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Information on EC 1.4.3.2 - L-amino-acid oxidase and Organism(s) Bothrops moojeni and UniProt Accession Q6TGQ8

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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:
Bothrops moojeni
UNIPROT: Q6TGQ8
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The taxonomic range for the selected organisms is: Bothrops moojeni
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
glycine + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-alanine + H2O + O2
2-oxopropanoic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-amino acid + H2O + O2
2-oxocarboxylate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-arginine + H2O + O2
2-oxo-5-guanidinovaleric acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-glutamic acid + H2O + O2
2-oxoglutarate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-histidine + H2O + O2
3-(1H-imidazol-4-yl)-2-oxopropionic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-isoleucine + H2O + O2
3-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram
-
high catalytic activity
-
-
?
L-leucine + H2O + O2
4-methyl-2-oxopentanoic acid + NH3 + H2O2
show the reaction diagram
L-lysine + H2O + O2
6-amino-2-oxohexanoic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-methionine + H2O + O2
4-methylsulfanyl-2-oxobutanoate + NH3 + H2O2
show the reaction diagram
-
high affinity for the substrate
-
-
?
L-norleucine + H2O + O2
2-oxohexanoate + NH3 + H2O2
show the reaction diagram
-
high catalytic activity
-
-
?
L-phenylalanine + H2O + O2
phenylpyruvate + NH3 + H2O2
show the reaction diagram
-
high affinity for the substrate
-
-
?
L-proline + H2O + O2
? + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-serine + H2O + O2
2-oxo-3-hydroxypropionic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-threonine + H2O + O2
2-oxo-3-hydroxybutanoic acid + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
L-tryptophan + H2O + O2
3-indole-2-oxopropanoate + NH3 + H2O2
show the reaction diagram
-
high affinity for the substrate
-
-
?
L-tyrosine + H2O + O2
p-hydroxyphenylpyruvate + NH3 + H2O2
show the reaction diagram
-
high affinity for the substrate
-
-
?
L-valine + H2O + O2
2-oxoisovalerate + 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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the glycosylation site of the enzyme is not important for structural delineation of the active site
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
with L-glutamine as substrate
140
-
with L-histidine as substrate
230
-
with L-alanine as substrate
35
-
with L-serine as substrate
40
-
with L-threonine or L-proline as substrate
430
-
with L-valine as substrate
435
-
with L-isoleucine as substrate
460
-
with L-methionine as substrate
480
-
with L-leucine as substrate
487.7
-
12.9fold purified
5
-
with glycine or L-lysine as substrate
585
-
with L-tryptophan as substrate
635
-
with L-tyrosine as substrate
665
-
with L-phenylalanine as substrate
90
-
with L-arginine as substrate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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_BOTMO
502
0
56840
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53780
sequence analysis
130800
-
mass spectrometry
64889
-
2 * 64889, mass spectrometry, 1 * 66000, SDS-PAGE
66000
-
2 * 64889, mass spectrometry, 1 * 66000, SDS-PAGE
69000
-
2 * 69000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 69000
homodimer
-
2 * 64889, mass spectrometry, 1 * 66000, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
at a pH below 4, enzymatic activity is completely lost
692650
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
at temperatures lower than 4°C, enzymatic activity is completely lost
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by molecular exclusion, ion exchange and hydrophobic chromatography
by ion-exchange chromatography and gel filtration, 12.9fold
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
purified LAAO-I exhibits antiprotozoal activities which are demonstrated to be hydrogen-peroxide mediated. Exposure of promastigotes of Leishmania sp. results in dose-dependent parasite killing. LAAOs are interesting multifunctional enzymes, not only for a better understanding of the ophidian envenomation mechanism, but also due to their biotechnological potential as model for therapeutic agents
medicine
-
LAAO-I exhibited bactericidal, antitumoral, trypanocidal, edematogenic, and platelet-aggregating activities. It induces typical apoptotic DNA fragmentation in HL-60 cells. Potential use of LAAO-I as a therapeutic agent for treatment of diseases in which induction of H2O2 production can be beneficial
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Du, X.Y.; Clemetson, K.J.
Snake venom L-amino acid oxidases
Toxicon
40
659-665
2002
Agkistrodon contortrix laticinctus, Gloydius blomhoffii, Calloselasma rhodostoma, Bothrops moojeni, Crotalus adamanteus, Crotalus atrox, Eristicophis macmahoni, Ophiophagus hannah, snake, Protobothrops flavoviridis, Protobothrops mucrosquamatus, Naja kaouthia, Pseudechis australis
Manually annotated by BRENDA team
Franca, S.C.; Kashima, S.; Roberto, P.G.; Marins, M.; Ticli, F.K.; Pereira, J.O.; Astolfi-Filho, S.; Stabeli, R.G.; Magro, A.J.; Fontes, M.R.; Sampaio, S.V.; Soares, A.M.
Molecular approaches for structural characterization of Bothrops L-amino acid oxidases with antiprotozoal activity: cDNA cloning, comparative sequence analysis, and molecular modeling
Biochem. Biophys. Res. Commun.
355
302-306
2007
Bothrops moojeni (Q6TGQ8), Bothrops jararacussu (Q6TGQ9)
Manually annotated by BRENDA team
Stabeli, R.G.; SantAna, C.D.; Ribeiro, P.H.; Costa, T.R.; Ticli, F.K.; Pires, M.G.; Nomizo, A.; Albuquerque, S.; Malta-Neto, N.R.; Marins, M.; Sampaio, S.V.; Soares, A.M.
Cytotoxic L-amino acid oxidase from Bothrops moojeni: biochemical and functional characterization
Int. J. Biol. Macromol.
41
132-140
2007
Bothrops moojeni
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