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P81383

- OXLA_OPHHA

UniProt

P81383 - OXLA_OPHHA

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Protein
L-amino-acid oxidase
Gene
N/A
Organism
Ophiophagus hannah (King cobra) (Naja hannah)
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. Unlike most snake L-amino-acid oxidases, this enzyme exhibits potent activity against L-Lys. Has also potent activity against L-Met, L-Leu, L-His, L-Lys and L-Ile. Its activity on platelet aggregation is controversial. It has potent inhibitory activity on platelet aggregation induced by ADP and the thromboxane analog U46619, but not by thrombin, mucetin, ristocetin and stejnulxin (1 Publication), but it has also been shown to induce platelet aggregation through the formation of hydrogen peroxide (1 Publication). It binds to bacteria and shows antibacterial activities by generating hydrogen peroxide. Binding and antibacterial activities are higher against Gram-positive than against Gram-negative bacteria. May also have an ability to induce hemorrhage, hemolysis, edema, apoptosis.5 Publications

Catalytic activityi

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

Cofactori

FAD.2 Publications

Kineticsi

  1. KM=2.3 mM for L-His (1 Publication)3 Publications
  2. KM=2.9 mM for L-Ile (1 Publication)
  3. KM=2.2 mM for L-Leu (1 Publication)
  4. KM=2.6 mM for L-Lys (1 Publication)
  5. KM=0.7 mM for L-Met (1 Publication)
  6. KM=0.20 mM for L-Leu (1 Publication)
  7. KM=0.63 mM for L-Met (1 Publication)
  8. KM=0.10 mM for L-Phe (1 Publication)
  9. KM=0.10 mM for L-Trp (1 Publication)

Temperature dependencei

Exhibits unusual thermal stability. At pH 7.4, the enzyme retains full activity after incubation at 25 degrees Celsius for 30 days. Is stable at alkaline condition and is not inactivated by freezing.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891FAD By similarity
Binding sitei106 – 1061Substrate By similarity
Binding sitei269 – 2691FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding sitei380 – 3801Substrate By similarity
Binding sitei465 – 4651FAD By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 622FAD By similarity
Nucleotide bindingi81 – 822FAD By similarity
Nucleotide bindingi103 – 1064FAD By similarity
Nucleotide bindingi472 – 4776FAD By similarity
Nucleotide bindingi472 – 4732Substrate By similarity

GO - Molecular functioni

  1. L-amino-acid oxidase activity Source: UniProtKB
  2. flavin adenine dinucleotide binding Source: UniProtKB
  3. protein dimerization activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
  3. hemolysis in other organism Source: UniProtKB-KW
  4. killing of cells of other organism Source: UniProtKB
  5. modification of morphology or physiology of other organism Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Apoptosis, Cytolysis, Hemolysis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

SABIO-RKP81383.

Names & Taxonomyi

Protein namesi
Recommended name:
L-amino-acid oxidase (EC:1.4.3.2)
Short name:
LAAO
Short name:
LAO
Short name:
Oh-LAAO
OrganismiOphiophagus hannah (King cobra) (Naja hannah)
Taxonomic identifieri8665 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeElapinaeOphiophagus

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 5 mg/kg by intravenous injection into mice.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20203 Publications
Add
BLAST
Chaini21 – 491471L-amino-acid oxidase
PRO_0000099871Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 182 By similarity
Glycosylationi122 – 1221N-linked (GlcNAc...) Reviewed prediction
Glycosylationi238 – 2381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi266 – 2661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi338 ↔ 420 By similarity
Glycosylationi410 – 4101N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated Inferred.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Tissue specificityi

Expressed by the venom gland.

Interactioni

Subunit structurei

Homodimer; non-covalently linked.4 Publications

Structurei

3D structure databases

ProteinModelPortaliP81383.
SMRiP81383. Positions 25-491.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG005729.

Family and domain databases

InterProiIPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
PRINTSiPR00757. AMINEOXDASEF.

Sequencei

Sequence statusi: Complete.

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

P81383-1 [UniParc]FASTAAdd to Basket

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MNDFLLLLLV LFLGVPRSEN HVINLEECFQ EPEYENWLAT ASHGLTKTLN    50
PKKIVIVGAG ISGLTAAKLF REAGHEVVIL EASDRVGGRI KTHREDGWYV 100
DVGPMRVPQT HRIVREYIKK FNISLNPFRQ TDENAWYLIK HVRQKMSANN 150
PENFGYQLNP NERGKSASQL FDETLDKVTD DCTLQKEKYD SFSTKEYLIK 200
EGKLSTGAVE MIGDFLNEEA GFHNSFLISV MDHFLFLNNS FDEITGGFDQ 250
LPERFFKDMD SIVHLNSTVE KIVHINNKVT VFYEGLSTNM RLVADYVLIT 300
ATARATRLIK FVPPLSIPKT RALRSLIYAS ATKIILVCTD KFWEKDGIHG 350
GRSITDLPSR VIYYPNHDFT NGIGVLLASY TWYSDSEFYT TLSDEKCVDV 400
VMDDLVEIHN VSKDYLKSVC GKHVVQKWAL DQYSMGAFST YTPYQITHYS 450
QMLAQNEGRI YFAGEYTAHP HGWIETSMKS AIREAINIHN A 491
Length:491
Mass (Da):55,977
Last modified:September 21, 2011 - v3
Checksum:i2FD1E740BD73313E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211H → S AA sequence 1 Publication
Sequence conflicti28 – 281C → S AA sequence 1 Publication
Sequence conflicti28 – 281C → S AA sequence 1 Publication
Sequence conflicti37 – 371W → H AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF080831 mRNA. Translation: ABN72538.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EF080831 mRNA. Translation: ABN72538.1 .

3D structure databases

ProteinModelPortali P81383.
SMRi P81383. Positions 25-491.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG005729.

Enzyme and pathway databases

SABIO-RK P81383.

Family and domain databases

InterProi IPR002937. Amino_oxidase.
IPR001613. Flavin_amine_oxidase.
[Graphical view ]
Pfami PF01593. Amino_oxidase. 1 hit.
[Graphical view ]
PRINTSi PR00757. AMINEOXDASEF.
ProtoNeti Search...

Publicationsi

  1. "Molecular characterization of L-amino acid oxidase from king cobra venom."
    Jin Y., Lee W.-H., Zeng L., Zhang Y.
    Toxicon 50:479-489(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-45; 121-129; 189-195; 272-278 AND 428-439, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
    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 21-39, SUBUNIT, GLYCOSYLATION, COFACTOR.
    Tissue: Venom.
  3. "Characterization and cytotoxicity of L-amino acid oxidase from the venom of king cobra (Ophiophagus hannah)."
    Ahn M.Y., Lee B.M., Kim Y.S.
    Int. J. Biochem. Cell Biol. 29:911-919(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-35, FUNCTION, SUBUNIT, GLYCOSYLATION.
    Tissue: Venom.
  4. "Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom."
    Tan N.H., Saifuddin M.N.
    Biochem. Int. 19:937-944(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, TOXIC DOSE.
  5. "Substrate specificity of king cobra (Ophiophagus hannah) venom L-amino acid oxidase."
    Tan N.H., Saifuddin M.N.
    Int. J. Biochem. 23:323-327(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY.
    Tissue: Venom.
  6. "The edema inducing activity of Ophiophagus hannah (king cobra) venom L-amino acid oxidase."
    Tan N.-H., Choy S.-K.
    Toxicon 32:539-539(1994)
    Cited for: ISOFORM.
  7. "Purification and characterization of L-amino acid oxidase from king cobra (Ophiophagus hannah) venom and its effects on human platelet aggregation."
    Li Z.Y., Yu T.F., Lian E.C.
    Toxicon 32:1349-1358(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Tissue: Venom.
  8. "Antibacterial action of a heat-stable form of L-amino acid oxidase isolated from king cobra (Ophiophagus hannah) venom."
    Lee M.L., Tan N.H., Fung S.Y., Sekaran S.D.
    Comp. Biochem. Physiol. 153:237-242(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ANTIBACTERIAL ACTIVITY.
    Tissue: Venom.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Venom.

Entry informationi

Entry nameiOXLA_OPHHA
AccessioniPrimary (citable) accession number: P81383
Secondary accession number(s): A8QL50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 21, 2011
Last modified: April 16, 2014
This is version 56 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

The existence of two isoforms has been reported (1 Publication), and could explain the differences in sequence and kinetic parameters.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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