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Enzyme Nomenclature
Information on EC 1.4.1.1 - alanine dehydrogenase
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
1.4.1.1
-
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RECOMMENDED NAME
GeneOntology No.
alanine dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
reductive amination: sequential mechanism with partially random binding
-
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
reductive amination proceeds through a sequential mechanism containing partially random binding. NADH binds first to the enzyme, and then pyruvate and ammonia bind in a random fashion
-
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
predominantly ordered kinetic mechanism in which NAD+ adds before L-Ala, and ammonia, pyruvate, and NADH are released in that order
-
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
sequential ordered ternary-binary mechanism, the enzyme is A-stereospecific, the pro-R hydrogen at C-4 of the reduced nicotinamide ring of NADH is exclusively transferred to pyruvate
-
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
the kinetic mechanism at pH 8.5 is determined to be ter-bi Theorell-Chance. In the amination direction, the substrates add in the order: NADH, NH4+, pyruvate, with NH4+ binding in rapid-equilibrium. In the reverse direction, NAD adds first followed by L-Ala
-
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
oxidative deamination proceeds by an random-ordered mechanism
-
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
sequential ordered binary-ternary mechanism. NAD+ binds first to the enzyme, followed by L-Ala. The products are released in the order: NH4+, pyruvate and NADH
-
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive amination
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-alanine:NAD+ oxidoreductase (deaminating)
-
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CAS REGISTRY NUMBER
COMMENTARY
9029-06-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
screening of thermostable alanine dehydrogenase in thermophilic Bacillus strains
-
-
glycine and alanine dehydrogenase activities are catalyzed by the same proteon in Mycobacterium smegamatis
-
-
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12940, 349549, 349555, 349556, 349559, 349560, 349562, 349563, 349568, 349580, 349585, 349587, 349590, 349593, 349597, 349598, 349599, 671289, 684793, 741751, 742134
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Uniprot
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
malfunction
-
an ald knockout strain grows without alanine or glycine and is able to utilize glycine but not alanine as a nitrogen source
malfunction
-
an ald knockout strain grows without alanine or glycine and is able to utilize glycine but not alanine as a nitrogen source
-
physiological function
-
the enzyme is involved in the alanine catabolism in the heterocysts, that is needed for normal diazotrophic growth
physiological function
-
the enzyme plays an important role in the carbon and nitrogen metabolism of microorganisms, it iis a key factor in assimilation of L-Ala as energy source through TCA cycle
physiological function
-
enzyme Ald may have several functions, including ammonium incorporation and alanine breakdown. Ald plays an essential role in the utilization of alanine but not of glycine. Ald is not essential for the breakdown of glycine
physiological function
-
both mRNA levels and enzymatic activities of isocitrate lyase, and alanine dehydrogenase increases during entry into nonreplicating persistence. Expression of alanine dehydrogenase is also induced in vitro by persistence-inducing stresses such as nitric oxide, and the gene is expressed at high levels in vivo during the initial lung infection in mice. Enzyme activity is maintained during extended hypoxia even after transcription levels decrease. A knockout mutant shows no reduction in anaerobic survival in vitro, but results in a significant lag in the resumption of growth after reoxygenation. During reactivation the mutant has an altered NADH/NAD ratio
physiological function
abundance and activity profiles of alanine dehydrogenase concomitantly increase with the onset of enhanced alanine utilization during transition into stationary growth phase
physiological function
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the enzyme is involved in the alanine catabolism in the heterocysts, that is needed for normal diazotrophic growth
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physiological function
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both mRNA levels and enzymatic activities of isocitrate lyase, and alanine dehydrogenase increases during entry into nonreplicating persistence. Expression of alanine dehydrogenase is also induced in vitro by persistence-inducing stresses such as nitric oxide, and the gene is expressed at high levels in vivo during the initial lung infection in mice. Enzyme activity is maintained during extended hypoxia even after transcription levels decrease. A knockout mutant shows no reduction in anaerobic survival in vitro, but results in a significant lag in the resumption of growth after reoxygenation. During reactivation the mutant has an altered NADH/NAD ratio; enzyme Ald may have several functions, including ammonium incorporation and alanine breakdown. Ald plays an essential role in the utilization of alanine but not of glycine. Ald is not essential for the breakdown of glycine
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physiological function
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abundance and activity profiles of alanine dehydrogenase concomitantly increase with the onset of enhanced alanine utilization during transition into stationary growth phase
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additional information
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alanine is transported from vegetative cells into heterocysts in the diazotrophic Anabaena filament
additional information
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alanine is transported from vegetative cells into heterocysts in the diazotrophic Anabaena filament
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-bromopyruvate + NH3 + NADH
2-amino-3-bromopropanoate + NAD+ + H2O
-
5.3% of the activity with pyruvate
-
-
?
