 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-199, BIOPHYSICOCHEMICAL PROPERTIES.
[21]"Engineering the hydrophobic pocket of carbonic anhydrase II."
Alexander R.S., Nair S.K., Christianson D.W.
Biochemistry 30:11064-11072(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS PHE-142; TYR-142 AND HIS-142 IN COMPLEX WITH INHIBITORS, MUTAGENESIS OF VAL-142.
[22]"Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121."
Nair S.K., Calderone T.L., Christianson D.W., Fierke C.A.
J. Biol. Chem. 266:17320-17325(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ALA-121, MUTAGENESIS OF VAL-121, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[23]"Crystallographic studies of the binding of protonated and unprotonated inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate anions."
Mangani S., Haakansson K.
Eur. J. Biochem. 210:867-871(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS, ENZYME REGULATION.
[24]"Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes."
Haakansson K., Carlsson M., Svensson L.A., Liljas A.
J. Mol. Biol. 227:1192-1204(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
[25]"Structure of cobalt carbonic anhydrase complexed with bicarbonate."
Haakansson K., Wehnert A.
J. Mol. Biol. 228:1212-1218(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH COBALT ION AND BICARBONATE.
[26]"Engineering the zinc binding site of human carbonic anhydrase II: structure of the His-94-->Cys apoenzyme in a new crystalline form."
Alexander R.S., Kiefer L.L., Fierke C.A., Christianson D.W.
Biochemistry 32:1510-1518(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT CYS-94 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF HIS-94.
[27]"Structural consequences of hydrophilic amino acid substitutions in the hydrophobic pocket of human carbonic anhydrase II."
Nair S.K., Christianson D.W.
Biochemistry 32:4506-4514(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT ALA-197; GLU-197; HIS-197 AND ARG-197, MUTAGENESIS OF LEU-197.
[28]"Structure of an engineered His3Cys zinc binding site in human carbonic anhydrase II."
Ippolito J.A., Christianson D.W.
Biochemistry 32:9901-9905(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT CYS-198 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-198.
[29]"Structure and energetics of a non-proline cis-peptidyl linkage in a proline-202-->alanine carbonic anhydrase II variant."
Tweedy N.B., Nair S.K., Paterno S.A., Fierke C.A., Christianson D.W.
Biochemistry 32:10944-10949(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-201 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF PRO-201.
[30]"The structure of human carbonic anhydrase II in complex with bromide and azide."
Joensson B.M., Haakansson K., Liljas A.
FEBS Lett. 322:186-190(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC ION AND INHIBITORS.
[31]"Structural and functional importance of a conserved hydrogen bond network in human carbonic anhydrase II."
Krebs J.F., Ippolito J.A., Christianson D.W., Fierke C.A.
J. Biol. Chem. 268:27458-27466(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT VAL-198 IN COMPLEX WITH ZINC ION AND INHIBITORS, MUTAGENESIS OF THR-198, BIOPHYSICOCHEMICAL PROPERTIES.
[32]"Crystal structure of the complex between human carbonic anhydrase II and the aromatic inhibitor 1,2,4-triazole."
Mangani S., Liljas A.
J. Mol. Biol. 232:9-14(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND ZINC ION.
[33]"Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and its complex with the substrate, HCO3-."
Xue Y., Vidgren J., Svensson L.A., Liljas A., Jonsson B.H., Lindskog S.
Proteins 15:80-87(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT HIS-199 IN COMPLEX WITH BICARBONATE AND ZINC ION, MUTAGENESIS OF THR-199.
[34]"Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond network in human carbonic anhydrase II."
Xue Y., Liljas A., Jonsson B.H., Lindskog S.
Proteins 17:93-106(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANTS IN COMPLEX WITH BICARBONATE AND ZINC ION, MUTAGENESIS OF GLU-106 AND THR-198.
[35]"X-ray analysis of metal-substituted human carbonic anhydrase II derivatives."
Haakansson K., Wehnert A., Liljas A.
Acta Crystallogr. D 50:93-100(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COBALT; COPPER; NICKEL AND MANGANESE IONS.
[36]"Wild-type and E106Q mutant carbonic anhydrase complexed with acetate."
Haakansson K., Briand C., Zaitsev V., Xue Y., Liljas A.
Acta Crystallogr. D 50:101-104(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) MUTANT GLN-106 IN COMPLEX WITH THE INHIBITOR ACETATE, MUTAGENESIS OF GLU-106.
[37]"Structural consequences of redesigning a protein-zinc binding site."
Ippolito J.A., Christianson D.W.
Biochemistry 33:15241-15249(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-259 OF MUTANTS ALA-94; CYS-94; CYS-96; CYS-119 AND ASP-119 IN COMPLEX WITH ZINC ION.
[38]"The structure of a complex between carbonic anhydrase II and a new inhibitor, trifluoromethane sulphonamide."
Haakansson K., Liljas A.
FEBS Lett. 350:319-322(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR TRIFLUOROMETHANE SULPHONAMIDE.
[39]"Positions of His-64 and a bound water in human carbonic anhydrase II upon binding three structurally related inhibitors."
Smith G.M., Alexander R.S., Christianson D.W., McKeever B.M., Ponticello G.S., Springer J.P., Randall W.C., Baldwin J.J., Habecker C.N.
Protein Sci. 3:118-125(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[40]"Structural basis of inhibitor affinity to variants of human carbonic anhydrase II."
Nair S.K., Krebs J.F., Christianson D.W., Fierke C.A.
Biochemistry 34:3981-3989(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS ARG-197; ASP-197 AND PHE-197 IN COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE.
[41]"Secondary interactions significantly removed from the sulfonamide binding pocket of carbonic anhydrase II influence inhibitor binding constants."
Boriack P.A., Christianson D.W., Kingery-Wood J., Whitesides G.M.
J. Med. Chem. 38:2286-2291(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[42]"Structure-assisted redesign of a protein-zinc-binding site with femtomolar affinity."
Ippolito J.A., Baird T.T. Jr., McGee S.A., Christianson D.W., Fierke C.A.
Proc. Natl. Acad. Sci. U.S.A. 92:5017-5021(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANTS ASP-198; GLU-198 AND HIS-198 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF THR-198, BIOPHYSICOCHEMICAL PROPERTIES.
[43]"Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically diminishes catalysis and enhances metal equilibration kinetics in carbonic anhydrase II."
Huang C.C., Lesburg C.A., Kiefer L.L., Fierke C.A., Christianson D.W.
Biochemistry 35:3439-3446(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF THE MUTANT GLN-117 IN COMPLEX WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, MUTAGENESIS OF GLU-117.
[44]"X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis."
Scolnick L.R., Christianson D.W.
Biochemistry 35:16429-16434(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS GLY-65; HIS-65; LEU-65; PHE-65; SER-65 AND THR-65 IN COMPLEX WITH ZINC ION.
[45]"Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-naphthalene sulfonamide to human carbonic anhydrase II. Implications for the development of a zinc biosensor."
Nair S.K., Elbaum D., Christianson D.W.
J. Biol. Chem. 271:1003-1007(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR DANSYLAMIDE.
[46]"Carbonic anhydrase activators: X-ray crystallographic and spectroscopic investigations for the interaction of isozymes I and II with histamine."
Briganti F., Mangani S., Orioli P., Scozzafava A., Vernaglione G., Supuran C.T.
Biochemistry 36:10384-10392(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH THE ACTIVATOR HISTAMINE, ENZYME REGULATION.
[47]"Histidine --> carboxamide ligand substitutions in the zinc binding site of carbonic anhydrase II alter metal coordination geometry but retain catalytic activity."
Lesburg C.A., Huang C., Christianson D.W., Fierke C.A.
Biochemistry 36:15780-15791(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS ASN-94; ASN-119 AND GLN-119 IN COMPLEX WITH ZINC ION, MUTAGENESIS OF HIS-94 AND HIS-119, BIOPHYSICOCHEMICAL PROPERTIES.
[48]"Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination."
Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A., Dean T., Laipis P., Silverman D.N., Christianson D.W.
Protein Sci. 7:556-563(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR BRINZOLAMIDE.
[49]"Structural analysis of inhibitor binding to human carbonic anhydrase II."
Boriack-Sjodin P.A., Zeitlin S., Chen H.H., Crenshaw L., Gross S., Dantanarayana A., Delgado P., May J.A., Dean T., Christianson D.W.
Protein Sci. 7:2483-2489(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SULFONAMIDE INHIBITORS AND ZINC ION.
[50]"Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking the physiological reaction?"
Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T.
J. Biol. Inorg. Chem. 4:528-536(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CYANAMIDE AND SUBSTRATE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[51]"Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II suggested by cryogenic X-ray diffraction."
Guerri A., Briganti F., Scozzafava A., Supuran C.T., Mangani S.
Biochemistry 39:12391-12397(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CYANAMIDE.
[52]"Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II."
Cox J.D., Hunt J.A., Compher K.M., Fierke C.A., Christianson D.W.
Biochemistry 39:13687-13694(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANTS ILE-93/MET-95/VAL-97 AND SER-93/LEU-95/MET-97 IN COMPLEX WITH COBALT; COPPER AND ZINC IONS.
[53]"Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II."
Duda D., Tu C., Qian M., Laipis P., Agbandje-McKenna M., Silverman D.N., McKenna R.
Biochemistry 40:1741-1748(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH 4-METHYLIMIDAZOLE, MUTAGENESIS OF HIS-64.
[54]"Fluoroaromatic-fluoroaromatic interactions between inhibitors bound in the crystal lattice of human carbonic anhydrase II."
Kim C.Y., Chandra P.P., Jain A., Christianson D.W.
J. Am. Chem. Soc. 123:9620-9627(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT VAL-130 IN COMPLEX WITH FLUOROAROMATIC INHIBITORS.
[55]"Crystal structure of human carbonic anhydrase II complexed with an anti-convulsant sugar sulphamate."
Recacha R., Costanzo M.J., Maryanoff B.E., Chattopadhyay D.
Biochem. J. 361:437-441(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR SUGAR SULFAMATE RWJ-37497, ENZYME REGULATION.
[56]"Organization of an efficient carbonic anhydrase: implications for the mechanism based on structure-function studies of a T199P/C206S mutant."
Huang S., Sjoeblom B., Sauer-Eriksson A.E., Jonsson B.H.
Biochemistry 41:7628-7635(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF THE MUTANT PRO-198/SER-205 IN COMPLEX WITH BICARBONATE AND INHIBITORS, MUTAGENESIS OF THR-198.
[57]"Kinetic analysis of multiple proton shuttles in the active site of human carbonic anhydrase."
Tu C., Qian M., An H., Wadhwa N.R., Duda D., Yoshioka C., Pathak Y., McKenna R., Laipis P.J., Silverman D.N.
J. Biol. Chem. 277:38870-38876(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF THE MUTANT HIS-7, MUTAGENESIS OF TYR-7.
[58]"Structural aspects of isozyme selectivity in the binding of inhibitors to carbonic anhydrases II and IV."
Kim C.Y., Whittington D.A., Chang J.S., Liao J., May J.A., Christianson D.W.
J. Med. Chem. 45:888-893(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH INHIBITORS, FUNCTION.
[59]"Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation."
Grueneberg S., Stubbs M.T., Klebe G.
J. Med. Chem. 45:3588-3602(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[60]"Combinatorial computational method gives new picomolar ligands for a known enzyme."
Grzybowski B.A., Ishchenko A.V., Kim C.Y., Topalov G., Chapman R., Christianson D.W., Whitesides G.M., Shakhnovich E.I.
