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Information on EC 1.4.3.2 - L-amino-acid oxidase and Organism(s) Aplysia californica and UniProt Accession Q6IWZ0

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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:
Aplysia californica
UNIPROT: Q6IWZ0
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Word Map
The taxonomic range for the selected organisms is: Aplysia californica
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-arginine + H2O + O2
2-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram
-
-
-
?
L-Lys + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram
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
-
-
-
-
?
additional information
?
-
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-Lys + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram
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
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
bactericidal assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.5
pH-profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
bactericidal assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
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_APLCA
535
0
60300
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 60000, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
sequence contains one potential glycosylation site. Glycosylation is not essential for antimicrobial activity
proteolytic modification
sequence contains a signal peptide of 18 amino acids
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
no decrease in antimicrobial activity during storage for up to 5 months at room temperature
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, H.; Johnson, P.M.; Ko, K.C.; Kamio, M.; Germann, M.W.; Derby, C.D.; Tai, P.C.
Cloning, characterization and expression of escapin, a broadly antimicrobial FAD-containing L-amino acid oxidase from ink of the sea hare Aplysia californica
J. Exp. Biol.
208
3609-3622
2005
Aplysia californica (Q6IWZ0), Aplysia californica
Manually annotated by BRENDA team
Ko, K.C.; Wang, B.; Tai, P.C.; Derby, C.D.
Identification of potent bactericidal compounds produced by escapin, an L-amino acid oxidase in the ink of the sea hare Aplysia californica
Antimicrob. Agents Chemother.
52
4455-4462
2008
Aplysia californica (Q6IWZ0), Aplysia californica
Manually annotated by BRENDA team
Kamio, M.; Ko, K.C.; Zheng, S.; Wang, B.; Collins, S.L.; Gadda, G.; Tai, P.C.; Derby, C.D.
The chemistry of escapin: identification and quantification of the components in the complex mixture generated by an L-amino acid oxidase in the defensive secretion of the sea snail Aplysia californica
Chemistry
15
1597-1603
2009
Aplysia californica (Q6IWZ0), Aplysia californica, Aplysia californica Cooper 1863 (Q6IWZ0)
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