BRENDA home
History
Information on EC 1.4.1.1 - alanine dehydrogenase
for references in articles please use BRENDA:EC1.4.1.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.4.1.1 alanine dehydrogenaseSpecify your search results
Word Map
- 1.4.1.1
- vkorc1
- cyp2c19
- cyp1a2
-
anticoagulation
- nicotine
-
smoking
-
interindividual
- cyp2d6
-
dosing
-
pharmacogenetic
- coumarin
- tolbutamide
-
s-warfarin
- phenytoin
-
drug-drug
- diclofenac
-
benzoapyrene
- cotinine
-
o-deethylase
-
concentration-time
-
7-hydroxylation
-
acenocoumarol
- beta-naphthoflavone
-
drug-metabolizing
- losartan
-
ethoxyresorufin-o-deethylase
-
ethoxyresorufin
-
cdna-expressed
-
procarcinogens
-
tobacco-related
- repaglinide
-
interethnic
- sulfaphenazole
- gemfibrozil
- alpha-naphthoflavone
-
dioxin-like
-
7-hydroxylase
-
tegafur
-
killifish
-
tobacco-specific
-
slco1b1
-
o-deethylation
- amodiaquine
- phenacetin
- s-mephenytoin
-
auc0-infinity
- 7-hydroxycoumarin
-
genotype-based
- phenprocoumon
- glimepiride
- biotechnology
- nutrition
- analysis
- medicine
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
(S)alanine dehydrogenase, (S)alanine:NAD oxidoreductase, 40 kDa antigen, ADH, AF1665, ALADH, alanine dehydrogenase, alanine oxidoreductase, ALD, AldA, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)alanine dehydrogenase
-
-
-
-
(S)alanine:NAD oxidoreductase
-
-
-
-
40 kDa antigen
-
-
-
-
ALADH
alanine dehydrogenase
alanine oxidoreductase
-
-
-
-
ALD
alpha-alanine dehydrogenase
-
-
-
-
dehydrogenase, alanine
-
-
-
-
L-AlaDH
L-alanine dehydrogenase
MtbALD
NAD-dependent alanine dehydrogenase
-
-
-
-
NAD-linked alanine dehydrogenase
-
-
-
-
NADH-dependent alanine dehydrogenase
-
-
-
-
PlaAlaDH
Rv2780
SheAlaDH
TB43
-
-
-
-
ALADH
-
-
-
-
L-alanine dehydrogenase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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+
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+
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+
reductive amination: sequential mechanism with partially random binding
-
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+
oxidative deamination proceeds by an random-ordered mechanism
-
L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive amination
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-alanine:NAD+ oxidoreductase (deaminating)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9029-06-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
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
-
11.7% of the activity with pyruvate
-
-
?
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+
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
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
32.3% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
54% of the activity with pyruvate
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
1.6% of the activity with pyruvate
-
-
?
D-Ala + H2O + NAD+
pyruvate + NH3 + NADH
3.5% of the activity with L-Ala
-
-
?
D-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
32.3% of the activity with L-Ala
-
-
?
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
D-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
1.3% of the activity with L-Ser
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
1.2% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
6.2% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
5.6% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
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
-
-
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
-
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
-
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
-
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 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-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
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-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
?
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
-
7.9% of the activity with L-Ala
-
-
?
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-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
-
-
?
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
?
-
-
Aâspecific 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
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
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
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
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
-
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
-
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
-
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
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-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
additional information
?
-
-
the enzyme is required for normal sporulation
-
-
?
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
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
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
?
-
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
-
-
?
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+
-
-
12940, 349549, 349555, 349556, 349559, 349560, 349562, 349563, 349568, 349580, 349585, 349587, 349590, 349593, 349597, 349598, 349599, 684793
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
NADH
-
-
12940, 349549, 349555, 349556, 349559, 349560, 349562, 349563, 349568, 349580, 349585, 349587, 349590, 349593, 349597, 349598, 349599, 705545, 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+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
absolute requirement for high ionic strength for optimum activity
additional information
-
highest activation by Cl-, much smaller effect occurs in presence of Br-, nitrate, or sulfate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
A blocking ELISA using a monoclonal antibody for the serological detection of Mycoplasma hyopneumoniae.