Proc. Natl. Acad. Sci. U.S.A. 99:1270-1273(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[61]"The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer."
Duda D., Govindasamy L., Agbandje-McKenna M., Tu C., Silverman D.N., McKenna R.
Acta Crystallogr. D 59:93-104(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH THE INHIBITOR 4-METHYLIMIDAZOLE AND ZINC ION.
[62]"Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective celecoxib: new pharmacological opportunities due to related binding site recognition."
Weber A., Casini A., Heine A., Kuhn D., Supuran C.T., Scozzafava A., Klebe G.
J. Med. Chem. 47:550-557(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[63]"Crystal structure of human carbonic anhydrase II at 1.95 A resolution in complex with 667-coumate, a novel anti-cancer agent."
Lloyd M.D., Pederick R.L., Natesh R., Woo L.W., Purohit A., Reed M.J., Acharya K.R., Potter B.V.
Biochem. J. 385:715-720(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THE ANTI-CANCER AGENT 667-COUMATE.
[64]"Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II."
Fisher Z., Hernandez Prada J.A., Tu C., Duda D., Yoshioka C., An H., Govindasamy L., Silverman D.N., McKenna R.
Biochemistry 44:1097-1105(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), MUTAGENESIS OF ASN-62; HIS-64 AND ASN-67, BIOPHYSICOCHEMICAL PROPERTIES.
[65]"First crystal structures of human carbonic anhydrase II in complex with dual aromatase-steroid sulfatase inhibitors."
Lloyd M.D., Thiyagarajan N., Ho Y.T., Woo L.W., Sutcliffe O.B., Purohit A., Reed M.J., Acharya K.R., Potter B.V.
Biochemistry 44:6858-6866(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH DUAL AROMATASE-STEROID SULFATASE INHIBITORS.
[66]"Carbonic anhydrase activators: X-ray crystal structure of the adduct of human isozyme II with L-histidine as a platform for the design of stronger activators."
Temperini C., Scozzafava A., Puccetti L., Supuran C.T.
Bioorg. Med. Chem. Lett. 15:5136-5141(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACTIVATOR L-HISTIDINE, ENZYME REGULATION.
[67]"Carbonic anhydrase inhibitors: stacking with Phe131 determines active site binding region of inhibitors as exemplified by the X-ray crystal structure of a membrane-impermeant antitumor sulfonamide complexed with isozyme II."
Menchise V., De Simone G., Alterio V., Di Fiore A., Pedone C., Scozzafava A., Supuran C.T.
J. Med. Chem. 48:5721-5727(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[68]"Proton transfer in a Thr200His mutant of human carbonic anhydrase II."
Bhatt D., Tu C., Fisher S.Z., Hernandez Prada J.A., McKenna R., Silverman D.N.
Proteins 61:239-245(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), MUTAGENESIS OF HIS-64 AND THR-199.
[69]"Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II."
Budayova-Spano M., Fisher S.Z., Dauvergne M.T., Agbandje-McKenna M., Silverman D.N., Myles D.A., McKenna R.
Acta Crystallogr. F 62:6-9(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
[70]"X-ray crystallographic studies reveal that the incorporation of spacer groups in carbonic anhydrase inhibitors causes alternate binding modes."
Fisher S.Z., Govindasamy L., Boyle N., Agbandje-McKenna M., Silverman D.N., Blackburn G.M., McKenna R.
Acta Crystallogr. F 62:618-622(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[71]"Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II 'selective' inhibitor celecoxib."
Di Fiore A., Pedone C., D'Ambrosio K., Scozzafava A., De Simone G., Supuran C.T.
Bioorg. Med. Chem. Lett. 16:437-442(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS VALDECOXIB AND CELECOXIB, ENZYME REGULATION.
[72]"N-hydroxyurea -- a versatile zinc binding function in the design of metalloenzyme inhibitors."
Temperini C., Innocenti A., Scozzafava A., Supuran C.T.
Bioorg. Med. Chem. Lett. 16:4316-4320(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH N-HYDROXYUREA, ENZYME REGULATION.
[73]"Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of 5-amino-1,3,4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide to human isoform II."
Menchise V., De Simone G., Di Fiore A., Scozzafava A., Supuran C.T.
Bioorg. Med. Chem. Lett. 16:6204-6208(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[74]"Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II: engineering proton-transfer processes within the active site of an enzyme."
Temperini C., Scozzafava A., Vullo D., Supuran C.T.
Chemistry 12:7057-7066(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH L- AND D-HISTIDINE, ENZYME REGULATION.
[75]"Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with 'two-prong' inhibitors reveal the molecular basis of high affinity."
Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B., Mallik S., Srivastava D.K., Christianson D.W.
J. Am. Chem. Soc. 128:3011-3018(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) IN COMPLEX WITH TWO-PRONG INHIBITORS.
[76]"Carbonic anhydrase inhibitors: X-ray and molecular modeling study for the interaction of a fluorescent antitumor sulfonamide with isozyme II and IX."
Alterio V., Vitale R.M., Monti S.M., Pedone C., Scozzafava A., Cecchi A., De Simone G., Supuran C.T.
J. Am. Chem. Soc. 128:8329-8335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[77]"Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II: stereospecific recognition within the active site of an enzyme and its consequences for the drug design."
Temperini C., Scozzafava A., Vullo D., Supuran C.T.
J. Med. Chem. 49:3019-3027(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH L- AND D-PHENYLALANINE, ENZYME REGULATION.
[78]"Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides incorporating disulfide bonds that target the tumor-associated isoform IX."
De Simone G., Vitale R.M., Di Fiore A., Pedone C., Scozzafava A., Montero J.-L., Winum J.-Y., Supuran C.T.
J. Med. Chem. 49:5544-5551(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[79]"Carbonic anhydrase inhibitors: clash with Ala65 as a means for designing inhibitors with low affinity for the ubiquitous isozyme II, exemplified by the crystal structure of the topiramate sulfamide analogue."
Winum J.Y., Temperini C., El Cheikh K., Innocenti A., Vullo D., Ciattini S., Montero J.-L., Scozzafava A., Supuran C.T.
J. Med. Chem. 49:7024-7031(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[80]"2-substituted estradiol bis-sulfamates, multitargeted antitumor agents: synthesis, in vitro SAR, protein crystallography, and in vivo activity."
Leese M.P., Leblond B., Smith A., Newman S.P., Di Fiore A., De Simone G., Supuran C.T., Purohit A., Reed M.J., Potter B.V.
J. Med. Chem. 49:7683-7696(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[81]"Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SACCHARIN, ENZYME REGULATION.
[82]"Atomic crystal and molecular dynamics simulation structures of human carbonic anhydrase II: insights into the proton transfer mechanism."
Fisher S.Z., Maupin C.M., Budayova-Spano M., Govindasamy L., Tu C., Agbandje-McKenna M., Silverman D.N., Voth G.A., McKenna R.
Biochemistry 46:2930-2937(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
[83]"Speeding up proton transfer in a fast enzyme: kinetic and crystallographic studies on the effect of hydrophobic amino acid substitutions in the active site of human carbonic anhydrase II."
Fisher S.Z., Tu C., Bhatt D., Govindasamy L., Agbandje-McKenna M., McKenna R., Silverman D.N.
Biochemistry 46:3803-3813(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), MUTAGENESIS OF TYR-7; ASN-62 AND ASN-67, BIOPHYSICOCHEMICAL PROPERTIES.
[84]"Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV."
Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.
Bioorg. Med. Chem. Lett. 17:628-635(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ACTIVATOR L-ADRENALINE, ENZYME REGULATION.
[85]"Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-sulfanilamide derivative to human isoform II and its consequences for the drug design of enzyme inhibitors incorporating sugar moieties."
Di Fiore A., Scozzafava A., Winum J.-Y., Montero J.-L., Pedone C., Supuran C.T., De Simone G.
Bioorg. Med. Chem. Lett. 17:1726-1731(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
[86]"Carbonic anhydrase inhibitors: the X-ray crystal structure of the adduct of N-hydroxysulfamide with isozyme II explains why this new zinc binding function is effective in the design of potent inhibitors."
Temperini C., Winum J.Y., Montero J.L., Scozzafava A., Supuran C.T.
Bioorg. Med. Chem. Lett. 17:2795-2801(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR N-HYDROXYSULFAMIDE.
[87]"Carbonic anhydrase inhibitors: inhibition of human, bacterial, and archaeal isozymes with benzene-1,3-disulfonamides -- solution and crystallographic studies."
Alterio V., De Simone G., Monti S.M., Scozzafava A., Supuran C.T.
Bioorg. Med. Chem. Lett. 17:4201-4207(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[88]"Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug sulthiame with twelve mammalian isoforms: kinetic and X-ray crystallographic studies."
Temperini C., Innocenti A., Mastrolorenzo A., Scozzafava A., Supuran C.T.
Bioorg. Med. Chem. Lett. 17:4866-4872(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[89]"Location of binding sites in small molecule rescue of human carbonic anhydrase II."
Bhatt D., Fisher S.Z., Tu C., McKenna R., Silverman D.N.
Biophys. J. 92:562-570(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH 4-METHYLIMIDAZOLE, MUTAGENESIS OF TRP-5 AND HIS-64.
[90]"Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II."
Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S., Kooren J., Mallik S., Christianson D.W.
J. Am. Chem. Soc. 129:5528-5537(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[91]"Inhibition of carbonic anhydrase II by thioxolone: a mechanistic and structural study."
Barrese A.A. III, Genis C., Fisher S.Z., Orwenyo J.N., Kumara M.T., Dutta S.K., Phillips E., Kiddle J.J., Tu C., Silverman D.N., Govindasamy L., Agbandje-McKenna M., McKenna R., Tripp B.C.
Biochemistry 47:3174-3184(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITOR THIOXOLONE, ENZYME REGULATION.
[92]"Role of hydrophilic residues in proton transfer during catalysis by human carbonic anhydrase II."
Zheng J., Avvaru B.S., Tu C., McKenna R., Silverman D.N.
Biochemistry 47:12028-12036(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANTS, MUTAGENESIS OF ASN-62, BIOPHYSICOCHEMICAL PROPERTIES.
[93]"Carbonic anhydrase inhibitors. Interaction of 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies."
Guezel O., Temperini C., Innocenti A., Scozzafava A., Salman A., Supuran C.T.
Bioorg. Med. Chem. Lett. 18:152-158(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[94]"Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: kinetic and X-ray crystallographic studies."
Temperini C., Cecchi A., Boyle N.A., Scozzafava A., Cabeza J.E., Wentworth P. Jr., Blackburn G.M., Supuran C.T.
Bioorg. Med. Chem. Lett. 18:999-1005(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[95]"Carbonic anhydrase inhibitors. Interaction of indapamide and related diuretics with 12 mammalian isozymes and X-ray crystallographic studies for the indapamide-isozyme II adduct."
Temperini C., Cecchi A., Scozzafava A., Supuran C.T.
Bioorg. Med. Chem. Lett. 18:2567-2573(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[96]"Carbonic anhydrase inhibitors: the X-ray crystal structure of ethoxzolamide complexed to human isoform II reveals the importance of thr200 and gln92 for obtaining tight-binding inhibitors."
Di Fiore A., Pedone C., Antel J., Waldeck H., Witte A., Wurl M., Scozzafava A., Supuran C.T., De Simone G.
Bioorg. Med. Chem. Lett. 18:2669-2674(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[97]"Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate EMD 486019 with twelve mammalian carbonic anhydrase isoforms: Kinetic and X-ray crystallographic studies."
Temperini C., Innocenti A., Scozzafava A., Supuran C.T.
