Information on EC 1.4.3.2 - L-amino-acid oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.4.3.2
-
RECOMMENDED NAME
GeneOntology No.
L-amino-acid oxidase
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
arginine degradation VIII (arginine oxidase pathway)
-
Cysteine and methionine metabolism
-
Isoquinoline alkaloid biosynthesis
-
Metabolic pathways
-
Phenylalanine metabolism
-
Phenylalanine, tyrosine and tryptophan biosynthesis
-
Tryptophan metabolism
-
Tyrosine metabolism
-
Valine, leucine and isoleucine degradation
-
SYSTEMATIC NAME
IUBMB Comments
L-amino-acid:oxygen oxidoreductase (deaminating)
A flavoprotein (FAD).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
APIT
Q6T277
-
aromatic L-amino acid oxidase
-
-
-
-
Balt-LAAO-I
-
-
Bpir-LAOO-1
-
-
Dolabellanin
-
-
escapin
Aplysia californica Cooper 1863
Q6IWZ0
-
-
IL4I1
-
interleukin 4 induced gene 1
IL4I1
-
-
Il4i1 protein
-
secreted L-phenylalanine oxidase, physiologically expressed by myeloid cells, gene expression in primary mediastinal B-cell lymphoma
Il4i1 protein
-
-
ink toxin 1
Q6T277
-
Interleukin Four Induced Gene 1 protein
-
first described in the mouse, characterized in human B cells, expression is restricted to lymphoid tissues and induced by interleukin-4
L-AAO
Q6IWZ0
-
L-AAO
Pseudoalteromonas flavipulchra C2
-
-
-
L-AAO
Rhodococcus sp. AIU Z-35-1
-
-
-
L-amino acid oxidase
-
-
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
Hypocrea lixii ETS 323
-
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
-
L-amino acid oxidase
-
-
L-amino acid oxidase
-
-
L-amino acid: O2 oxidoreductase
-
-
L-amino acid:O2 oxidoreductase
-
-
-
-
L-amino acid:O2 oxidoreductase (deaminating)
-
-
L-aminooxidase
-
-
-
-
L-phenylalanine oxidase
-
-
LAAO
-
-
-
-
LAAO
Q6IWZ0
-
LAAO
Aplysia californica Cooper 1863
Q6IWZ0
-
-
LAAO
A8QL52
-
LAAO
-
-
LAAO
Hypocrea lixii ETS 323
-
-
-
LAAO
-
-
LAAO
A8QL58
-
LAAO
-
-
LAAO
A8QL50
-
LAAO-I
Q6TGQ9
-
LAAO-I
Q6TGQ8
-
LAO
-
-
-
-
LAO
Hebeloma cylindrosporum CBS 558.96
-
-
-
LAO
Hebeloma sp., Laccaria bicolor
-
-
LAO
Laccaria bicolor S238N
-
-
-
LAO
Pseudoalteromonas luteoviolacea CPMOR-1, Pseudoalteromonas luteoviolacea CPMOR-2, Pseudoalteromonas luteoviolacea NCIMB 1893T
-
-
-
M-LAO
Q90W54
-
ophio-amino-acid oxidase
-
-
-
-
Sebastes schlegeli antibacterial protein
A1IGW6
-
Sebastes schlegelii antibacterial protein
-
-
SSAP
A1IGW6
-
toxophallin
-
-
CAS REGISTRY NUMBER
COMMENTARY
9000-89-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cottonmouth moccasin
-
-
Manually annotated by BRENDA team
sea hare, strain Cooper 1863 collected in California
Swissprot
Manually annotated by BRENDA team
strain Cooper 1863 collected in California
Swissprot
Manually annotated by BRENDA team
Aplysia californica Cooper 1863
strain Cooper 1863 collected in California
Swissprot
Manually annotated by BRENDA team
-
Q6T277
SwissProt
Manually annotated by BRENDA team
Bacillus carotarum
2Pfa
-
-
Manually annotated by BRENDA team
Bacillus carotarum 2Pfa
2Pfa
-
-
Manually annotated by BRENDA team
Bothrops sp.
