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Information on EC 1.5.1.17 - alanopine dehydrogenase
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EC Tree
1.5.1.17 alanopine dehydrogenaseIUBMB Comments
In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22 strombine dehydrogenase).
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Word Map
- 1.5.1.17
- analysis
- fulgidus
-
1.4.1.1
- archaeoglobus
- proteolyticus
-
cyclodeaminase
-
phormidium
- octopine
- diagnostics
The enzyme appears in viruses and cellular organisms
Synonyms
aladh, alanopine dehydrogenase, alpdh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH
ALPDH
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-
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Dehydrogenase, alanopine
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-
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meso-N-(1-Carboxyethyl)-alanine dehydrogenase
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-
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ADH
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-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,2'-iminodipropanoate + NAD+ + H2O = L-alanine + pyruvate + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
2,2'-iminodipropanoate:NAD+ oxidoreductase (L-alanine-forming)
In the reverse reaction, L-alanine can be replaced by L-cysteine, L-serine or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22 strombine dehydrogenase).
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CAS REGISTRY NUMBER
COMMENTARY
71343-07-2
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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
2,2'-iminodipropanoate + NAD+ + H2O
L-alanine + pyruvate + NADH + H+
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-
-
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r
glycine + pyruvate + NADH + H+
? + NAD+ + H2O
reductive condensation, low activity
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-
?
Gly + pyruvate + NADH
Strombine + NAD+ + H2O
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at 161.5% of the activity with L-Ala
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?
Gly + pyruvate + NADH
Strombine + NAD+ + H2O
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at 69% of the activity with L-Ala
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-
?
Gly + pyruvate + NADH
Strombine + NAD+ + H2O
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at 9% of the activity with L-Ala
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-
?
L-2-Aminobutyrate + pyruvate + NADH
?
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at 60% of the activity with L-Ala
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-
?
L-2-Aminobutyrate + pyruvate + NADH
?
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at 94% of the activity with L-Ala
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?
L-Ala + 2-oxobutanoate + NADH
?
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at 21% of the activity with pyruvate
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?
L-Ala + 2-oxobutanoate + NADH
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at 68% of the activity with pyruvate
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?
L-Ala + 2-oxobutanoate + NADH
?
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at 22% the activity with pyruvate
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?
L-Ala + 2-oxopentanoate + NADH
?
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at 25.6% of the activity with pyruvate
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?
L-Ala + 2-oxopentanoate + NADH
?
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at 58% of the activity with pyruvate
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?
L-Ala + hydroxypyruvate + NADH
?
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at 12.8% of the activity with pyruvate
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?
L-Ala + hydroxypyruvate + NADH
?
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at 3.3% of the activity with pyruvate
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?
L-Ala + oxaloacetate + NADH
?
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at 106.6% of the activity with pyruvate
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?
L-Ala + pyruvate + NADH
2,2'-Iminodipropanoate + NAD+ + H2O
Busycotypus canaliculatum
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-
-
-
?
L-Ala + pyruvate + NADH
2,2'-Iminodipropanoate + NAD+ + H2O
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?
L-alanine + pyruvate + NADH + H+
2,2'-iminodipropanoate + NAD+ + H2O
reductive condensation, the enzyme is highy specific for L-alanine
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?
L-alanine + pyruvate + NADH + H+
2,2'-iminodipropanoate + NAD+ + H2O
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r
additional information
?
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L-alanine binding region of alanopine dehydrogenase near a distinct helix-link-helix motif predicted by unbiased molecular dynamics simulations of ligand diffusion using a homology model of alanopine dehydrogenase, overview
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?
additional information
?
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L-alanine binding region of alanopine dehydrogenase near a distinct helix-link-helix motif predicted by unbiased molecular dynamics simulations of ligand diffusion using a homology model of alanopine dehydrogenase, overview
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?
additional information
?
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Busycotypus canaliculatum
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the enzyme from hepatopancreas is involved in alanopine oxidation
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?
additional information
?
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Busycotypus canaliculatum
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muscle enzyme is involved in anaerobic glycolysis
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?
additional information
?
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enzyme catalyzes the terminal step of anaerobic glycolysis during muscle anoxia associated with locomotion
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?
additional information
?
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the enzyme probably functions in the maintenance of a redox balance during anaerobiosis in the adductor muscle and heart of the oyster
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?
additional information
?
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the enzyme functions in cytoplasmic redox balance during anoxia stress
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?
additional information
?
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the enzyme functions as the terminal dehydrogenase of glycolysis and has a role in maintaining energy production under the stresses of environmental or functional anoxia
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?
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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
2,2'-iminodipropanoate + NAD+ + H2O
L-alanine + pyruvate + NADH + H+
-
-
-
-
r
L-alanine + pyruvate + NADH + H+
2,2'-iminodipropanoate + NAD+ + H2O
reductive condensation, the enzyme is highy specific for L-alanine
-
-
?
L-alanine + pyruvate + NADH + H+
2,2'-iminodipropanoate + NAD+ + H2O
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-
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r
additional information
?
-
Busycotypus canaliculatum
-
the enzyme from hepatopancreas is involved in alanopine oxidation
-
-
?
additional information
?
-
Busycotypus canaliculatum
-
muscle enzyme is involved in anaerobic glycolysis
-
-
?
additional information
?
-
-
enzyme catalyzes the terminal step of anaerobic glycolysis during muscle anoxia associated with locomotion
-
-
?
additional information
?
-
-
the enzyme probably functions in the maintenance of a redox balance during anaerobiosis in the adductor muscle and heart of the oyster
-
-
?
additional information
?
-
-
the enzyme functions in cytoplasmic redox balance during anoxia stress
-
-
?
additional information
?
-
-
the enzyme functions as the terminal dehydrogenase of glycolysis and has a role in maintaining energy production under the stresses of environmental or functional anoxia
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
cofactor binding region determination predicted by unbiased molecular dynamics simulations of ligand diffusion
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additional information
-
cofactor binding region determination predicted by unbiased molecular dynamics simulations of ligand diffusion
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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the enzyme activity in adductor muscle decreases following the marine-brackish gradient
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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increased activity of alanopine dehydrogenase, ADH, and strombine dehydrogenase, SDH, enzymes in Montipora capitata exposed to prolonged durations of hypoxic conditions
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
IFN-? and IL-2 Responses to Recombinant AlaDH against ESAT-6/CFP-10 Fusion Antigens in the Diagnosis of Latent versus Active Tuberculosis Infection.
Tuberculosis
Host vector system for high-level expression and purification of recombinant, enzymatically active alanine dehydrogenase of Mycobacterium tuberculosis.
Tuberculosis
IFN-? and IL-2 Responses to Recombinant AlaDH against ESAT-6/CFP-10 Fusion Antigens in the Diagnosis of Latent versus Active Tuberculosis Infection.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE