Information on EC 1.5.1.17 - alanopine dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.17
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RECOMMENDED NAME
GeneOntology No.
alanopine dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,2'-iminodipropanoate + NAD+ + H2O = L-alanine + pyruvate + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyruvate fermentation to opines
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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).
CAS REGISTRY NUMBER
COMMENTARY hide
71343-07-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Bursa sp.
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Manually annotated by BRENDA team
Busycotypus canaliculatum
Cantharus undosus
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Cymatium pileare
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Cypraecassis rufa
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Lambis millepeda
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Manually annotated by BRENDA team
Lambis scorpius
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
weak
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Manually annotated by BRENDA team
Mitra eremitarum
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Manually annotated by BRENDA team
from Hawaii
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Nassarius glans particeps
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Aplysia juliana
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Manually annotated by BRENDA team
no activity in Aplysia kurodai
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Manually annotated by BRENDA team
no activity in Asterias amurensis
weak
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Manually annotated by BRENDA team
no activity in Asterina pectinifera
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Manually annotated by BRENDA team
no activity in Aurelia aurita
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Manually annotated by BRENDA team
no activity in Balanus cariosus
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Manually annotated by BRENDA team
no activity in Halichondria japonica
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Manually annotated by BRENDA team
no activity in Halocynthia roretzi
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Manually annotated by BRENDA team
no activity in Hemigrapsus sanguineus
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Manually annotated by BRENDA team
no activity in Hexagrammos otakii
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Manually annotated by BRENDA team
no activity in Octopus membranaceus
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Manually annotated by BRENDA team
no activity in Oncorhynchus keta
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Manually annotated by BRENDA team
no activity in Pagurus samuelis
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Manually annotated by BRENDA team
no activity in Pollicipes mitella
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Manually annotated by BRENDA team
no activity in Pugettia quadridens
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Manually annotated by BRENDA team
no activity in Solaster paxillatus
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Manually annotated by BRENDA team
no activity in Stichopus japonicus
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Manually annotated by BRENDA team
Nucula nitida
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
collected in the straits of Messina area (central Mediterranean) between May and June of 2011, from two nearby marine and brackish-water sites, two populations
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Polydora commensalis
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Manually annotated by BRENDA team
Polydora glycymerica
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Scolelepis fuliginosa
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Tibia martinii
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Xenophora crispa
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
AlaDHAm is a member of the family of opine dehydrogenases (OpDHs), which catalyze the reductive condensation of pyruvate with an L-amino acid in the presence of NADH to so-called opines during anaerobic glycolysis. Residue E141 of domain I and W279 of domain II are conserved in OpDHs and are present in AlaDHAm, stucture comparisons, overview
metabolism
physiological function
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enzyme ADH acts as one of the primary and anaerobic metabolic responses pathways during hypoxia. Montipora capitata increasingly relies upon alanopine dehydrogenase, ADH, and strombine dehydrogenase, SDH, for anaerobic catabolism under low-oxygen conditions
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-alanine + pyruvate + NADH + H+
beta-alanopine + NAD+ + H2O
show the reaction diagram
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r
Gly + pyruvate + NADH
Strombine + NAD+ + H2O
show the reaction diagram
glycine + pyruvate + NADH + H+
? + NAD+ + H2O
show the reaction diagram
reductive condensation, low activity
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?
L-2-Aminobutyrate + pyruvate + NADH
?
show the reaction diagram
L-Ala + 2-oxobutanoate + NADH
?
show the reaction diagram
L-Ala + 2-oxopentanoate + NADH
?
show the reaction diagram
L-Ala + glyoxylate + NADH
?
show the reaction diagram
L-Ala + hydroxypyruvate + NADH
?
show the reaction diagram
L-Ala + oxaloacetate + NADH
?
show the reaction diagram
L-Ala + pyruvate + NADH
2,2'-Iminodipropanoate + NAD+ + H2O
show the reaction diagram
L-alanine + pyruvate + NADH + H+
2,2'-iminodipropanoate + NAD+ + H2O
show the reaction diagram
L-Cys + pyruvate + NADH
?
show the reaction diagram
L-Ser + pyruvate + NADH
?
show the reaction diagram
L-Thr + pyruvate + NADH
?
show the reaction diagram
L-Val + pyruvate + NADH
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-alanine + pyruvate + NADH + H+
beta-alanopine + NAD+ + H2O
show the reaction diagram
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r
L-alanine + pyruvate + NADH + H+
2,2'-iminodipropanoate + NAD+ + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
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200 mM, 16% inhibition
2-oxoglutarate
3-phosphoglycerate
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AMP
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competitive with respect to NADH
D-lactate
D-strombine
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dihydroxyacetone phosphate
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fructose 1,6-bisphosphate
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KCl
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200 mM, 33% inhibition
L-Ala
L-alanine
uncompetitive substrate inhibition
L-lactate
meso-Alanopine
NaCl
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200 mM, 38% inhibition
NH4Cl
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200 mM, 23% inhibition
oxamate
pyruvate
succinate
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 hide
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150
2-aminobutanoate
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2.35 - 3.45
2-oxobutanoate
2.5
2-oxobutyrate
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9.1
2-Oxopentanoate
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16
2-oxovalerate
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1
alanopine
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50 - 2542
Gly
655.1
glycine
pH and temperature not specified in the publication
3.49 - 11.9
glyoxylate
2.3 - 6.48
Hydroxypyruvate
15
L-2-aminobutyrate
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2.75 - 98
L-Ala
14.8
L-alanine
pH and temperature not specified in the publication
12 - 35
L-Cys
48 - 247
L-Ser
25.5 - 110
L-Thr
20 - 70.5
L-Val
1.68 - 6.5
meso-Alanopine
0.03 - 0.75
NAD+
0.01 - 9
NADH
0.9
oxaloacetate
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0.17 - 1.3
pyruvate
680
Ser
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additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
176.4
glycine
pH and temperature not specified in the publication
1084.6
L-alanine
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
58
L-alanine
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
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with L-Ala and pyruvate as substrates
7.1
Busycotypus canaliculatum
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with 50 mM L-Ala and 2 mM pyruvate as substrates, foot muscle enzyme
7.2
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assay at
7.5
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with 130 mM L-Ala, 0.1 mM NADH and 1.3 mM pyruvate as substrates
8.1
Busycotypus canaliculatum
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with 15 mM meso-alanopine and 1.2 mM NAD+ as substrates, enzyme from hepatopancreas
8.6
Busycotypus canaliculatum
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with 15 mM meso-alanopine and 1.2 mM NAD+ as substrates, enzyme from gill
9.2
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with 50 mM meso-alanopine as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
28
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
the adductor muscle also shows a conspicuous amount of strombine dehydrogenase
Manually annotated by BRENDA team
Busycotypus canaliculatum
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Manually annotated by BRENDA team
Busycotypus canaliculatum
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Manually annotated by BRENDA team
additional information
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enzyme tissue distribution and expression analysis
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38500
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gel filtration
42200
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gel filtration
42400
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1 * 42400, SDS-PAGE
44000
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gel filtration
46500
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1 * 46500, SDS-PAGE
47200
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 45000, SDS-PAGE
monomer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stable for at least 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme to homogeneity
partial
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
diagnostics
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the significant positive relationship between exposure length and enzyme activity of ADH and strombine dehydrogenase, SDH, in Montipora capitata supports the implementation of these enzymes as biomarkers for rapid analysis of hypoxia-induced stress in corals