venom
-
-
Manually annotated by BRENDA team
llected from Guangxi Province, P.R. China
-
-
Manually annotated by BRENDA team
; expression in Pichia pastoris
-
-
Manually annotated by BRENDA team
Corynebacterium sp. A20
A20
-
-
Manually annotated by BRENDA team
eastern diamondback rattlesnake, multiple electrophoretic components
-
-
Manually annotated by BRENDA team
Crotalus terrificus terrificus
-
-
-
Manually annotated by BRENDA team
strain CBS 558.96
-
-
Manually annotated by BRENDA team
Hebeloma cylindrosporum CBS 558.96
strain CBS 558.96
-
-
Manually annotated by BRENDA team
Hebeloma sp.
strains SE5, F-NB01 , F-RS01, R-RS01 and SIV
-
-
Manually annotated by BRENDA team
lymphoid and non lymphoid malignancies, lymphoma cell lines L428, KM-H2, and SU-DHL-4
-
-
Manually annotated by BRENDA team
Hypocrea lixii ETS 323
-
-
-
Manually annotated by BRENDA team
strain S238N
-
-
Manually annotated by BRENDA team
Laccaria bicolor S238N
strain S238N
-
-
Manually annotated by BRENDA team
milk
Uniprot
Manually annotated by BRENDA team
isozymes MPLAO1, MPLAO2, and MPLAO3
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
inducible, expression in cells derepressed for nitrogen in presence of an amino acid, intracellular and extracellular location
-
-
Manually annotated by BRENDA team
no activity in Acinetobacter anitratum
-
-
-
Manually annotated by BRENDA team
no activity in Alcaligenes faecalis
-
-
-
Manually annotated by BRENDA team
no activity in Anabaena variabilis ATCC 29413
-
-
-
Manually annotated by BRENDA team
no activity in Bacillus subtilis
-
-
-
Manually annotated by BRENDA team
no activity in Bacillus subtilis subsp. subtilis
-
-
-
Manually annotated by BRENDA team
no activity in Bacillus subtilis subsp. subtilis NCIB 3610
-
-
-
Manually annotated by BRENDA team
no activity in Diplococcus pneumoniae
-
-
-
Manually annotated by BRENDA team
no activity in Enterobacter aerogenes
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia coli
-
-
-
Manually annotated by BRENDA team
no activity in Klebsiella pneumoniae
-
-
-
Manually annotated by BRENDA team
no activity in Micrococcus tetragenus
-
-
-
Manually annotated by BRENDA team
no activity in Moraxella catarrhalis
-
-
-
Manually annotated by BRENDA team
no activity in Mycobacterium phlei
-
-
-
Manually annotated by BRENDA team
no activity in Prochlorococcus marinus
-
-
-
Manually annotated by BRENDA team
no activity in Prochlorococcus marinus MED 4
-
-
-
Manually annotated by BRENDA team
no activity in Prochlorococcus marinus MIT 9211
-
-
-
Manually annotated by BRENDA team
no activity in Prochlorococcus marinus MIT 9312
-
-
-
Manually annotated by BRENDA team
no activity in Prochlorococcus marinus MIT 9313
-
-
-
Manually annotated by BRENDA team
no activity in Prochlorococcus marinus NATL 2A
-
-
-
Manually annotated by BRENDA team
no activity in Prochlorococcus marinus SS 120
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas aeruginosa
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas putida
-
-
-
Manually annotated by BRENDA team
no activity in Pseudomonas putida T1
-
-
-
Manually annotated by BRENDA team
no activity in Serratia marcescens
-
-
-
Manually annotated by BRENDA team
no activity in Shigella flexneri
-
-
-
Manually annotated by BRENDA team
no activity in Staphylococcus aureus
-
-
-
Manually annotated by BRENDA team
no activity in Staphylococcus epidermidis
-
-
-
Manually annotated by BRENDA team
no activity in Streptococcus viridans
-
-
-
Manually annotated by BRENDA team
no activity in Synechococcus sp.
