SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P81382

- OXLA_CALRH

UniProt

P81382 - OXLA_CALRH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
L-amino-acid oxidase
Gene
N/A
Organism
Calloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions By similarity.

Catalytic activityi

An L-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactori

FAD.

Kineticsi

  1. KM=0.63 mM for L-Leu1 Publication
  2. KM=0.24 mM for L-Met
  3. KM=0.05 mM for L-Phe
  4. KM=0.08 mM for L-Trp

pH dependencei

Optimum pH is 9.0.

Temperature dependencei

Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FAD
Binding sitei108 – 1081Substrate
Binding sitei241 – 2411Substrate
Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygen
Binding sitei390 – 3901Substrate
Binding sitei475 – 4751FAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 622FAD
Nucleotide bindingi81 – 822FAD
Nucleotide bindingi105 – 1084FAD
Nucleotide bindingi482 – 4876FAD
Nucleotide bindingi482 – 4832Substrate

GO - Molecular functioni

  1. L-amino-acid oxidase activity Source: UniProtKB-EC

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Hemostasis impairing toxin, Oxidoreductase, Platelet aggregation inhibiting toxin, Toxin

Keywords - Biological processi

Apoptosis, Cytolysis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

SABIO-RKP81382.

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
LAAO
Short name:
LAO
OrganismiCalloselasma rhodostoma (Malayan pit viper) (Agkistrodon rhodostoma)
Taxonomic identifieri8717 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaViperidaeCrotalinaeCalloselasma

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 Publications
Add
BLAST
Chaini19 – 516498L-amino-acid oxidase
PRO_0000001707Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 1911 Publication
Glycosylationi190 – 1901N-linked (GlcNAc...)1 Publication
Disulfide bondi349 ↔ 4301 Publication
Glycosylationi379 – 3791N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP81382.

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer; non-covalently linked.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 294
Helixi34 – 4310
Beta strandi53 – 575
Helixi61 – 7313
Beta strandi76 – 805
Beta strandi82 – 876
Beta strandi92 – 954
Turni96 – 994
Beta strandi100 – 1056
Helixi114 – 1229
Beta strandi127 – 1304
Beta strandi137 – 1415
Beta strandi144 – 1474
Helixi148 – 1536
Helixi155 – 1584
Helixi164 – 1663
Helixi171 – 1788
Helixi180 – 1889
Helixi191 – 1988
Beta strandi200 – 2023
Helixi203 – 2097
Helixi215 – 22410
Helixi228 – 2303
Helixi235 – 24511
Beta strandi251 – 2544
Helixi260 – 2689
Helixi269 – 2724
Beta strandi273 – 2764
Beta strandi278 – 2847
Beta strandi289 – 2946
Beta strandi296 – 2983
Beta strandi302 – 3109
Helixi314 – 3174
Beta strandi320 – 3245
Helixi328 – 3369
Beta strandi342 – 35110
Helixi353 – 3575
Beta strandi361 – 3688
Beta strandi372 – 3743
Beta strandi385 – 3928
Helixi393 – 3975
Turni398 – 4014
Helixi404 – 41916
Helixi423 – 4297
Beta strandi430 – 4378
Helixi438 – 4403
Turni442 – 4443
Beta strandi446 – 4494
Helixi455 – 46410
Beta strandi470 – 4723
Helixi475 – 4773
Beta strandi478 – 4825
Helixi484 – 50320

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F8RX-ray2.00A/B/C/D19-516[»]
1F8SX-ray2.00A/B/C/D/E/F/G/H19-516[»]
2IIDX-ray1.80A/B/C/D19-516[»]
ProteinModelPortaliP81382.
SMRiP81382. Positions 22-504.

Miscellaneous databases

EvolutionaryTraceiP81382.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P81382-1 [UniParc]FASTAAdd to Basket

« Hide

MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN    50
PKHVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW 100
YANLGPMRLP EKHRIVREYI RKFDLRLNEF SQENDNAWYF IKNIRKKVGE 150
VKKDPGLLKY PVKPSEAGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT 200
YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR 250
FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET 300
PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT 350
TKFWEDDGIH GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ 400
ALDFKDCADI VFNDLSLIHQ LPKKDIQSFC YPSVIQKWSL DKYAMGGITT 450
FTPYQFQHFS DPLTASQGRI YFAGEYTAQA HGWIDSTIKS GLRAARDVNL 500
ASENPSGIHL SNDNEL 516
Length:516
Mass (Da):58,221
Last modified:January 23, 2002 - v2
Checksum:i5F9435718B3A3BDE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281C → E AA sequence 1 Publication
Sequence conflicti33 – 331D → N AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ271725 mRNA. Translation: CAB71136.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ271725 mRNA. Translation: CAB71136.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F8R X-ray 2.00 A/B/C/D 19-516 [» ]
1F8S X-ray 2.00 A/B/C/D/E/F/G/H 19-516 [» ]
2IID X-ray 1.80 A/B/C/D 19-516 [» ]
ProteinModelPortali P81382.
SMRi P81382. Positions 22-504.
ModBasei Search...
MobiDBi Search...

PTM databases

UniCarbKBi P81382.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005729.

Enzyme and pathway databases

SABIO-RK P81382.

Miscellaneous databases

EvolutionaryTracei P81382.

Family and domain databases

InterProi IPR002937. Amino_oxidase.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "L-amino-acid oxidase from Malayan pit viper Calloselasma rhodostoma: comparative sequence analysis and characterization of active and inactive forms of the enzyme."
    Macheroux P., Seth O., Bollschweiler C., Schwarz M., Kurfuerst M., Au L.-C., Ghisla S.
    Eur. J. Biochem. 268:1679-1686(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-33.
    Tissue: Venom and Venom gland.
  2. "Purification and properties of the L-amino acid oxidase from Malayan pit viper (Calloselasma rhodostoma) venom."
    Ponnudurai G., Chung M.C.M., Tan N.-H.
    Arch. Biochem. Biophys. 313:373-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-38, SUBUNIT.
    Tissue: Venom.
  3. "Molecular cloning, expression and purification of L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma."
    Kommoju P.R., Macheroux P., Ghisla S.
    Protein Expr. Purif. 52:89-95(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPRESSION OF ACTIVE RECOMBINANT LAAO.
  4. "L-amino acid oxidase from Vipera lebetina venom: isolation, characterization, effects on platelets and bacteria."
    Tonismagi K., Samel M., Trummal K., Ronnholm G., Siigur J., Kalkkinen N., Siigur E.
    Toxicon 48:227-237(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  5. "The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site."
    Pawelek P.D., Cheah J., Coulombe R., Macheroux P., Ghisla S., Vrielink A.
    EMBO J. 19:4204-4215(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD, DISULFIDE BONDS, GLYCOSYLATION AT ASN-190 AND ASN-379.
    Tissue: Venom.
  6. "Crystal structure of LAAO from Calloselasma rhodostoma with an L-phenylalanine substrate: insights into structure and mechanism."
    Moustafa I.M., Foster S., Lyubimov A.Y., Vrielink A.
    J. Mol. Biol. 364:991-1002(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 19-516 IN COMPLEX WITH FAD AND SUBSTRATE L-PHE.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_CALRH
AccessioniPrimary (citable) accession number: P81382
Secondary accession number(s): Q9I849
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2002
Last modified: October 16, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi