1.4.1.1: alanine dehydrogenase
This is an abbreviated version!
For detailed information about alanine dehydrogenase, go to the full flat file.
Word Map on EC 1.4.1.1
-
1.4.1.1
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burn
-
children
-
postburn
-
sham
-
full-thickness
-
flame
-
admitted
-
superficial
-
admission
-
resuscitation
-
injured
-
trauma
-
sepsis
-
inflict
-
burn-induced
-
ringer
-
sacrificed
-
third-degree
-
anesthetized
-
immersion
-
xanthomonas
-
barley
-
child
-
demographic
-
dress
-
partial-thickness
-
victim
-
sugarcane
-
accident
-
home
-
second-degree
-
xylella
-
dorsum
-
work-related
-
postinjury
-
thermostat
-
epithelialization
-
debridement
-
hereinafter
-
1-methylcyclopropene
-
biotechnology
-
synthesis
-
fastidiosa
-
heater
-
toddler
-
hypermetabolic
-
delicious
-
guadeloupe
-
kitchen
-
diphenylamine
-
medicine
-
eschar
-
nutrition
-
analysis
-
shower
- 1.4.1.1
-
burn
- children
-
postburn
-
sham
-
full-thickness
-
flame
-
admitted
-
superficial
-
admission
-
resuscitation
-
injured
-
trauma
-
sepsis
-
inflict
-
burn-induced
-
ringer
-
sacrificed
-
third-degree
-
anesthetized
-
immersion
-
xanthomonas
- barley
- child
-
demographic
-
dress
-
partial-thickness
-
victim
-
sugarcane
-
accident
-
home
-
second-degree
-
xylella
-
dorsum
-
work-related
-
postinjury
-
thermostat
-
epithelialization
-
debridement
-
hereinafter
- 1-methylcyclopropene
- biotechnology
- synthesis
-
fastidiosa
-
heater
-
toddler
-
hypermetabolic
-
delicious
-
guadeloupe
-
kitchen
- diphenylamine
- medicine
-
eschar
- nutrition
- analysis
-
shower
Reaction
Synonyms
(S)alanine dehydrogenase, (S)alanine:NAD oxidoreductase, 40 kDa antigen, ADH, AF1665, ALADH, alanine dehydrogenase, alanine oxidative deaminase, alanine oxidoreductase, ALD, AldA, alpha-alanine dehydrogenase, ApalaDH, AsAlaDH, CQA66_00465, dehydrogenase, alanine, glyoxylate reductive aminase, GxrA, HAADH1, HAADH2, L-Ala dehydrogenase, L-AlaDH, L-AlaDH-Bs, L-alanine dehydrogenase, MtbALD, NAD(H)-dependent L-alanine dehydrogenase, NAD+ dependent amino acid dehydrogenase, NAD+-dependent alanine dehydrogenase, NAD-dependent alanine dehydrogenase, NAD-linked alanine dehydrogenase, NADH-dependent alanine dehydrogenase, OF4Ald, PlaAlaDH, PvRA, pyruvate reductive aminase, Rv2780, ScALD, SCO1773, SheAlaDH, TB43
ECTree
1.4.1.1 alanine dehydrogenaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 1.4.1.1 - alanine dehydrogenase
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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
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
r
2-oxopentanoate + NH3 + NADH + H+
L-norvaline + H2O + NAD+
-
-
-
r
3-bromopyruvate + NH3 + NADH
2-amino-3-bromopropanoate + NAD+ + H2O
-
5.3% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH
Ser + H2O + NAD+
-
15.4% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH + H+
L-serine + H2O + NAD+
-
-
-
r
L-2-aminobutyrate + H2O + NAD+
2-oxobutyrate + NH3 + NADH + H+
-
-
-
r
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-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
-
-
-
r
L-serine + H2O + NAD+
3-hydroxypyruvate + 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
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
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-oxobutyrate + NH3 + NADH + H+
L-2-aminobutyrate + H2O + NAD+
-
-
-
r
2-oxobutyrate + NH3 + NADH + H+
L-2-aminobutyrate + H2O + NAD+
-
-
-
r
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-fluoropyruvate + NH3 + NADH + H+
3-fluoro-L-alanine + H2O + NAD+
-
-
-
-
?
3-fluoropyruvate + NH3 + NADH + H+
3-fluoro-L-alanine + H2O + NAD+
recombinant enzyme in whole-cell catalysis at 25°C
-
-
r
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
-
-
?
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
r
glyoxylate + NH3 + NADH + H+
glycine + NAD+
-
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
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 + H+
-
13.3% of the activity with L-Ala
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
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 + H+
10.4% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
7.5% of the activity with L-Ala
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
in the reverse reaction 2-oxobutanoate reacts with 79% of the activity with pyruvate
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
8.7% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
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 + H+
-
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
2.4% of the activity with L-Ala
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
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 + H+
-
0.7% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
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+
Alkalihalophilus pseudofirmus
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus JCM 17055
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus OF4
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
reversible oxidative deamination and reductive amination reactions
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
reversible oxidative deamination and reductive amination reactions
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
reversible oxidative deamination and reductive amination reactions
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
reversible oxidative deamination and reductive amination reactions
-
-
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
-
-
-
?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
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
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
r
additional information
?