-
-
-
Manually annotated by BRENDA team
no activity in Synechococcus sp. CC9902
-
-
-
Manually annotated by BRENDA team
no activity in Synechococcus sp. JA-2-3B'a(2-13)
-
-
-
Manually annotated by BRENDA team
no activity in Synechococcus sp. JA-3-3Ab
-
-
-
Manually annotated by BRENDA team
no activity in Synechococcus sp. RS9917
-
-
-
Manually annotated by BRENDA team
no activity in Synechococcus sp. WH 8102
-
-
-
Manually annotated by BRENDA team
no activity in Thermosynechococcus elongatus BP-1
-
-
-
Manually annotated by BRENDA team
-
A8QL50
UniProt
Manually annotated by BRENDA team
king cobra
-
-
Manually annotated by BRENDA team
30 different strains
-
-
Manually annotated by BRENDA team
Taiwan habu snake
-
-
Manually annotated by BRENDA team
10 different strains
-
-
Manually annotated by BRENDA team
PCM 1298
-
-
Manually annotated by BRENDA team
Providencia sp. PCM 1298
PCM 1298
-
-
Manually annotated by BRENDA team
isolated from the encrusting pore coral Montipora aequituberculata from the Kenting coast of Southern Taiwan
-
-
Manually annotated by BRENDA team
Pseudoalteromonas flavipulchra C2
isolated from the encrusting pore coral Montipora aequituberculata from the Kenting coast of Southern Taiwan
-
-
Manually annotated by BRENDA team
strain CPMOR-1; strain CPMOR-2; strain NCIMB 1893T
-
-
Manually annotated by BRENDA team
Pseudoalteromonas luteoviolacea CPMOR-1
strain CPMOR-1
-
-
Manually annotated by BRENDA team
Pseudoalteromonas luteoviolacea CPMOR-2
strain CPMOR-2
-
-
Manually annotated by BRENDA team
Pseudoalteromonas luteoviolacea NCIMB 1893T
strain NCIMB 1893T
-
-
Manually annotated by BRENDA team
DSM 43250; DSM 43250, one of the best L-AAO producer
SwissProt
Manually annotated by BRENDA team
lao-gene; DSM 43250 strain
SwissProt
Manually annotated by BRENDA team
Rhodococcus sp. AIU Z-35-1
-
-
-
Manually annotated by BRENDA team
-
A1IGW6
SwissProt
Manually annotated by BRENDA team
Synechococcus cedrorum PCC 6908
-
-
-
Manually annotated by BRENDA team
Synechococcus leopoliensis (blue-green algae)
-
-
Manually annotated by BRENDA team
captured in northwest Bulgaria, five LAAO isozymes
-
-
Manually annotated by BRENDA team
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.02
-
L-Ala
-
pH 7.5, 0.9% NaCl, at 25C
12025
0.94
-
L-Arg
-
pH 7.5, 0.9% NaCl, at 25C
12085
3.72
-
L-Ile
-
pH 7.5, 0.9% NaCl, at 25C
12263
21.53
-
L-Leu
-
pH 7.5, 0.9% NaCl, at 25C
12275
195
-
L-leucine
-
in 50 mM Tris-HCl buffer pH 8.0, at 37C
12291
0.03
-
L-Lys
-
pH 7.5, 0.9% NaCl, at 25C
12303
21.93
-
L-Met
-
pH 7.5, 0.9% NaCl, at 25C
12324
41.3
-
L-Phe
-
pH 7.5, 0.9% NaCl, at 25C
12354
18.02
-
L-Trp
-
pH 7.5, 0.9% NaCl, at 25C
12438
40.56
-
L-Tyr
-
pH 7.5, 0.9% NaCl, at 25C
12441
0.11
-
L-Val
-
pH 7.5, 0.9% NaCl, at 25C
12462
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01189
