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).By similarity

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=0.63 mM for L-Leu1 Publication
  2. KM=0.24 mM for L-Met1 Publication
  3. KM=0.05 mM for L-Phe1 Publication
  4. KM=0.08 mM for L-Trp1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Temperature dependencei

Thermostable.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FAD2 Publications
Binding sitei108 – 1081Substrate
Binding sitei241 – 2411Substrate
Binding sitei279 – 2791FAD; via amide nitrogen and carbonyl oxygen2 Publications
Binding sitei390 – 3901Substrate
Binding sitei475 – 4751FAD2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 622FAD2 Publications
Nucleotide bindingi81 – 822FAD2 Publications
Nucleotide bindingi105 – 1084FAD2 Publications
Nucleotide bindingi482 – 4876FAD2 Publications
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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18182 PublicationsAdd
BLAST
Chaini19 – 516498L-amino-acid oxidasePRO_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.3 Publications

Structurei

Secondary structure

1
516
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 294Combined sources
Helixi34 – 4310Combined sources
Beta strandi53 – 575Combined sources
Helixi61 – 7313Combined sources
Beta strandi76 – 805Combined sources
Beta strandi82 – 876Combined sources
Beta strandi92 – 954Combined sources
Turni96 – 994Combined sources
Beta strandi100 – 1056Combined sources
Helixi114 – 1229Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi137 – 1415Combined sources
Beta strandi144 – 1474Combined sources
Helixi148 – 1536Combined sources
Helixi155 – 1584Combined sources
Helixi164 – 1663Combined sources
Helixi171 – 1788Combined sources
Helixi180 – 1889Combined sources
Helixi191 – 1988Combined sources
Beta strandi200 – 2023Combined sources
Helixi203 – 2097Combined sources
Helixi215 – 22410Combined sources
Helixi228 – 2303Combined sources
Helixi235 – 24511Combined sources
Beta strandi251 – 2544Combined sources
Helixi260 – 2689Combined sources
Helixi269 – 2724Combined sources
Beta strandi273 – 2764Combined sources
Beta strandi278 – 2847Combined sources
Beta strandi289 – 2946Combined sources
Beta strandi296 – 2983Combined sources
Beta strandi302 – 3109Combined sources
Helixi314 – 3174Combined sources
Beta strandi320 – 3245Combined sources
Helixi328 – 3369Combined sources
Beta strandi342 – 35110Combined sources
Helixi353 – 3575Combined sources
Beta strandi361 – 3688Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi385 – 3928Combined sources
Helixi393 – 3975Combined sources
Turni398 – 4014Combined sources
Helixi404 – 41916Combined sources
Helixi423 – 4297Combined sources
Beta strandi430 – 4378Combined sources
Helixi438 – 4403Combined sources
Turni442 – 4443Combined sources
Beta strandi446 – 4494Combined sources
Helixi455 – 46410Combined sources
Beta strandi470 – 4723Combined sources
Helixi475 – 4773Combined sources
Beta strandi478 – 4825Combined sources
Helixi484 – 50320Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

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

        10         20         30         40         50
MNVFFMFSLL FLAALGSCAD DRNPLAECFQ ENDYEEFLEI ARNGLKATSN
60 70 80 90 100
PKHVVIVGAG MAGLSAAYVL AGAGHQVTVL EASERPGGRV RTYRNEEAGW
110 120 130 140 150
YANLGPMRLP EKHRIVREYI RKFDLRLNEF SQENDNAWYF IKNIRKKVGE
160 170 180 190 200
VKKDPGLLKY PVKPSEAGKS AGQLYEESLG KVVEELKRTN CSYILNKYDT
210 220 230 240 250
YSTKEYLIKE GDLSPGAVDM IGDLLNEDSG YYVSFIESLK HDDIFAYEKR
260 270 280 290 300
FDEIVDGMDK LPTAMYRDIQ DKVHFNAQVI KIQQNDQKVT VVYETLSKET
310 320 330 340 350
PSVTADYVIV CTTSRAVRLI KFNPPLLPKK AHALRSVHYR SGTKIFLTCT
360 370 380 390 400
TKFWEDDGIH GGKSTTDLPS RFIYYPNHNF TNGVGVIIAY GIGDDANFFQ
410 420 430 440 450
ALDFKDCADI VFNDLSLIHQ LPKKDIQSFC YPSVIQKWSL DKYAMGGITT
460 470 480 490 500
FTPYQFQHFS DPLTASQGRI YFAGEYTAQA HGWIDSTIKS GLRAARDVNL
510
ASENPSGIHL SNDNEL
Length:516
Mass (Da):58,221
Last modified:January 23, 2002 - v2
Checksum:i5F9435718B3A3BDE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281C → E AA sequence (PubMed:8080286)Curated
Sequence conflicti33 – 331D → N AA sequence (PubMed:8080286)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271725 mRNA. Translation: CAB71136.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ271725 mRNA. Translation: CAB71136.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein 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