-
Alkalihalophilus pseudofirmus
the activity assay includes L-alanine, NAD+, phenazine methosulfate and 0.24 mM nitroblue tetrazolium in carbonate buffer (50 mn, pH 10.5)
-
-
-
additional information
?
-
Alkalihalophilus pseudofirmus ATCC BAA-2126
the activity assay includes L-alanine, NAD+, phenazine methosulfate and 0.24 mM nitroblue tetrazolium in carbonate buffer (50 mn, pH 10.5)
-
-
-
additional information
?
-
Alkalihalophilus pseudofirmus JCM 17055
the activity assay includes L-alanine, NAD+, phenazine methosulfate and 0.24 mM nitroblue tetrazolium in carbonate buffer (50 mn, pH 10.5)
-
-
-
additional information
?
-
Alkalihalophilus pseudofirmus OF4
the activity assay includes L-alanine, NAD+, phenazine methosulfate and 0.24 mM nitroblue tetrazolium in carbonate buffer (50 mn, pH 10.5)
-
-
-
additional information
?
-
-
Aspecific 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
?
-
one-pot preparation of D-amino acids through biocatalytic deracemization using alanine dehydrogenase and omega-transaminase. AlaDH produces pyruvate from L-alanine with NAD+, NOX oxidizes NADH to NAD+, and reductive amination of the resulting pyruvate back to the amino acid in an enantiomerically opposite form by D-selective omega-transaminase (omega-TA) using isopropylamine as an amino donor cosubstrate
-
-
-
additional information
?
-
one-pot preparation of D-amino acids through biocatalytic deracemization using alanine dehydrogenase and omega-transaminase. AlaDH produces pyruvate from L-alanine with NAD+, NOX oxidizes NADH to NAD+, and reductive amination of the resulting pyruvate back to the amino acid in an enantiomerically opposite form by D-selective omega-transaminase (omega-TA) using isopropylamine as an amino donor cosubstrate
-
-
-
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
?
-
isozyme HAADH2 has no oxidation activity for 20 amino acids, 3-fluoroalanine, D/L-lactic acid, D/L -DOPA and L-2-aminobutyric acid. It also has no reduction activity for all tested 2-oxo acids
-
-
-
additional information
?
-
isozyme HAADH2 has no oxidation activity for 20 amino acids, 3-fluoroalanine, D/L-lactic acid, D/L -DOPA and L-2-aminobutyric acid. It also has no reduction activity for all tested 2-oxo acids
-
-
-
additional information
?
-
-
isozyme HAADH2 has no oxidation activity for 20 amino acids, 3-fluoroalanine, D/L-lactic acid, D/L -DOPA and L-2-aminobutyric acid. It also has no reduction activity for all tested 2-oxo acids
-
-
-
additional information
?
-
L-alanine and pyruvate are the preferred substrates of the enzyme for the deamination and amination reaction, respectively. Oxaloacetate, 2-oxobutyrate, 3-fluoropyruvate, 2-oxoglutarate, and glyoxylate show 93.30%, 8.93%, 5.62%, 2.57%, 2.51% activity compared to pyruvate, respectively
-
-
-
additional information
?
-
L-alanine and pyruvate are the preferred substrates of the enzyme for the deamination and amination reaction, respectively. Oxaloacetate, 2-oxobutyrate, 3-fluoropyruvate, 2-oxoglutarate, and glyoxylate show 93.30%, 8.93%, 5.62%, 2.57%, 2.51% activity compared to pyruvate, respectively
-
-
-
additional information
?
-
-
L-alanine and pyruvate are the preferred substrates of the enzyme for the deamination and amination reaction, respectively. Oxaloacetate, 2-oxobutyrate, 3-fluoropyruvate, 2-oxoglutarate, and glyoxylate show 93.30%, 8.93%, 5.62%, 2.57%, 2.51% activity compared to pyruvate, respectively
-
-
-
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
additional information
?
-
Ald catalyzes the reductive amination reaction faster and more efficiently than the oxidative deamination reaction
-
-
-
additional information
?
-
-
Ald catalyzes the reductive amination reaction faster and more efficiently than the oxidative deamination reaction
-
-
-
additional information
?
-
Ald catalyzes the reductive amination reaction faster and more efficiently than the oxidative deamination reaction
-
-
-
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
additional information
?
-
Ald catalyzes the reductive amination reaction faster and more efficiently than the oxidative deamination reaction
-
-
-
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
?
-
an enzymatic assay system to eliminate or measure D-Ala is constructed using alanine racemase (L-AlaR from Synechocystis sp. PCC6803) and L-alanine dehydrogenase (L-AlaDH from Phormidium lapideum). D-Ala is converted to L-Ala by alanine racemase and then deaminated by L-alanine dehydrogenase with the reduction of NAD+ to NADH, which is determined with water-soluble tetrazolium. NADH nonenzymatically reduces WST-1 to form water soluble formazan.Using the assay system, the D-Ala contents of 7 crustaceans are determined. Method evaluation, overview
-
-
-
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
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
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
-
-
?
