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Information on EC 1.4.3.2 - L-amino-acid oxidase and Organism(s) Trimeresurus stejnegeri and UniProt Accession Q6WP39

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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:
Trimeresurus stejnegeri
UNIPROT: Q6WP39
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Word Map
The taxonomic range for the selected organisms is: Trimeresurus stejnegeri
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
-
-
-
-
L-amino acid oxidase
L-amino acid:O2 oxidoreductase
-
-
-
-
L-aminooxidase
-
-
-
-
LAO
-
-
-
-
ophio-amino-acid oxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidative deamination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-amino-acid:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
CAS REGISTRY NUMBER
COMMENTARY hide
9000-89-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme exhibits antibacterial, antiviral, and antiprotozoal effects
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OXLA_TRIST
516
0
58601
Swiss-Prot
Secretory Pathway (Reliability: 1)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
enzyme displays dosedependent inhibition on HIV-1 infection and replication
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Y.J.; Wang, J.H.; Lee, W.H.; Wang, Q.; Liu, H.; Zheng, Y.T.; Zhang, Y.
Molecular characterization of Trimeresurus stejnegeri venom L-amino acid oxidase with potential anti-HIV activity
Biochem. Biophys. Res. Commun.
309
598-604
2003
Trimeresurus stejnegeri (Q6WP39), Trimeresurus stejnegeri
Manually annotated by BRENDA team
Lukasheva, E.; Efremova, A.; Treshalina, E.; Arinbasarova, A.; Medentzev, A.; Berezov, T.
L-Amino acid oxidases: Properties and molecular mechanisms of action
Biomed. Khim.
58
372-384
2012
Lissachatina fulica, Aplysia californica, Bothrops jararaca, Bothrops moojeni, Mus musculus, Trichoderma harzianum, Macrovipera lebetina, Protobothrops jerdonii, Crotalus durissus cascavella, Bothrops alternatus, Trimeresurus stejnegeri, Bothrops pirajai, Sebastes schlegelii, Platichthys stellatus
Manually annotated by BRENDA team