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Information on EC 1.4.3.2 - L-amino-acid oxidase and Organism(s) Naja atra and UniProt Accession A8QL58

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EC Tree
     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.2 L-amino-acid oxidase
IUBMB Comments
A flavoprotein (FAD).
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This record set is specific for:
Naja atra
UNIPROT: A8QL58
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Word Map
The taxonomic range for the selected organisms is: Naja atra
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
laao, il4i1, l-amino-acid oxidase, l-aao, escapin, head kidney and gill, dolabellanin, l-phenylalanine oxidase, akbu-laao, m-lao, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aromatic L-amino acid oxidase
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L-amino acid oxidase
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L-amino acid:O2 oxidoreductase
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L-aminooxidase
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LAO
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ophio-amino-acid oxidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidative deamination
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SYSTEMATIC NAME
IUBMB Comments
L-amino-acid:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9000-89-9
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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inhibits platelet aggregation induced by LAAO
EMD 132338
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inhibits platelet aggregation induced by LAAO
additional information
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LAAO has no activity on platelets in platelet-rich plasma. Catalase inhibits the platelet aggregation and platelet protein phosphorylation induced by LAAO
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OXLA_NAJAT
507
0
57963
Swiss-Prot
Secretory Pathway (Reliability: 1)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by cation ion exchange chromatography, gel filtration and anion ion exchange chromatography, to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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LAAO dose-dependently induces aggregation of washed human platelets. It induces tyrosine phosphorylation of a number of platelet proteins including Src kinase, spleen tyrosine kinase, and phospholipase C gamma2. Both H2O2 production and binding to platelet membrane proteins may be involved in its action. The enzyme binds to the platelet membrane to enhance the sensitivity of platelets to H2O2. At the same time, H2O2 released by the enzyme activates platelets by an unknown mechanism
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, R.; Zhu, S.; Wu, J.; Wang, W.; Lu, Q.; Clemetson, K.J.
L-amino acid oxidase from Naja atra venom activates and binds to human platelets
Acta Biochim. Biophys. Sin.
40
19-26
2008
Naja atra
Manually annotated by BRENDA team
Jin, Y.; Lee, W.H.; Zeng, L.; Zhang, Y.
Molecular characterization of L-amino acid oxidase from king cobra venom
Toxicon
50
479-489
2007
Bungarus fasciatus (A8QL52), Bungarus fasciatus, Bungarus multicinctus (A8QL51), Bungarus multicinctus, Naja atra (A8QL58), Naja atra, Ophiophagus hannah (P81383), Ophiophagus hannah
Manually annotated by BRENDA team