Bioorg. Med. Chem. Lett. 18:4282-4286(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[98]"Carbonic anhydrase inhibitors: binding of indanesulfonamides to the human isoform II."
D'Ambrosio K., Masereel B., Thiry A., Scozzafava A., Supuran C.T., De Simone G.
ChemMedChem 3:473-477(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH INHIBITORS INDANESULFONAMIDES.
[99]"Structure of a (129)Xe-cryptophane biosensor complexed with human carbonic anhydrase II."
Aaron J.A., Chambers J.M., Jude K.M., Di Costanzo L., Dmochowski I.J., Christianson D.W.
J. Am. Chem. Soc. 130:6942-6943(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH (129)XE-CRYPTOPHANE BIOSENSOR.
[100]"Entrapment of carbon dioxide in the active site of carbonic anhydrase II."
Domsic J.F., Avvaru B.S., Kim C.U., Gruner S.M., Agbandje-McKenna M., Silverman D.N., McKenna R.
J. Biol. Chem. 283:30766-30771(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH CO2.
[101]"Structure-activity relationships of C-17 cyano-substituted estratrienes as anticancer agents."
Leese M.P., Jourdan F.L., Gaukroger K., Mahon M.F., Newman S.P., Foster P.A., Stengel C., Regis-Lydi S., Ferrandis E., Di Fiore A., De Simone G., Supuran C.T., Purohit A., Reed M.J., Potter B.V.
J. Med. Chem. 51:1295-1308(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[102]"Carbonic anhydrase inhibitors: bioreductive nitro-containing sulfonamides with selectivity for targeting the tumor associated isoforms IX and XII."
D'Ambrosio K., Vitale R.-M., Dogne J.-M., Masereel B., Innocenti A., Scozzafava A., De Simone G., Supuran C.T.
J. Med. Chem. 51:3230-3237(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[103]"Anticancer steroid sulfatase inhibitors: synthesis of a potent fluorinated second-generation agent, in vitro and in vivo activities, molecular modeling, and protein crystallography."
Woo L.W.L., Fischer D.S., Sharland C.M., Trusselle M., Foster P.A., Chander S.K., Di Fiore A., Supuran C.T., De Simone G., Purohit A., Reed M.J., Potter B.V.L.
Mol. Cancer Ther. 7:2435-2444(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[104]"Design of a carbonic anhydrase IX active-site mimic to screen inhibitors for possible anticancer properties."
Genis C., Sippel K.H., Case N., Cao W., Avvaru B.S., Tartaglia L.J., Govindasamy L., Tu C., Agbandje-McKenna M., Silverman D.N., Rosser C.J., McKenna R.
Biochemistry 48:1322-1331(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ENZYME REGULATION, MUTAGENESIS OF ALA-65 AND ASN-67.
[105]"Apo-human carbonic anhydrase II revisited: implications of the loss of a metal in protein structure, stability, and solvent network."
Avvaru B.S., Busby S.A., Chalmers M.J., Griffin P.R., Venkatakrishnan B., Agbandje-McKenna M., Silverman D.N., McKenna R.
Biochemistry 48:7365-7372(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) FREE AND IN COMPLEX WITH ZINC ION, COFACTOR.
[106]"A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITOR THIABENDAZOLE-5-SULFONAMIDE, ENZYME REGULATION.
[107]"Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-260 IN COMPLEX WITH COUMARIN INHIBITORS, ENZYME REGULATION.
[108]"Carbonic anhydrase inhibitors. Comparison of chlorthalidone and indapamide X-ray crystal structures in adducts with isozyme II: when three water molecules and the keto-enol tautomerism make the difference."
Temperini C., Cecchi A., Scozzafava A., Supuran C.T.
J. Med. Chem. 52:322-328(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[109]"Carbonic anhydrase inhibitors. Comparison of aliphatic sulfamate/bis-sulfamate adducts with isozymes II and IX as a platform for designing tight-binding, more isoform-selective inhibitors."
Vitale R.M., Alterio V., Innocenti A., Winum J.-Y., Monti S.M., De Simone G., Supuran C.T.
J. Med. Chem. 52:5990-5998(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
[110]"S-glycosyl primary sulfonamides--a new structural class for selective inhibition of cancer-associated carbonic anhydrases."
Lopez M., Paul B., Hofmann A., Morizzi J., Wu Q.K., Charman S.A., Innocenti A., Vullo D., Supuran C.T., Poulsen S.-A.
J. Med. Chem. 52:6421-6432(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS.
[111]"Dissecting the inhibition mechanism of cytosolic versus transmembrane carbonic anhydrases by ESR."
Ciani L., Cecchi A., Temperini C., Supuran C.T., Ristori S.
J. Phys. Chem. B 113:13998-14005(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS, ENZYME REGULATION.
[112]"Structural study of X-ray induced activation of carbonic anhydrase."
Sjoeblom B., Polentarutti M., Djinovic-Carugo K.
Proc. Natl. Acad. Sci. U.S.A. 106:10609-10613(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, ENZYME REGULATION.
[113]"Chemical and enzymological characterization of an Indonesian variant of human erythrocyte carbonic anhydrase II, CAII Jogjakarta (17 Lys leads to Glu)."
Jones G.L., Sofro A.S.M., Shaw D.C.
Biochem. Genet. 20:979-1000(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JOGJAKARTA GLU-18.
[114]"A chemical and enzymological comparison of the common major human erythrocyte carbonic anhydrase II, its minor component, and a new genetic variant, CA II Melbourne (237 Pro leads to His)."
Jones G.L., Shaw D.C.
Hum. Genet. 63:392-399(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MELBOURNE HIS-236.
[115]"Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His-->Tyr): complete structure of the normal human CA II gene."
Venta P.J., Welty R.J., Johnson T.M., Sly W.S., Tashian R.E.
Am. J. Hum. Genet. 49:1082-1090(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPTB3 TYR-107.
[116]"Molecular basis of human carbonic anhydrase II deficiency."
Roth D.E., Venta P.J., Tashian R.E., Sly W.S.
Proc. Natl. Acad. Sci. U.S.A. 89:1804-1808(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPTB3 TYR-107.
[117]"A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese patients with carbonic anhydrase II deficiency with central nervous system involvement."
Soda H., Yukizane S., Yoshida I., Koga Y., Aramaki S., Kato H.
Hum. Genet. 97:435-437(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPTB3 TYR-107.
[118]"Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis."
Hu P.Y., Lim E.J., Ciccolella J., Strisciuglio P., Sly W.S.
Hum. Mutat. 9:383-387(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPTB3 PRO-92.
[119]"Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation."
Shah G.N., Bonapace G., Hu P.Y., Strisciuglio P., Sly W.S.
Hum. Mutat. 24:272-272(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144, CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77181 expand/collapse EMBL AC list , M77176, M77177, M77178, M77179, M77180 Genomic DNA. Translation: AAA51909.1.
Y00339 mRNA. Translation: CAA68426.1.
X03251 Genomic DNA. Translation: CAA27012.1.
J03037 mRNA. Translation: AAA51908.1.
CR536526 mRNA. Translation: CAG38763.1.
CR541875 mRNA. Translation: CAG46673.1.
AK312978 mRNA. Translation: BAG35815.1.
CH471068 Genomic DNA. Translation: EAW87136.1.
BC011949 mRNA. Translation: AAH11949.1.
M36532 mRNA. Translation: AAA51911.1.
PIRCRHU2. A27175.
RefSeqNP_000058.1. NM_000067.2.
UniGeneHs.155097.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
12CAX-ray2.40A2-260[»]
1A42X-ray2.25A2-260[»]
1AM6X-ray2.00A2-260[»]
1AVNX-ray2.00A2-260[»]
1BCDX-ray1.90A2-260[»]
1BICX-ray1.90A2-260[»]
1BN1X-ray2.10A2-260[»]
1BN3X-ray2.20A2-260[»]
1BN4X-ray2.10A2-260[»]
1BNMX-ray2.60A2-260[»]
1BNNX-ray2.30A2-260[»]
1BNQX-ray2.40A2-260[»]
1BNTX-ray2.15A2-260[»]
1BNUX-ray2.15A2-260[»]
1BNVX-ray2.40A2-260[»]
1BNWX-ray2.25A2-260[»]
1BV3X-ray1.85A2-260[»]
1CA2X-ray2.00A2-260[»]
1CA3X-ray2.30A2-260[»]
1CAHX-ray1.88A2-260[»]
1CAIX-ray1.80A2-260[»]
1CAJX-ray1.90A2-260[»]
1CAKX-ray1.90A2-260[»]
1CALX-ray2.20A2-260[»]
1CAMX-ray1.70A2-260[»]
1CANX-ray1.90A2-260[»]
1CAOX-ray1.90A2-260[»]
1CAYX-ray2.10A2-260[»]
1CAZX-ray1.90A2-260[»]
1CCSX-ray2.35A2-260[»]
1CCTX-ray2.20A2-260[»]
1CCUX-ray2.25A2-260[»]
1CILX-ray1.60A2-260[»]
1CIMX-ray2.10A2-260[»]
1CINX-ray2.10A2-260[»]
1CNBX-ray2.35A2-260[»]
1CNCX-ray2.20A2-260[»]
1CNGX-ray1.90A2-260[»]
1CNHX-ray2.05A2-260[»]
1CNIX-ray1.80A2-260[»]
1CNJX-ray1.80A2-260[»]
1CNKX-ray2.15A2-260[»]
1CNWX-ray2.00A2-260[»]
1CNXX-ray1.90A2-260[»]
1CNYX-ray2.30A2-260[»]
1CRAX-ray1.90A2-260[»]
1CVAX-ray2.25A2-260[»]
1CVBX-ray2.40A2-260[»]
1CVCX-ray2.30A2-260[»]
1CVDX-ray2.20A2-258[»]
1CVEX-ray2.25A2-260[»]
1CVFX-ray2.25A2-260[»]
1CVHX-ray2.30A2-259[»]
1DCAX-ray2.20A2-260[»]
1DCBX-ray2.10A2-260[»]
1EOUX-ray2.10A2-260[»]
1F2WX-ray1.90A2-260[»]
1FQLX-ray2.00A2-260[»]
1FQMX-ray2.00A2-260[»]
1FQNX-ray2.00A2-260[»]
1FQRX-ray2.00A2-260[»]
1FR4X-ray1.60A2-260[»]
1FR7X-ray1.50A/B2-260[»]
1FSNX-ray2.00A/B2-260[»]
1FSQX-ray2.00A/B2-260[»]
1FSRX-ray2.00A/B2-260[»]
1G0EX-ray1.60A2-260[»]
1G0FX-ray1.60A2-260[»]
1G1DX-ray2.04A2-260[»]
1G3ZX-ray1.86A2-260[»]
1G45X-ray1.83A2-260[»]
1G46X-ray1.84A2-260[»]
1G48X-ray1.86A2-260[»]
1G4JX-ray1.84A2-260[»]
1G4OX-ray1.96A2-260[»]
1G52X-ray1.80A2-260[»]
1G53X-ray1.94A2-260[»]
1G54X-ray1.86A2-259[»]
1H4NX-ray2.00A2-260[»]
1H9NX-ray1.85A2-260[»]
1H9QX-ray2.20A2-260[»]
1HCAX-ray2.30A2-260[»]
1HEAX-ray2.00A2-260[»]
1HEBX-ray2.00A2-260[»]
1HECX-ray2.00A2-260[»]
1HEDX-ray2.00A2-260[»]
1HVAX-ray2.30A2-260[»]
1I8ZX-ray1.93A2-260[»]
1I90X-ray2.00A2-260[»]
1I91X-ray2.00A2-260[»]
1I9LX-ray1.93A2-260[»]
1I9MX-ray1.84A2-260[»]
1I9NX-ray1.86A2-260[»]
1I9OX-ray1.86A2-260[»]
1I9PX-ray1.92A2-260[»]
1I9QX-ray1.80A2-260[»]
1IF4X-ray1.93A2-260[»]
1IF5X-ray2.00A2-260[»]
1IF6X-ray2.09A2-260[»]
1IF7X-ray1.98A2-260[»]
1IF8X-ray1.94A2-260[»]
1IF9X-ray2.00A2-260[»]
1KWQX-ray2.60A2-260[»]
1KWRX-ray2.25A2-260[»]
1LG5X-ray1.75A2-260[»]
1LG6X-ray2.20A2-260[»]
1LGDX-ray1.90A2-260[»]
1LUGX-ray0.95A2-260[»]
1LZVX-ray2.30A2-260[»]
1MOOX-ray1.05A2-260[»]
1MUAX-ray1.70A2-260[»]
1OKLX-ray2.10A2-260[»]
1OKMX-ray2.20A2-260[»]
1OKNX-ray2.40A2-260[»]
1OQ5X-ray1.50A2-260[»]
1RAYX-ray1.80A2-260[»]
1RAZX-ray1.90A2-260[»]
1RZAX-ray1.90A2-260[»]
1RZBX-ray1.80A2-260[»]
1RZCX-ray1.90A2-260[»]
1RZDX-ray1.90A2-260[»]
1RZEX-ray1.90A2-260[»]
1T9NX-ray2.00A2-260[»]
1TB0X-ray2.00X2-260[»]
1TBTX-ray2.00X2-260[»]
1TE3X-ray2.00X2-260[»]
1TEQX-ray2.00X2-260[»]
1TEUX-ray2.00X2-260[»]
1TG3X-ray1.80A2-260[»]
1TG9X-ray1.90A2-260[»]
1TH9X-ray1.63A2-260[»]
1THKX-ray1.80A2-260[»]
1TTMX-ray1.95A2-260[»]
1UGAX-ray2.00A2-260[»]
1UGBX-ray2.00A2-260[»]
1UGCX-ray2.00A2-260[»]
1UGDX-ray2.00A2-260[»]
1UGEX-ray1.90A2-260[»]
1UGFX-ray2.00A2-260[»]
1UGGX-ray2.20A2-260[»]
1XEGX-ray1.81A2-260[»]
1XEVX-ray2.20A/B/C/D2-260[»]
1XPZX-ray2.02A2-260[»]
1XQ0X-ray1.76A2-260[»]
1YDAX-ray2.10A2-260[»]
1YDBX-ray1.90A2-260[»]
1YDCX-ray1.95A2-260[»]
1YDDX-ray2.10A2-260[»]
1YO0X-ray1.80A2-260[»]
1YO1X-ray1.70A2-260[»]
1YO2X-ray1.80A2-260[»]
1Z9YX-ray1.66A2-260[»]
1ZE8X-ray2.00A2-260[»]
1ZFKX-ray1.56A2-260[»]
1ZFQX-ray1.55A2-260[»]
1ZGEX-ray1.65A2-260[»]
1ZGFX-ray1.75A2-260[»]
1ZH9X-ray1.70A2-260[»]
1ZSAX-ray2.50A2-260[»]
1ZSBX-ray2.00A2-260[»]
1ZSCX-ray1.80A2-260[»]
2ABEX-ray2.00A2-260[»]
2AW1X-ray1.46A2-260[»]
2AX2X-ray1.50A2-260[»]
2CA2X-ray1.90A2-260[»]
2CBAX-ray1.54A2-260[»]
2CBBX-ray1.67A2-260[»]
2CBCX-ray1.88A2-260[»]
2CBDX-ray1.67A2-260[»]
2CBEX-ray1.82A2-260[»]
2EU2X-ray1.15A2-260[»]
2EU3X-ray1.60A2-260[»]
2EZ7X-ray2.00A2-260[»]
2F14X-ray1.71A2-260[»]
2FMGX-ray1.60A2-260[»]
2FMZX-ray1.60A2-260[»]
2FNKX-ray1.80A2-260[»]
2FNMX-ray1.80A2-260[»]
2FNNX-ray1.80A2-260[»]
2FOQX-ray1.25A2-260[»]
2FOSX-ray1.10A2-260[»]
2FOUX-ray0.99A2-260[»]
2FOVX-ray1.15A2-260[»]
2GD8X-ray1.46A2-260[»]
2GEHX-ray2.00A2-260[»]
2H15X-ray1.90A2-260[»]
2H4NX-ray1.90A2-260[»]
2HD6X-ray1.80A2-260[»]
2HKKX-ray1.90A2-260[»]
2HL4X-ray1.55A2-260[»]
2HNCX-ray1.55A2-260[»]
2HOCX-ray2.10A2-260[»]
2ILIX-ray1.05A2-260[»]
2NNGX-ray1.20A2-260[»]
2NNOX-ray1.01A2-260[»]
2NNSX-ray1.03A2-260[»]
2NNVX-ray1.10A2-260[»]
2NWOX-ray1.70A2-260[»]
2NWPX-ray1.80A2-260[»]
2NWYX-ray1.65A2-260[»]
2NWZX-ray1.80A2-260[»]
2NXRX-ray1.70A2-260[»]
2NXSX-ray1.80A2-260[»]
2NXTX-ray1.15A2-260[»]
2O4ZX-ray2.10A2-260[»]
2OSFX-ray1.60A2-260[»]
2OSMX-ray1.60A2-260[»]
2POUX-ray1.60A2-260[»]
2POVX-ray1.60A2-260[»]
2POWX-ray1.75A2-260[»]
2Q1BX-ray1.70A2-260[»]
2Q1QX-ray1.90A2-260[»]
2Q38X-ray1.95A2-260[»]
2QO8X-ray1.40A2-260[»]
2QOAX-ray1.60A2-260[»]
2QP6X-ray1.45A2-260[»]
2VVAX-ray1.56X2-260[»]
2VVBX-ray1.66X2-260[»]
2WD2X-ray1.49A2-260[»]
2WD3X-ray1.80A2-260[»]
2WEGX-ray1.10A2-260[»]
2WEHX-ray2.09A2-260[»]
2WEJX-ray1.45A2-260[»]
2WEOX-ray1.40A2-260[»]
2X7SX-ray1.64A2-260[»]
2X7TX-ray1.89A2-260[»]
2X7UX-ray2.12A2-260[»]
3B4FX-ray1.89A2-260[»]
3BETX-ray1.85A2-260[»]
3BL0X-ray1.90A2-260[»]
3BL1X-ray2.10A2-260[»]
3C7PX-ray1.70A2-260[»]
3CA2X-ray2.00A2-260[»]
3CAJX-ray1.80A2-260[»]
3CYUX-ray1.70A2-260[»]
3D8WX-ray1.70A2-260[»]
3D92X-ray1.10A2-260[»]
3D93X-ray1.10A2-260[»]
3D9ZX-ray1.65A2-260[»]
3DAZX-ray1.60A2-260[»]
3DBUX-ray1.70A2-260[»]
3DC3X-ray1.70A2-260[»]
3DC9X-ray1.60A2-260[»]
3DCCX-ray1.60A2-260[»]
3DCSX-ray1.80A2-260[»]
3DCWX-ray1.50A2-260[»]
3DD0X-ray1.48A2-260[»]
3DD8X-ray1.90A2-260[»]
3DV7X-ray1.70A2-260[»]
3DVBX-ray1.70A2-260[»]
3DVCX-ray1.60A2-260[»]
3DVDX-ray1.60A2-260[»]
3EFIX-ray1.75A2-260[»]
3EFTX-ray1.85A1-260[»]
3F4XX-ray1.90A2-260[»]
3F8EX-ray2.00A1-260[»]
3FFPX-ray1.81X1-260[»]
3GZ0X-ray1.26A2-260[»]
3HFPX-ray2.10A1-260[»]
3HKNX-ray1.80A1-260[»]
3HKQX-ray1.70A1-260[»]
3HKTX-ray2.36A1-260[»]
3HKUX-ray1.80A1-260[»]
3HLJX-ray1.44A1-260[»]
3HS4X-ray1.10A1-260[»]
3IBIX-ray1.93A2-260[»]
3IBLX-ray1.55A2-260[»]
3IBNX-ray2.20A2-260[»]
3IBUX-ray1.41A2-260[»]
3IEOX-ray2.00A1-260[»]
3IGPX-ray1.65A1-260[»]
3K2FX-ray1.98A1-260[»]
3K34X-ray0.90A1-260[»]
3K7KX-ray1.90A1-260[»]
3KIGX-ray1.39A1-260[»]
3KKXneutron diffraction2.00A1-260[»]
3KNEX-ray1.35A1-260[»]
3KOIX-ray1.64A1-260[»]
3KOKX-ray1.50A1-260[»]
3KONX-ray1.50A1-260[»]
3KS3X-ray0.90A1-260[»]
3KWAX-ray2.00A1-260[»]
3L14X-ray1.22A1-260[»]
3M04X-ray1.40A1-260[»]
3M14X-ray1.38A1-260[»]
3M1JX-ray1.80A1-260[»]
3M1KX-ray1.35A1-260[»]
3M1QX-ray1.69A1-260[»]
3M1WX-ray1.38A1-260[»]
3M2NX-ray1.65A1-260[»]
3M2XX-ray1.87A1-260[»]
3M2YX-ray1.17A1-260[»]
3M2ZX-ray1.70A1-260[»]
3M3XX-ray1.68A1-260[»]
3M40X-ray1.60A1-260[»]
3M5EX-ray1.70A1-260[»]
3M5SX-ray1.40A1-260[»]
3M5TX-ray1.95A1-260[»]
3M67X-ray1.80A1-260[»]
3M96X-ray1.40A1-260[»]
3M98X-ray1.50A1-260[»]
3MHCX-ray1.70A1-260[»]
3MHIX-ray1.70A1-260[»]
3MHLX-ray1.90A1-260[»]
3MHMX-ray1.50A1-260[»]
3MHOX-ray1.15A1-260[»]
3ML2X-ray1.80A1-260[»]
3MMFX-ray1.50A1-260[»]
3MNAX-ray1.50A1-260[»]
3MNHX-ray1.65A1-260[»]
3MNIX-ray1.75A1-260[»]
3MNJX-ray1.75A1-260[»]
3MNKX-ray1.75A1-260[»]
3MNUX-ray1.80A2-260[»]
3MWOX-ray1.40A/B1-260[»]
3MYQX-ray1.35A1-260[»]
3MZCX-ray1.50A1-260[»]
3N0NX-ray1.50A1-260[»]
3N2PX-ray1.65A1-260[»]
3N3JX-ray1.50A1-260[»]
3N4BX-ray1.60A1-260[»]
3NB5X-ray1.80A1-260[»]
3NI5X-ray2.10A1-260[»]
3NJ9X-ray2.00A1-260[»]
3OIKX-ray1.50A1-260[»]
3OILX-ray1.50A1-260[»]
3OIMX-ray1.45A1-260[»]
3OKUX-ray1.45A1-260[»]
3OKVX-ray1.45A1-260[»]
3OY0X-ray1.60A1-260[»]
3OYQX-ray1.47A1-260[»]
3OYSX-ray1.54A1-260[»]
3P3HX-ray1.50A1-260[»]
3P3JX-ray1.60A1-260[»]
3P44X-ray2.20A1-260[»]
3P4VX-ray2.00A1-260[»]
3P55X-ray2.00A1-260[»]
3P58X-ray1.49A1-260[»]
3P5AX-ray1.49A1-260[»]
3P5LX-ray1.50A1-260[»]
3PJJX-ray1.80A2-260[»]
3PO6X-ray1.47A2-260[»]
3PYKX-ray1.30A3-260[»]
3QYKX-ray1.47A1-260[»]
3R16X-ray1.60A4-260[»]
3R17X-ray1.70B4-260[»]
3RG3X-ray1.90A1-260[»]
3RG4X-ray1.50A1-260[»]
3RGEX-ray2.10A1-260[»]
3RJ7X-ray1.20A3-260[»]
3RLDX-ray1.50A1-260[»]
3RYJX-ray1.39B2-260[»]
3RYVX-ray1.20B2-260[»]
3RYXX-ray1.60B2-260[»]
3RYYX-ray1.16A2-260[»]
3RYZX-ray1.37A2-260[»]
3RZ0X-ray1.80B2-260[»]
3RZ1X-ray1.51B2-260[»]
3RZ5X-ray1.65A2-260[»]
3RZ7X-ray1.80A2-260[»]
3RZ8X-ray1.70A2-260[»]
3S71X-ray1.25B3-260[»]
3S72X-ray1.60B3-260[»]
3S73X-ray1.75B3-260[»]
3S74X-ray1.40B3-260[»]
3S75X-ray1.50B3-260[»]
3S76X-ray1.60A3-260[»]
3S77X-ray1.86B3-260[»]
3S78X-ray1.98B3-260[»]
3S8XX-ray1.30A1-260[»]
3S9TX-ray1.30A1-260[»]
3SAPX-ray1.75A1-260[»]
3SAXX-ray1.10A1-260[»]
3SBHX-ray1.65A1-260[»]
3SBIX-ray1.40A1-260[»]
3T5UX-ray1.75A2-260[»]
3T5ZX-ray1.65A2-260[»]
3T82X-ray2.00A1-260[»]
3T83X-ray1.80A1-260[»]
3T84X-ray2.00A1-260[»]
3T85X-ray2.40A1-260[»]
3TMJOther2.00A3-260[»]
3TVNX-ray1.50X3-260[»]
3TVOX-ray1.60X3-260[»]
3U3AX-ray1.55X1-260[»]
3U45X-ray1.70X1-260[»]
3U47X-ray1.60A1-260[»]
3U7CX-ray0.93A1-260[»]
3V2JX-ray1.70A1-260[»]
3V2MX-ray1.47A1-260[»]
3V3FX-ray2.00A1-260[»]
3V3GX-ray1.56B1-260[»]
3V3HX-ray1.85B1-260[»]
3V3IX-ray1.73B1-260[»]
3V3JX-ray1.63A1-260[»]
3V5GX-ray1.50A1-260[»]
3V7XX-ray1.03A2-260[»]
3VBDX-ray1.05A2-260[»]
3ZP9X-ray1.31A1-260[»]
4BCWX-ray1.50A4-260[»]
4BF1X-ray1.35A2-260[»]
4BF6X-ray1.82A2-260[»]
4CA2X-ray2.10A2-260[»]
4CACX-ray2.20A2-260[»]
4DZ7X-ray1.49A1-260[»]
4DZ9X-ray1.49A1-260[»]
4E3DX-ray1.60A1-260[»]
4E3FX-ray1.50A1-260[»]
4E3GX-ray1.55A1-260[»]
4E3HX-ray1.50A1-260[»]
4E49X-ray1.45A1-260[»]
4E4AX-ray1.45A1-260[»]
4E5QX-ray1.70A1-260[»]
4FIKX-ray1.20A1-260[»]
4FL7X-ray1.85A2-260[»]
4FPTX-ray0.98A1-260[»]
4FRCX-ray0.98A1-260[»]
4FU5X-ray0.98A1-260[»]
4FVNX-ray1.05A1-260[»]
4FVOX-ray1.05A1-260[»]
4G0Cneutron diffraction2.00A4-260[»]
4GGEX-ray1.47A1-260[»]
4GL1X-ray1.50X1-260[»]
4HBAX-ray1.76A1-260[»]
4HEWX-ray1.70A1-260[»]
4HEYX-ray1.45A1-260[»]
4HEZX-ray1.34A1-260[»]
4HF3X-ray1.15A1-260[»]
4HT0X-ray1.60A1-260[»]
4IDRX-ray1.60X3-260[»]
4ILXX-ray1.60A4-260[»]
4ITPX-ray1.70A4-260[»]
4IWZX-ray1.60A4-260[»]
4JS6X-ray1.55A1-260[»]
4JSAX-ray1.50A1-260[»]
4JSSX-ray1.50A1-260[»]
4JSWX-ray1.90A1-260[»]
4JSZX-ray1.90A1-260[»]
4KAPX-ray1.45A5-260[»]
4KNIX-ray1.80A1-260[»]
4KNJX-ray2.00A1-260[»]
4LP6X-ray2.15A/B1-260[»]
4M2RX-ray1.99A4-260[»]
4M2UX-ray2.00A4-260[»]
4M2VX-ray1.72A4-260[»]
4M2WX-ray1.66A4-260[»]
4MDGX-ray1.35A3-260[»]
4MDLX-ray1.52A3-260[»]
4MDMX-ray1.55A3-260[»]
4MO8X-ray1.85A1-260[»]
4MTYX-ray1.00A1-260[»]
4N0XX-ray1.63B1-260[»]
5CA2X-ray2.10A2-260[»]
5CACX-ray2.20A2-260[»]
6CA2X-ray2.50A2-260[»]
7CA2X-ray2.40A2-260[»]
8CA2X-ray2.40A2-260[»]
9CA2X-ray2.80A2-260[»]
ProteinModelPortalP00918.
SMRP00918. Positions 3-260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107215. 12 interactions.
IntActP00918. 5 interactions.
MINTMINT-1367766.
STRING9606.ENSP00000285379.

Chemistry

BindingDBP00918.
ChEMBLCHEMBL205.
DrugBankDB00819. Acetazolamide.
DB00436. Bendroflumethiazide.
DB00562. Benzthiazide.
DB01194. Brinzolamide.
DB00880. Chlorothiazide.
DB00606. Cyclothiazide.
DB01119. Diazoxide.
DB00869. Dorzolamide.
DB01031. Ethinamate.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00232. Methyclothiazide.
DB01325. Quinethazone.
DB00273. Topiramate.
DB01021. Trichlormethiazide.

PTM databases

PhosphoSiteP00918.

2D gel databases

OGPP00918.
REPRODUCTION-2DPAGEIPI00218414.
P00918.
UCD-2DPAGEP00918.

Proteomic databases

PaxDbP00918.
PeptideAtlasP00918.
PRIDEP00918.

Protocols and materials databases

DNASU760.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285379; ENSP00000285379; ENSG00000104267.
GeneID760.
KEGGhsa:760.
UCSCuc003ydk.2. human.

Organism-specific databases

CTD760.
GeneCardsGC08P086376.
HGNCHGNC:1373. CA2.
HPACAB010102.
HPA001550.
MIM259730. phenotype.
611492. gene.
neXtProtNX_P00918.
Orphanet2785. Osteopetrosis with renal tubular acidosis.
PharmGKBPA25989.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3338.
HOGENOMHOG000112637.
HOVERGENHBG002837.
InParanoidP00918.
KOK01672.
OMADEANEAC.
OrthoDBEOG7WMCK7.
PhylomeDBP00918.
TreeFamTF316425.

Enzyme and pathway databases

BRENDA4.2.1.1. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKP00918.

Gene expression databases

ArrayExpressP00918.
BgeeP00918.
CleanExHS_CA2.
GenevestigatorP00918.

Family and domain databases

Gene3D3.10.200.10. 1 hit.
InterProIPR018443. CA2/13.
IPR001148. Carbonic_anhydrase_a.
IPR023561. Carbonic_anhydrase_a-class.
IPR018338. Carbonic_anhydrase_a-class_CS.
[Graphical view]
PANTHERPTHR18952. PTHR18952. 1 hit.
PTHR18952:SF31. PTHR18952:SF31. 1 hit.
PfamPF00194. Carb_anhydrase. 1 hit.
[Graphical view]
SMARTSM01057. Carb_anhydrase. 1 hit.
[Graphical view]
SUPFAMSSF51069. SSF51069. 1 hit.
PROSITEPS00162. ALPHA_CA_1. 1 hit.
PS51144. ALPHA_CA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCA2. human.
EvolutionaryTraceP00918.
GeneWikiCarbonic_anhydrase_II.
GenomeRNAi760.
NextBio3074.
PROP00918.
SOURCESearch...

Entry information

Entry nameCAH2_HUMAN
AccessionPrimary (citable) accession number: P00918
Secondary accession number(s): B2R7G8, Q6FI12, Q96ET9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 183 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM