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
Anthopleura pacifica
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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
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
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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
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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
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
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
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
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, 25°C
9.17
D-Strombine
apparent value, isozyme St/AlDH1, with 1 mM NAD+, in 0.1 M PIPES-NaOH (pH 9.1), at 30°C
36.5 - 180
Gly
34.2
glycine
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pH 7.5, 25°C
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, 25°C
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 30°C
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 30°C; apparent value, isozyme St/AlDH1, with 5 mM pyruvate and 100 mM L-Ala, in 0.1 M PIPES-NaOH (pH 7.2), at 30°C
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
Marphysa sanguinea
A0A9I9
apparent value, isozyme St/AlDH1, with 1 mM NAD+, in 0.1 M PIPES-NaOH (pH 9.1), at 30°C
50.08
Gly
Marphysa sanguinea
A0A9I9
apparent value, isozyme St/AlDH1, with 0.3 mM NADH and 5 mM pyruvate, in 0.1 M PIPES-NaOH (pH 7.2), at 30°C
51.7
L-Ala
Marphysa sanguinea
A0A9I9
apparent value, isozyme St/AlDH1, with 0.3 mM NADH and 5 mM pyruvate, in 0.1 M PIPES-NaOH (pH 7.2), at 30°C
23.64
L-Ser
Marphysa sanguinea
A0A9I9
apparent value, isozyme St/AlDH1, with 0.3 mM NADH and 5 mM pyruvate, in 0.1 M PIPES-NaOH (pH 7.2), at 30°C
5.12
meso-Alanopine
Marphysa sanguinea
A0A9I9
apparent value, isozyme St/AlDH1, with 1 mM NAD+, in 0.1 M PIPES-NaOH (pH 9.1), at 30°C
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 30°C
87
after 29fold purification, at 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
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with Gly and pyruvate as substrates
7
assay at; assay at and optimal pH
7.2
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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
25
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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
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 56°C for 20 sec only retains 20% of its original activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, glycerol, 2 weeks, 100% activity
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4°C, 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