3-fluoropyruvate + NH3 + NADH + H+
3-fluoro-L-alanine + H2O + NAD+
-
-
-
-
?
3-hydroxypyruvate + NH3 + NADH
Ser + H2O + NAD+
-
15.4% of the activity with pyruvate
-
-
?
L-Ala + H2O + 3-pyridinealdehyde-NAD+
?
-
5.0% of the activity with NAD+
-
-
?
L-homophenylalanine + H2O + NADH + H+
2-oxo-4-phenylbutanoate + NH3 + NAD+
-
-
-
-
?
L-homoserine + H2O + NAD+
4-hydroxy-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-isoleucine + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH + H+
-
-
-
-
r
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-methionine + H2O + NAD+
4-(methylsulfanyl)-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-norleucine + H2O + NADH + H+
2-oxohexanoate + NH3 + NAD+
-
-
-
-
?
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + NH3 + NADH + H+
-
-
-
-
r
L-threonine + H2O + NAD+
3-hydroxy-2-oxobutyrate + NH3 + NADH + H+
-
-
-
-
r
pyruvate + NH3 + NADH
L-Ala + NAD+ + H2O
-
primary route for alanine synthesis in isolated bacteroids, alanine synthesis and secretion contributes to the efficiency of N2-fixation and therefore biomass accumulation
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-
?
pyruvate + NH3 + NADPH + H+
L-Ala + H2O + NADP+
-
NADPH is a poor cofactor for wild-type
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
-
-
-
r
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
-
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
-
-
-
r
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
62% of the activity with pyruvate
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
4.1% of the activity with pyruvate
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
no activity
-
-
-
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
3.7% of the activity with pyruvate
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
15% of maximal activity
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
15.8% of the activity with pyruvate
-
-
?
2-oxoglutarate + NH3 + NADH
L-Gln + NAD+ + H2O
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11.7% of the activity with pyruvate
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-
?
3-fluoropyruvate + NH3 + NADH
3-fluoro-L-alanine + H2O + NAD+
-
-
-
?
3-fluoropyruvate + NH3 + NADH
3-fluoro-L-alanine + H2O + NAD+
-
97% of the activity with pyruvate
-
-
?
3-fluoropyruvate + NH3 + NADH
? + H2O + NAD+
O85596
74% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
123% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
6.9% of the activity with pyruvate
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-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
32.3% of the activity with pyruvate
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-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
O85596
54% of the activity with pyruvate
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-
?
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
1.6% of the activity with pyruvate
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-
?
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
-
-
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-
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
-
-
-
?
D-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
32.3% of the activity with L-Ala
-
-
?
D-Ala + H2O + NAD+
pyruvate + NH3 + NADH
3.5% of the activity with L-Ala
-
-
?
D-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
1.3% of the activity with L-Ser
-
-
?
D-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
4.4% of the activity with L-Ala
-
r
D-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
in the reverse reaction the enzyme reacts at 9.3% of the activity with pyruvate
-
r
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
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6.2% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
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1.2% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
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5.6% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
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13.3% of the activity with pyruvate
-
-
?
L-2-amino-4-pentenoate + H2O + NAD+
2-oxo-4-pentenoate + NH3 + NADH
-
-
-
-
?