Starvation
Alanine dehydrogenase activity is required for adequate progression of phycobilisome degradation during nitrogen starvation in Synechococcus elongatus PCC 7942.
Starvation
Expression of an L-alanine dehydrogenase gene in Zymomonas mobilis and excretion of L-alanine.
Starvation
Identification of novel inhibitors against Mycobacterium tuberculosis L-alanine dehydrogenase (MTB-AlaDH) through structure-based virtual screening.
Tuberculosis
A study of combined filtration and adsorption on nylon-based dye-affinity membranes: separation of recombinant L-alanine dehydrogenase from crude fermentation broth.
Tuberculosis
ald of Mycobacterium tuberculosis encodes both the alanine dehydrogenase and the putative glycine dehydrogenase.
Tuberculosis
An inducible expression system for high-level expression of recombinant proteins in slow growing mycobacteria.
Tuberculosis
Bacterial luciferase is naturally destabilized in Mycobacterium tuberculosis and can be used to monitor changes in gene expression.
Tuberculosis
Contribution of L-alanine dehydrogenase to in vivo persistence and protective efficacy of the BCG vaccine.
Tuberculosis
Crystal Structure of Mycobacterium tuberculosis H37Rv AldR (Rv2779c), a Regulator of the ald Gene: DNA BINDING AND IDENTIFICATION OF SMALL MOLECULE INHIBITORS.
Tuberculosis
Crystal structures of the Mycobacterium tuberculosis secretory antigen alanine dehydrogenase (Rv2780) in apo and ternary complex forms captures 'open' and 'closed' enzyme conformations.
Tuberculosis
Domain Motions and Functionally-Key Residues of l-Alanine Dehydrogenase Revealed by an Elastic Network Model.
Tuberculosis
Extracellular enzyme activities potentially involved in the pathogenicity of Mycobacterium tuberculosis.
Tuberculosis
Flexible nitrogen utilisation by the metabolic generalist pathogen Mycobacterium tuberculosis.
Tuberculosis
HLA-A2-restricted CD8+-cytotoxic-T-cell responses to novel epitopes in Mycobacterium tuberculosis superoxide dismutase, alanine dehydrogenase, and glutamine synthetase.
Tuberculosis
Host vector system for high-level expression and purification of recombinant, enzymatically active alanine dehydrogenase of Mycobacterium tuberculosis.
Tuberculosis
Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins.
Tuberculosis
Identification of novel inhibitors against Mycobacterium tuberculosis L-alanine dehydrogenase (MTB-AlaDH) through structure-based virtual screening.
Tuberculosis
Isolation of a 43 kDa protein from Mycobacterium tuberculosis H37Rv and its identification as a pyridine nucleotide transhydrogenase.
Tuberculosis
Molecular dynamics simulations of mutated Mycobacterium tuberculosis L-alanine dehydrogenase to illuminate the role of key residues.
Tuberculosis
Molecular dynamics simulations of the coenzyme induced conformational changes of Mycobacterium tuberculosis L-alanine dehydrogenase.
Tuberculosis
Overexpression, purification, crystallization and preliminary X-ray analysis of Rv2780 from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Properties of the 40 kDa antigen of Mycobacterium tuberculosis, a functional L-alanine dehydrogenase.
Tuberculosis
Regulation Mechanism of the ald Gene Encoding Alanine Dehydrogenase in Mycobacterium smegmatis and Mycobacterium tuberculosis by the Lrp/AsnC Family Regulator AldR.
Tuberculosis
Role of Alanine Dehydrogenase of Mycobacterium tuberculosis during Recovery from Hypoxic Nonreplicating Persistence.
Tuberculosis
Serological markers of pulmonary tuberculosis and of response to anti-tuberculosis treatment in a patient population in Guinea.
Tuberculosis
Similarities between alanine dehydrogenase and the N-terminal part of pyridine nucleotide transhydrogenase and their possible implication in the virulence mechanism of Mycobacterium tuberculosis.
Tuberculosis
Three-dimensional structures of apo- and holo-L-alanine dehydrogenase from Mycobacterium tuberculosis reveal conformational changes upon coenzyme binding.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.2