Information on EC 1.4.1.5 - L-amino-acid dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.4.1.5
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RECOMMENDED NAME
GeneOntology No.
L-amino-acid dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an L-amino acid + H2O + NAD+ = a 2-oxo carboxylate + NH3 + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidative deamination
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redox reaction
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SYSTEMATIC NAME
IUBMB Comments
L-amino-acid:NAD+ oxidoreductase (deaminating)
Acts on aliphatic amino acids.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-13-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
PCC 6803
UniProt
Manually annotated by BRENDA team
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 + NAD+
? + NH3 + NADH
show the reaction diagram
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-
-
?
L-alanine + H2O + NAD+
? + NH3 + NADH
show the reaction diagram
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-
-
?
L-Amino acid + H2O + NAD+
2-Oxo acid + NH3 + NADH
show the reaction diagram
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aliphatic amino acids, e.g. L-valine, L-leucine, L-isoleucine
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-
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L-Amino acid + H2O + NAD+
?
show the reaction diagram
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-
-
-
-
L-arginine + H2O + NAD+
? + NH3 + NADH
show the reaction diagram
-
-
-
?
L-cysteine + H2O + NAD+
3-mercapto-2-oxopropanoate + NH3 + NADH
show the reaction diagram
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
show the reaction diagram
-
-
-
?
L-glutamine + H2O + NAD+
2-oxoglutaramate + NH3 + NADH
show the reaction diagram
L-histidine + H2O + NAD+
3-(1H-imidazol-4-yl)-2-oxopropanoate + NH3 + NADH
show the reaction diagram
-
-
-
?
L-isoleucine + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
show the reaction diagram
L-leucine + H2O + NAD+
? + NH3 + NADH
show the reaction diagram
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-
-
?
L-Lysine + H2O + NAD+
? + NH3 + NADH
show the reaction diagram
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-
-
?
L-methionine + H2O + NAD+
(4-methylsulfanyl)-2-oxobutanoate + NH3 + NADH
show the reaction diagram
L-ornithine + H2O + NAD+
? + NH3 + NADH
show the reaction diagram
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH
show the reaction diagram
-
-
-
?
L-proline + H2O + NAD+
? + NH3 + NADH
show the reaction diagram
-
-
-
?
L-serine + H2O + NAD+
3-hydroxy-2-oxopropanoate + NH3 + NADH
show the reaction diagram
L-threonine + H2O + NAD+
3-hydroxy-2-oxopropanoate + NH3 + NADH
show the reaction diagram
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-
-
?
L-tryptophan + H2O + NAD+
3-(1H-indol-3-yl)-2-oxopropanoate + NH3 + NADH
show the reaction diagram
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-
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?
L-tyrosine + H2O + NAD+
(4-hydroxyphenyl)pyruvate + NH3 + NADH
show the reaction diagram
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-
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?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + NAD+
?
show the reaction diagram
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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MgCl2
0.5 mM stimulate activity by 1.7fold
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
0.03 mM, 50% inhibition
CaCl2
0.09 mM, 50% inhibition
CoCl2
0.11 mM, 50% inhibition
dipyridyl
0.01 mM, 50% inhibition
KCN
0.1 mM, 50% inhibition
MgCl2
2 mM inhibits enzymatic activity by 50%, 10 mM MgCl2 completely inhibits enzymatic activity
NaCl
8 mM, 50% inhibition
NaN3
0.1 mM, 50% inhibition
NiCl2
0.09 mM, 50% inhibition
o-phenanthroline
0.05 mM, 50% inhibition
Salicylhydroxamic acid
0.02 mM, 50% inhibition
SrCl2
0.13 mM, 50% inhibition
ZnCl2
0.2 mM, 50% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2
L-arginine
pH 8.5
0.012
L-glutamine
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in 100 mM glycine-KCl-KOH buffer (pH 10.4)
0.025 - 2.2
L-isoleucine
0.034
L-methionine
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in 100 mM glycine-KCl-KOH buffer (pH 10.4)
0.044 - 25
L-valine
0.16 - 33
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.15
L-glutamine
Proteus sp.
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in 100 mM glycine-KCl-KOH buffer (pH 10.4)
2.84
L-isoleucine
Citrobacter sp.
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in 100 mM glycine-KCl-KOH buffer (pH 10.4)
2.11
L-methionine
Proteus sp.
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in 100 mM glycine-KCl-KOH buffer (pH 10.4)
4.95
L-valine
Pseudomonas sp.
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in 100 mM glycine-KCl-KOH buffer (pH 10.4)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.47
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using L-valine, L-cysteine, L-serine, or L-glutamine as substrate, in 100 mM glycine-KCl-KOH buffer (pH 10.4)
0.7
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using L-glutamine as substrate, in 100 mM glycine-KCl-KOH buffer (pH 10.4)
0.73
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using L-cysteine, L-serine, or L-glutamine as substrate, in 100 mM glycine-KCl-KOH buffer (pH 10.4)
1.2
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using L-methionine as substrate, in 100 mM glycine-KCl-KOH buffer (pH 10.4)
1.59
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using L-isoleucine as substrate, in 100 mM glycine-KCl-KOH buffer (pH 10.4)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.7
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L-valine, L-isoleucine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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resting
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51400
deduced from amino acid sequence
290000
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gel filtration
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
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10 min, 25-35% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
slot-blot RNA-DNA hybridization experiments show that the slr0782 mRNA level increases, when cells are grown with L-arginine as compared to the growth of cells with nitrate