L-2-amino-4-pentenoate + H2O + NAD+
2-oxo-4-pentenoate + NH3 + NADH
-
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
13.3% of the activity with L-Ala
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
in the reverse reaction the enzyme reacts at 15.3% of the activity with pyruvate
-
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r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
10.4% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
7.5% of the activity with L-Ala
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
in the reverse reaction 2-oxobutanoate reacts with 79% of the activity with pyruvate
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
8.7% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
in the reverse reaction 2-oxobutanoate reacts with 2.0% of the activity with pyruvate
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
2.4% of the activity with L-Ala
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
in the reverse reaction 2-oxobutanoate reacts with 1.2% of the activity with pyruvate
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
0.7% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
1.6% of the activity with L-Ala
-
-
-
L-Ala + H2O + 1,N6-etheno-NAD+
pyruvate + NH3 + 1,N6-etheno-NADH
-
45% of the activity with NAD+
-
-
?
L-Ala + H2O + 1,N6-etheno-NAD+
pyruvate + NH3 + 1,N6-etheno-NADH
-
59% of the activity with NAD+
-
-
?
L-Ala + H2O + 3-acetylpyridine-NAD+
pyruvate + H2O + 3-acetylpyridine-NADH
-
as active as NAD+
-
-
?
L-Ala + H2O + 3-acetylpyridine-NAD+
pyruvate + H2O + 3-acetylpyridine-NADH
-
43% of the activity with NAD+
-
-
?
L-Ala + H2O + 3-acetylpyridine-NAD+
pyruvate + H2O + 3-acetylpyridine-NADH
-
62% of the activity with NAD+
-
-
?
L-Ala + H2O + deamino-NAD+
pyruvate + NH3 + deamino-NADH
-
90.2% of the activity with NAD+
-
-
?
L-Ala + H2O + deamino-NAD+
pyruvate + NH3 + deamino-NADH
-
4.4% of the activity with NAD+
-
-
?
L-Ala + H2O + deamino-NAD+
pyruvate + NH3 + deamino-NADH
-
77% of the activity with NAD+
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
highly specific for L-Ala
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
the physiological role is to catabolize L-Ala to pyruvate and NH3, inducible by L-Ala, D-Ala and 11 other D-amino acids. The enzyme catabolizes L-Ala, and thereby limits the amount of L-Ala available to alanine racemase for the synthesis of D-Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme is involved in primary ammonium assimilation and the rapid formation of key metabolites pyruvate and NH3 from L-Ala and also in cell differentiation
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
absolutely specific for L-Ala in oxidative deamination
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
highly specific for L-Ala
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
physiological role in nitrogen metabolism in Streptomycetes
-
-
-
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
the reaction rate for deamination of pyruvate at the optimum is about 2.8times higher than that for amination of L-Ala at the optimum
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
specific for L-Ala
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme is required for utilization of alanine as a sole nitrogen source, enzyme is required for optimal growth under anaerobic conditions
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
highly specific for L-Ala
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
since the physiological environment of the organism has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
Mycobacterium tuberculosis displays less Ald activity than the complemented Mycobacterium bovis BCG strain
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
key enzyme in the metabolism of alanine, Ala is onyl fermented after lactate exhaustion and then at a slow rate
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
rate of the deaminating reaction is only 2.2% of the aminating reaction
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
role in NH3 assimilation and alanine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
rate of the deaminating reaction is only 2.2% of the aminating reaction
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
role in NH3 assimilation and alanine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
no function in NH4+-assimilation but rather is required to supply the cells with the appropriate quantities of organic carbon when the organism grows at the expense of L-Ala as C-source and N-source
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
alternative route for ammonia assimilation when glutamine synthetase is inactivated
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
involved in taurine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme formation is effectively induced by Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
NH4+ assimilating enzyme
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
highly specific for L-Ala
-
r
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
7% of the activity with NAD+
-
-
?
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
in the reverse direction NADPH reacts at 1.6% of the activity with NADH
-
-
r
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
2.5% of the activity with NAD+
-
-
r
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
wild-type enzyme and mutant enzyme R199I acts specifically on NAD+, mutant enzyme I198R is also active with NADP+
-
-
?
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
wild-type enzyme shows high activity with NAD+ and low activity with NADP+. The mutant enzymes D198G, D198A, D198V and D198L show higher efficiency with NADP+ than with NAD+ as coenzyme
-
-
?
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
wild-type enzyme shows high activity with NAD+ and low activity with NADP+. The mutant enzymes D198G, D198A, D198V and D198L show higher efficiency with NADP+ than with NAD+ as coenzyme
-
-
?
L-Ala + H2O + nicotinamide guanine dinucleotide
?
-
59.9% of the activity with NAD+
-
-
?
L-Ala + H2O + nicotinamide guanine dinucleotide
?
-
69.7% of the activity with NAD+
-
-
?
L-Ala + H2O + nicotinamide guanine dinucleotide
?
-
71% of the activity with NAD+
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
?
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
-
5% of the activity with L-Ala
-
-
?
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
-
-
-
?
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
-
0.1% of the activity with L-Ala
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
at 4.6% of the activity with L-Ala
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
1.5% of the activity with L-Ala
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
in the reverse reaction 2-oxopentanoate reacts with 6.6% of the activity of pyruvate
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
in the reverse reaction 2-oxopentanoate reacts with 0.12% of the activity of pyruvate
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
7.9% of the activity with L-Ala
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
3.5% of the activity with L-Ala
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
in the reverse reaction 3-hydroxypyruvate reacts with 0.4% of the activity with pyruvate
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
in the reverse reaction 3-hydroxypyruvate reacts with 14.2% of the activity with pyruvate
-
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
4.1% of the activity with L-Ala
-
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
no activity
-
-
-
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
no activity
-
-
-
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
2.4% of the activity with L-Ala
-
-
-
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
9% of the activity with L-Ala
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
4.8% of the activity with L-Ala
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
1.5% of the activity with L-Ala
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
0.2% of the activity with L-Ala
-
-
?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
99% of the activity with pyruvate
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
94% of maximal activity
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
43.1% of the activity with pyruvate
-
-
?
pyruvate + NH3 + NADH
L-alanine + H2O + NAD+
the structural analysis leads to the identification of a water molecule which is hydrogen bonded to the active site His 96 and probably drives the conversion of the iminopyruvate intermediate to a carbinolamine
-
-
?
additional information
?
-
-
A–specific enzyme with regard to stereochemistry of the hydrogen transfer to NAD+
-
-
-
additional information
?
-
-
the enzyme is required for normal sporulation
-
-
-
additional information
?
-
-
transfer of hydride is a partially limiting step and the reaction rate is limited by the release of product NADH. The fluorine constituent doesn't cause a significant change in the area of bonds that are being converted, and deuteriated solvent present in the reaction medium only slightly affects the conversion of [E-S] complex into [E-P] complex
-
-
-
additional information
?
-
-
enzyme is involved in taurine metabolism
-
-
-
additional information
?
-
enzyme is involved in taurine metabolism
-
-
-
additional information
?
-
-
circadian oscillations in alanine dehydrogenase
-
-
-
additional information
?
-
-
circadian oscillations in alanine dehydrogenase
-
-
-
additional information
?
-
-
strong induction immediately after deflection from aerobic growth suggests that alanine dehydrogenase may be required for the adaption from aerobic growth to anaerobic dormacy, the induction of alanine dehydrogenase may also support the maintenance of the NAD+ pool when oxygen as the terminal electron acceptor becomes limiting
-
-
-
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
-
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
-
additional information
?
-
the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction
-
-
?
additional information
?
-
the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction
-
-
?
additional information
?
-
-
important role in biosynthesis of erythromycin
-
-
-
additional information
?
-
-
enzyme activity during production phase of the antibiotic A 6599, enzyme induction by an excess of alanine or ammonia
-
-
-
additional information
?
-
-
substrate specifiicty, overview. The enzyme is also active with substrates DL-alanine, L-serine, L-isoleucine, L-threonine, and glycine, with L-serine giving the highest activity rate
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-isoleucine + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH + H+
-
-
-
-
r
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + NH3 + NADH + H+
-
-
-
-
r
L-threonine + H2O + NAD+
3-hydroxy-2-oxobutyrate + NH3 + NADH + H+
-
-
-
-
r
pyruvate + NH3 + NADH
L-Ala + NAD+ + H2O
-
primary route for alanine synthesis in isolated bacteroids, alanine synthesis and secretion contributes to the efficiency of N2-fixation and therefore biomass accumulation
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
the physiological role is to catabolize L-Ala to pyruvate and NH3, inducible by L-Ala, D-Ala and 11 other D-amino acids. The enzyme catabolizes L-Ala, and thereby limits the amount of L-Ala available to alanine racemase for the synthesis of D-Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme is involved in primary ammonium assimilation and the rapid formation of key metabolites pyruvate and NH3 from L-Ala and also in cell differentiation
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
physiological role in nitrogen metabolism in Streptomycetes
-
-
-
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme is required for utilization of alanine as a sole nitrogen source, enzyme is required for optimal growth under anaerobic conditions
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
since the physiological environment of the organism has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
key enzyme in the metabolism of alanine, Ala is onyl fermented after lactate exhaustion and then at a slow rate
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
role in NH3 assimilation and alanine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
role in NH3 assimilation and alanine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
no function in NH4+-assimilation but rather is required to supply the cells with the appropriate quantities of organic carbon when the organism grows at the expense of L-Ala as C-source and N-source
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
alternative route for ammonia assimilation when glutamine synthetase is inactivated
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
Q5LX18
involved in taurine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme formation is effectively induced by Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
NH4+ assimilating enzyme
-
-
?
additional information
?
-
-
the enzyme is required for normal sporulation
-
-
-
additional information
?
-
-
enzyme is involved in taurine metabolism
-
-
-
additional information
?
-
Q9AIK2
enzyme is involved in taurine metabolism
-
-
-
additional information
?
-
-
circadian oscillations in alanine dehydrogenase
-
-
-
additional information
?
-
-
circadian oscillations in alanine dehydrogenase
-
-
-
additional information
?
-
-
strong induction immediately after deflection from aerobic growth suggests that alanine dehydrogenase may be required for the adaption from aerobic growth to anaerobic dormacy, the induction of alanine dehydrogenase may also support the maintenance of the NAD+ pool when oxygen as the terminal electron acceptor becomes limiting
-
-
-
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
-
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
-
additional information
?
-
Q9RLB2
the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction
-
-
?
additional information
?
-
Q9RLB3
the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction
-
-
?
additional information
?
-
-
important role in biosynthesis of erythromycin
-
-
-
additional information
?
-
-
enzyme activity during production phase of the antibiotic A 6599, enzyme induction by an excess of alanine or ammonia
-
-
-
additional information
?
-
-
substrate specifiicty, overview. The enzyme is also active with substrates DL-alanine, L-serine, L-isoleucine, L-threonine, and glycine, with L-serine giving the highest activity rate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
independent of cytochrome c, assayed with ferricyanide as an electron acceptor
-
NAD+
wild-type enzyme and mutant enzyme R199I acts specifically on NAD+, mutant enzyme I198R is also active with NADP+
NAD+
-
wild-type enzyme shows high activity with NAD+ and low activity with NADP+. The mutant enzymes D198G, D198A, D198V and D198L show higher efficiency with NADP+ than with NAD+ as coenzyme
NAD+
-
affinity for NAD+ immobilized through an N6 linkage, as opposed to an N1 linkage, replacement of the nitrogen with sulfur to produce an S6 linkage
NAD+
-
-
12940, 349549, 349555, 349556, 349559, 349560, 349562, 349563, 349568, 349580, 349585, 349587, 349590, 349593, 349597, 349598, 349599, 684793
NADH
-
-
12940, 349549, 349555, 349556, 349559, 349560, 349562, 349563, 349568, 349580, 349585, 349587, 349590, 349593, 349597, 349598, 349599, 705545, 705546, 742134
NADP+
wild-type enzyme and mutant enzyme R199I acts specifically on NAD+, mutant enzyme I198R is also active with NADP+
NADP+
-
wild-type enzyme shows high activity with NAD+ and low activity with NADP+. The mutant enzymes D198G, D198A, D198V and D198L show higher efficiency with NADP+ than with NAD+ as coenzyme
nicotinamide guanine dinucleotide
-
59.9% of the activity with NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cs+
KCl
Li+
NaCl
additional information
Cs+
-
reductive amination is activated equally well by K+, Na+ or NH4+ and to a lesser extent with Cs+ or Li+
KCl
-
reductive amination is activated equally well by K+, Na+ or NH4+ and to a lesser extent with Cs+ or Li+, absolute requirement for K+ in oxidative deamination, completely inactive with Na+ or NH4+
Li+
-
reductive amination is activated equally well by K+, Na+ or NH4+ and to a lesser extent with Cs+ or Li+
NaCl
-
reductive amination is activated equally well by K+, Na+ or NH4+ and to a lesser extent with Cs+ or Li+
additional information
-
highest activation by Cl-, much smaller effect occurs in presence of Br-, nitrate, or sulfate
additional information
-
absolute requirement for high ionic strength for optimum activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(isonicotinamido)-N2,N4-bis(benzo[d]thiazol-2-yl)azetidine-2,4-dicarboxamide
-
compound shows 100fold reduction in nutrient starved dormant Mycobacterium tuberculosis model and MIC of 11.81 microM in actively replicative Mycobacterium tuberculosis
1-(isonicotinamido)-N2,N4-bis(phenyl)azetidine-2,4-dicarboxamide
-
lead compound for inhibitor screening, involved in hydrophobic interactions with residues Pro242, Val241, Ala176, Leu130, Ile267, Ala179, Ile199 and Ile174
2,4,6-Trinitrobenzenesulfonic acid
-
inactivation follows pseudo first-order kinetics with a 1:1 stoichiometric ratio between the reagent and the enzyme subunit. Partial protection by each of the substrates, NADH or pyruvate. Complete protection only in presence of the ternary complex enzyme-NADH-pyruvate
3-(2-pyridyldithio)propionate
-
inactivation follows pseudo first-order kinetics with a 1:1 stoichiometric ratio between the reagent and the enzyme subunit. Partial protection by each of the substrates, NADH or pyruvate. Complete protection only in presence of the ternary complex enzyme-NADH-pyruvate
5'-(p-(fluorosulfonyl)-benzoyl)adenosine
-
inactivation follows pseudo-first-order kinetics, complete inactivation of the enzyme can not be obtained even at high reagent concentration
5-(4-(benzyloxy)benzylidene)-3-(2,5-dimethylphenyl)-2-iminothiazolidin-4-one
-
compound shows potency, selectivity, and no cytotoxicity up to 50 microM in a mouse macrophage cell line
5-(4-(benzyloxy)benzylidene)-3-(2,6-dimethylphenyl)-2-iminothiazolidin-4-one
-
compound shows potency, selectivity, and no cytotoxicity up to 50 microM in a mouse macrophage cell line
6-acetyl-2-(4-chlorobenzamido)-4,5,6,7-tetrahydrothieno[2,3-c]pyridine-3-carboxamide
-
compound shows potency, selectivity, and no cytotoxicity up to 50 microM in a mouse macrophage cell line
p-hydroxymercuribenzoate
-
no effect on aminating activity, inhibition of deaminating activity
tert-butyl 3-carbamoyl-2-(4-chlorobenzamido)-4,5-dihydrothieno[2,3-c]pyridine-6(7H)-carboxylate
-
compound shows potency, selectivity, and no cytotoxicity up to 50 microM in a mouse macrophage cell line
CuSO4
-
50.7% inhibition by 1 mM, 96.3% inhibition by 20 mM, EDTA in a 10fold molar excess restores activity almost completely, recombinant enzyme
D-Ala
-
aminating reaction, competitive with respect to NADH, noncompetitive with respect to NH4+ and pyruvate
pyruvate
-
inhibition at pH 7.5 greater than at pH 9.5; product inhibition
Zn2+
-
allosteric competitive inhibitor, reversible, inducing conformational change through the intersubunit interaction, positive cooperative binding of the substrate in presence of Zn2+
Zn2+
-
26.5% inhibition by 1 mM ZnCl2, 90.1% inhibition by 20 mM ZnCl2, EDTA in a 10fold molar excess restores activity almost completely, recombinant enzyme
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24
L-serine
-
wild-type, pH 10.2, temperature not specified in the publication
additional information
additional information
-
kinetics of ald and glyoxylate dehydrogenae activities, overview
-
15.64
L-Ala
-
wild type enzyme, in 125 mM glycine/KOH (pH 10.2), at 25°C
53
L-alanine
-
wild-type, pH 10.2, temperature not specified in the publication