-
2-aminobenzoic acid
-
isoform L2, free enzyme
0.02544
-
2-aminobenzoic acide
-
isoform L2, enzyme-substrate complex
-
1.7
-
Benzoate
-
-
11
-
D-mandelate
-
-
4.5
-
Gly
Q8VPD4
pH 7.6, 30C
4.5
-
glycine
Q8VPD4
pH 7.6, 30C
221
-
L-alanine
Q8VPD4
recombinant L-AAO, expressed in and Streptomyces lividans, 30C, pH 7.6
5.42
-
L-Arg
Q8VPD4
pH 7.6, 30C
5.42
-
L-arginine
Q8VPD4
pH 7.6, 30C
20.6
-
L-citrulline
Q8VPD4
pH 7.6, 30C; pH 7.6, 30C
5.69
-
L-Leu
Q8VPD4
pH 7.6, 30C
5.69
-
L-leucine
Q8VPD4
pH 7.6, 30C
63.7
-
L-Lys
Q8VPD4
pH 7.6, 30C
63.7
-
L-lysine
Q8VPD4
pH 7.6, 30C
11
-
L-Mandelate
-
-
6.84
-
L-Met
Q8VPD4
pH 7.6, 30C
6.84
-
L-methionine
Q8VPD4
pH 7.6, 30C
2.91
-
L-Norleucine
Q8VPD4
pH 7.6, 30C; pH 7.6, 30C
12.5
-
L-Orn
Q8VPD4
pH 7.6, 30C
12.5
-
L-ornithine
Q8VPD4
pH 7.6, 30C
2.28
-
L-Phe
Q8VPD4
pH 7.6, 30C
2.28
-
L-phenylalanine
Q8VPD4
pH 7.6, 30C
7.49
-
L-Propargylglycine
-
in 20 mM Na-phosphate, pH 7.5, at 28C
9.69
-
L-Propargylglycine
-
in 20 mM Na-phosphate, pH 7.5, at 28C
192
-
L-Ser
Q8VPD4
pH 7.6, 30C
192
-
L-serine
Q8VPD4
pH 7.6, 30C
1.06
-
L-Tyr
Q8VPD4
pH 7.6, 30C
1.06
-
L-tyrosine
Q8VPD4
pH 7.6, 30C
1.6
-
m-Aminobenzoate
-
-
0.15
-
m-chlorobenzoate
-
-
0.37
-
m-fluorobenzoate
-
-
2.1
-
m-Hydroxybenzoate
-
-
0.3788
-
N-acetyl-L-tryptophan amide
-
isoform L2, free enzyme
0.3846
-
N-acetyl-L-tryptophan amide
-
isoform L1, enzyme-substrate complexe
0.5916
-
N-acetyl-L-tryptophan amide
-
isoform L1, free enzyme
0.7448
-
N-acetyl-L-tryptophan amide
-
isoform L2, enzyme-substrate complex
0.0935
-
N-acetyltryptophan
-
isoform L1, enzyme-substrate complex
0.1146
-
N-acetyltryptophan
-
isoform L2, free enzyme
0.1275
-
N-acetyltryptophan
-
isoform L1, free enzyme
0.2001
-
N-acetyltryptophan
-
isoform L2, enzyme-substrate complex
0.42
-
o-aminobenzoate
-
-
1
-
o-chlorobenzoate
-
-
1.4
-
o-fluorobenzoate
-
-
2.2
-
o-hydroxybenzoate
-
-
1
-
o-mercaptobenzoate
-
-
0.86
-
o-Nitrobenzoate
-
-
1.2
-
orthanilic acid
-
-
1.4
-
p-Aminobenzoate
-
-
0.7
-
p-Chlorobenzoate
-
-
1.3
-
p-fluorobenzoate
-
-
2.3
-
p-hydroxybenzoate
-
-
2.3
-
p-nitrobenzoate
-
-
0.34
-
m-Nitrobenzoate
-
-
additional information
-
additional information
Q8VPD4
wild-type L-AAO, no substrate inhibition up to 0.5 M L-alanine
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.1
-
CaCl2
Synechococcus cedrorum PCC 6908, Synechococcus elongatus PCC 7942
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
12
-
half maximal activity at pH 3.5 and 12
4
11
Q8VPD4
L-phenylalanine as substrate, pH 4: ca. 10% of the activity, pH 11: ca. 60% of the activity
4.5
10.5
Bacillus carotarum
-
-
4.5
10.5
Q8VPD4
L-alanine as substrate, pH 4.5, ca. 3% of the activity, pH 10.5, ca. 30% of the activity
4.5
8.5
-, Q6IWZ0
pH-profile, overview
5.5
8.5
-
activity assay range
6
10
Hebeloma sp.
-
-
7
9
-
about 55% activity at pH 7.0, about 85% activity at pH 9.0
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
37
-
almost inactive at 0C and 37C
35
45
-
decrease of activity to 35-50% and 90-78% of maximal activity at 20-30C and 45-50C, respectively
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
9
-
the enzyme is stable at pH 6.0-8.0 (90% activity) and less stable at both pH 4.0-5.5 (less than 40% of maximal activity) and pH 9.0 (77% of maximal activity)
4
-
-
at a pH below 4, enzymatic activity is completely lost
5
-
-
4C, 24 h, complete inactivation
5.5
7
-
40C, 60 min, loss of about 20-30% activity
6.5
8.8
-
both isoforms retain 100% activity, drastic inactivation above and below this range
7
8
-
4C, 24 h, stable
7
8.5
-
40C, 60 min, highly stable
7
-
-
reversible inactivation: at pH near neutrality change into inactive configuration, regaining of active configuration on lowering the pH, monovalent anions, substrate and substrate analogs prevent inactivation
7
-
-
at pH above neutrality reversible inactivation
9
-
-
25C, 1 h stable; 25C, 5 min, 47% loss of activity, complete loss of activity after 30 min
9
-
-
unstable at
10
-
-
4C, 24 h, complete inactivation
additional information
-
-
slow reversible and temperature-dependent transition to an inactive form under alkaline conditions
additional information
-
-
protection by acetate (high concentration) and some aliphatic and aromatic monocarboxylic acids at pH 9.0
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
resistant against tryptic digest
-, Q6T277
2-mercaptoethanol stabilizes
-
KCl stabilizes
-
acetate at high concentrations increases pH-stability at pH 9
-
aliphatic and aromatic monocarboxylic acids protect at pH 9.0
-
freezing, inactivation between -5C and -60C, maximal inactivation at -20C, rate of inactivation is dependent on pH of storage, in most cases complete reactivation by heating at pH 5, inactivation not prevented by monovalent cations
-
freezing, quick freezing with dry ice/acetone mixture and storage at -15C for 60 h, enzyme loses 33% of activity, complete reactivation by heating at pH 5, inactivation not prevented by monovalent cations
-
freezing, quick freezing with dry ice/acetone mixture and storage at -15C for 60 h, enzyme is stable
-
freezing, irreversible inactivation
-
irreversible inactivation by lyophilization
-
stability of enzyme in immobilized whole cells
-
freezing at -18C without addition of glycerol inactivates the enzyme
Q8VPD4
stability of the enzyme can be increased by storage or incubation of the enzyme in glycine/NaOH buffer
Q8VPD4
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
loss of function mutants reverse the areA102 phenotype that results in pleiotropic effects on nitrogen utilization, areA102 encodes a GATA transkription factor. Elevated enzyme expression in an areA102 background accounts for the strong growth of these strains on amino acids that are substrates for the enzyme
additional information
-
gln-1bR8, mutant altered in the regulation of L-amino acid oxidase
additional information
-
development of a simple enzymatic method for production of a wide variety of D-amino acids using L-amino acid oxidase from Rhodococcus sp. AIU Z-35-1, overview
additional information
Rhodococcus sp. AIU Z-35-1
-
development of a simple enzymatic method for production of a wide variety of D-amino acids using L-amino acid oxidase from Rhodococcus sp. AIU Z-35-1, overview
-
additional information
-
an aaoSo mutant loses H2O2 formation from L-amino acids. Inhibition by Streptococcus oligofermentans of Streptococcus mutans in a peptone-rich mixed-species biofilm is greatly reduced