Information on EC 1.5.1.22 - Strombine dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.5.1.22
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RECOMMENDED NAME
GeneOntology No.
Strombine dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-(carboxymethyl)-D-alanine + NAD+ + H2O = glycine + 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
N-(carboxymethyl)-D-alanine:NAD+ oxidoreductase (glycine-forming)
Also catalyses the reaction of EC 1.5.1.17 alanopine dehydrogenase, but more slowly. Does not act on L-strombine.
CAS REGISTRY NUMBER
COMMENTARY hide
79393-84-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
weak
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Manually annotated by BRENDA team
Balanus cariosus
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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
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UniProt
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
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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 Aurelia aurita
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Manually annotated by BRENDA team
no activity in Cellana grata
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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 Hexagrammos otakii
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Manually annotated by BRENDA team
no activity in Liolophura japonica
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Manually annotated by BRENDA team
no activity in Loligo bleekeri
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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 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
no activity in Strongylocentrotus nudus
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Manually annotated by BRENDA team
no activity in Todarodes pacificus
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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
Paraprionospio pinnata
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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
Scolelepis fuliginosa
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
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enzyme SDH 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
Ala + pyruvate + NADH
meso-alanopine + NAD+ + H2O
show the reaction diagram
Paraprionospio pinnata
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?
beta-Ala + pyruvate + NADH
?
show the reaction diagram
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?
Gly + 2-ketobutyrate + NADH + H+
2-[(carboxymethyl)amino]butanoic acid + NAD+ + H2O
show the reaction diagram
8.9% activity compared to Gly + pyruvate + NADH with isozyme St/AlDH1
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?
Gly + 2-oxobutanoate + NADH
?
show the reaction diagram
Gly + 2-oxopentanoate + NADH
?
show the reaction diagram
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19.6% of the activity with pyruvate
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Gly + glyoxylate + NADH
?
show the reaction diagram
Gly + glyoxylate + NADH + H+
[(carboxymethyl)amino]propanedioic acid + NAD+ + H2O
show the reaction diagram
3.9% activity compared to Gly + pyruvate + NADH with isozyme St/AlDH1
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?
Gly + hydroxypyruvate + NADH
?
show the reaction diagram
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29.5% of the activity with pyruvate
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Gly + oxaloacetate + NADH
?
show the reaction diagram
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106% of the activity with pyruvate
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Gly + oxaloacetate + NADH + H+
N-carboxymethylglycine + NAD+ + H2O
show the reaction diagram
39.1% activity compared to Gly + pyruvate + NADH with isozyme St/AlDH1
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?
Gly + pyruvate + NADH
D-Strombine + NAD+ + H2O
show the reaction diagram
Gly + pyruvate + NADH + H+
D-strombine + NAD+ + H2O
show the reaction diagram
94.6% activity compared to L-Ala + pyruvate + NADH with isozyme St/AlDH1
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?
Gly + pyruvate + NADPH
D-strombine + NADP+ + H2O
show the reaction diagram
less than 0.5% activity compared to Gly + pyruvate + NADH with isozyme St/AlDH1
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?
glycine + pyruvate + NADH
D-strombine + NAD+ + H2O
show the reaction diagram
glycine + pyruvate + NADH + H+
N-(carboxymethyl)-D-alanine + NAD+ + H2O
show the reaction diagram
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the reduction reaction is preferred
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r
L-2-Aminobutanoate + pyruvate + NADH
?
show the reaction diagram
L-2-Aminobutyrate + pyruvate + NADH
?
show the reaction diagram
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?
L-Ala + 2-ketobutyrate + NADH + H+
2-[[(1S)-1-carboxyethyl]amino]butanoic acid + NAD+ + H2O
show the reaction diagram
8.9% activity compared to L-Ala + pyruvate + NADH with isozyme St/AlDH1
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?
L-Ala + glyoxylate + NADH + H+
N-(carboxymethyl)-L-Ala + NAD+ + H2O
show the reaction diagram
4.0% activity compared to L-Ala + pyruvate + NADH with isozyme St/AlDH1
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?
L-Ala + oxaloacetate + NADH + H+
[[(1S)-1-carboxyethyl]amino]propanedioic acid + NAD+ + H2O
show the reaction diagram
40.0% activity compared to L-Ala + pyruvate + NADH with isozyme St/AlDH1
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?
L-Ala + pyruvate + NADH
?
show the reaction diagram
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Gly and Ala are preferred substrates
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?
L-Ala + pyruvate + NADH
meso-Alanopine + NAD+ + H2O
show the reaction diagram
L-Ala + pyruvate + NADH + H+
meso-alanopine + NAD+ + H2O
show the reaction diagram
100% activity
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?
L-Ala + pyruvate + NADPH
meso-alanopine + NADP+ + H2O
show the reaction diagram
less than 0.5% activity compared to L-Ala + pyruvate + NADH with isozyme St/AlDH1
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?
L-Cys + pyruvate + NADH
?
show the reaction diagram
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19.9% of the activity with Gly
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L-Cys + pyruvate + NADH + H+
N-(1-carboxyethyl)-L-Cys + NAD+ + H2O
show the reaction diagram
1.7% activity compared to L-Ala + pyruvate + NADH with isozyme St/AlDH1
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?
L-Met + pyruvate + NADH
?
show the reaction diagram
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3.7% of the activity with Gly
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L-Ser + pyruvate + NADH
?
show the reaction diagram
L-Ser + pyruvate + NADH + H+
N-(1-carboxyethyl)-L-Ser + NAD+ + H2O
show the reaction diagram
14.2% activity compared to L-Ala + pyruvate + NADH with isozyme St/AlDH1
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?
L-Thr + pyruvate + NADH
?
show the reaction diagram
L-Val + pyruvate + NADH
?
show the reaction diagram
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11.2% of the activity with Gly
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L-Val + pyruvate + NADH + H+
N-(1-carboxyethyl)-L-Val + NAD+ + H2O
show the reaction diagram
0.9% activity compared to L-Ala + pyruvate + NADH with isozyme St/AlDH1
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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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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
glycine + pyruvate + NADH + H+
N-(carboxymethyl)-D-alanine + NAD+ + H2O
show the reaction diagram
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the reduction reaction is preferred
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r
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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10% of enzymatic activity is inhibited at 10 mM
Cu2+
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50% of enzymatic activity is inhibited at 1 mM
Fe3+
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inhibits enzyme at 0.2 mM
Mg2+
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20% of enzymatic activity is inhibited at 10 mM
Mn2+
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13% of enzymatic activity is inhibited at 1 mM
Zn2+
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inhibits enzyme at 0.6 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
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D-lactate
D-strombine
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iminodiacetate
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iminodiacetic acid
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L-lactate
meso-Alanopine
oxaloacetate
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pyruvate
inhibited by an excess of substrate pyruvate; substrate inhibition, in excess, pyruvate enters in competition with the other substrate (glycine and/or NADH) preventing the site of reaction to take all the substrates to proceed with the enzymatic reaction. Its optimal concentration is determined to be round 2.0-2.3 mM
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
11.71 - 12.77
2-Ketobutyrate
2.46 - 3.55
2-oxobutanoate
23.8
2-Oxopentanoate
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196
beta-Ala
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pH 7.5, 25C
9.17
D-strombine
apparent value, isozyme St/AlDH1, with 1 mM NAD+, in 0.1 M PIPES-NaOH (pH 9.1), at 30C
36.5 - 180
Gly
34.2
glycine
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pH 7.5, 25C
4.18 - 32.5
glyoxylate
8.5
Hydroxypyruvate
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44 - 457
L-2-aminobutanoate
45.9
L-2-aminobutyrate
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pH 7.5, 25C
39.2 - 242
L-Ala
28
L-Cys
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163 - 693
L-Ser
48 - 303
L-Thr
310
L-Val
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9.07
meso-Alanopine
apparent value, isozyme St/AlDH1, with 1 mM NAD+, in 0.1 M PIPES-NaOH (pH 9.1), at 30C
0.85 - 0.87
NAD+
0.07
NADH
apparent value, isozyme St/AlDH1, with 5 mM pyruvate and 100 mM Gly, in 0.1 M PIPES-NaOH (pH 7.2), at 30C; apparent value, isozyme St/AlDH1, with 5 mM pyruvate and 100 mM L-Ala, in 0.1 M PIPES-NaOH (pH 7.2), at 30C
1.7 - 10.2
oxaloacetate
0.32 - 1.39
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.77 - 23.2
2-Ketobutyrate
4.99
D-strombine
apparent value, isozyme St/AlDH1, with 1 mM NAD+, in 0.1 M PIPES-NaOH (pH 9.1), at 30C
50.08
Gly
apparent value, isozyme St/AlDH1, with 0.3 mM NADH and 5 mM pyruvate, in 0.1 M PIPES-NaOH (pH 7.2), at 30C
51.7
L-Ala
apparent value, isozyme St/AlDH1, with 0.3 mM NADH and 5 mM pyruvate, in 0.1 M PIPES-NaOH (pH 7.2), at 30C
23.64
L-Ser
apparent value, isozyme St/AlDH1, with 0.3 mM NADH and 5 mM pyruvate, in 0.1 M PIPES-NaOH (pH 7.2), at 30C
5.12
meso-Alanopine
apparent value, isozyme St/AlDH1, with 1 mM NAD+, in 0.1 M PIPES-NaOH (pH 9.1), at 30C
3.86 - 3.96
NAD+
43.58 - 44.7
NADH
42.66 - 44.25
oxaloacetate
47.33 - 47.78
pyruvate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.69 - 5.57
acetate
16.4 - 17
D-lactate
0.63 - 1.35
iminodiacetate
21.2 - 22.9
L-lactate
6.93 - 14.3
oxaloacetate
3.98 - 15.4
succinate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.6
crude extract, at 30C
87
after 29fold purification, at 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
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with Gly and pyruvate as substrates
7.5
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assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 7.6
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pH optimum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 46
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temperature optimum
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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the adductor muscle also shows a conspicuous amount of strombine dehydrogenase
Manually annotated by BRENDA team
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very low enzyme content
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
35000
native PAGE; semi-native PAGE
38200
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gel filtration
40600
reduced and denatured enzyme, estimated by SDS-PAGE
42000
native enzyme, estimated by SDS-PAGE
43350
deduced from amino acid sequence from strombine/alanopine dehydrogenase
44000
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gel filtration
46000
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SDS-PAGE
75000
native PAGE; semi-native PAGE two bands at 35 kDa and 75 kDa are visible
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
native and semi-native PAGE analysis, 2 * 35000; native PAGE and semi-native PAGE, 2 * 35000 Da
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56
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enzyme is heat labile, pretreatment at 56C for 20 sec only retains 20% of its original activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, glycerol, 2 weeks, 100% activity
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4C, stable for at least 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-cellulose SH column chromatography, hydroxyapatite column chromatography, and Toyopearl Super Q-650S column chromatography
partial
purified over 470fold using ammonium sulfate fractionation, sephacryl S-100 chromatography, hydroxyapatite adsorption, DEAE-sepharose chromatography, Blue-sepharose chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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the significant positive relationship between exposure length and enzyme activity of alanopine dehydrogenase, ADH, and SDH in Montipora capitata supports the implementation of these enzymes as biomarkers for rapid analysis of hypoxia-induced stress in corals