Information on EC 1.1.1.381 - 3-hydroxy acid dehydrogenase

for references in articles please use BRENDA:EC1.1.1.381
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.381
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RECOMMENDED NAME
GeneOntology No.
3-hydroxy acid dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-2-amino-3-oxobutanoate = aminoacetone + CO2
show the reaction diagram
(1b), spontaneous
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L-allo-threonine + NADP+ = aminoacetone + CO2 + NADPH + H+
show the reaction diagram
overall reaction
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L-allo-threonine + NADP+ = L-2-amino-3-oxobutanoate + NADPH + H+
show the reaction diagram
(1a)
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Glycine, serine and threonine metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-allo-threonine:NADP+ 3-oxidoreductase
The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. The highest activity is seen with L-allo-threonine and D-threonine. The enzyme from Escherichia coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate. The enzyme has no activity with NAD+ or L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
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
D-3-hydroxyisobutyrate + NADP+
?
show the reaction diagram
D-glycerate + NADP+
?
show the reaction diagram
the Vmax/KM value is 20% compared to L-allo-threonine
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?
D-serine + NADP+
?
show the reaction diagram
D-threonine + NADP+
?
show the reaction diagram
L-3-hydroxybutyrate + NADP+
?
show the reaction diagram
L-3-hydroxyisobutyrate + NADP+
?
show the reaction diagram
L-allo-threonine + NADP+
aminoacetone + CO2 + NADPH + H+
show the reaction diagram
L-glycerate + NADP+
?
show the reaction diagram
the Vmax/KM value is 18% compared to L-allo-threonine
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?
L-serine + NADP+
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
57 - 61
D-3-hydroxyisobutyrate
50
D-glycerate
pH 9.0, 30°C
69 - 71
D-serine
7 - 60
D-threonine
95
L-3-hydroxybutyrate
pH 9.0, 30°C
36 - 60
L-3-hydroxyisobutyrate
3 - 29
L-allo-threonine
33
L-Glycerate
pH 9.0, 30°C
40 - 95
L-serine
0.54
NADP+
pH 9.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.78 - 8.61
D-3-hydroxyisobutyrate
2.01
D-glycerate
pH 9.0, 30°C
3.5 - 7.84
D-serine
6.55 - 52.8
D-threonine
9.38
L-3-hydroxybutyrate
pH 9.0, 30°C
4.03 - 20.1
L-3-hydroxyisobutyrate
5.76 - 43.8
L-allo-threonine
1.17
L-Glycerate
pH 9.0, 30°C
4.2 - 11
L-serine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.062 - 0.151
D-3-hydroxyisobutyrate
0.04
D-glycerate
pH 9.0, 30°C
0.05 - 0.11
D-serine
0.109 - 7.5
D-threonine
0.099
L-3-hydroxybutyrate
pH 9.0, 30°C
0.067 - 0.558
L-3-hydroxyisobutyrate
0.199 - 14.6
L-allo-threonine
0.036
L-Glycerate
pH 9.0, 30°C
0.105 - 0.116
L-serine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.4
pH 9.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
most stable over the pH-range 6.5 to 10.0
639084
7.5 - 10.5
most stable over the pH-range 6.5 to 10.0
639084
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
when heated for 10 min in 0.1 M potassium phosphate buffer (pH 7.4) containing 0.01% 2-mercaptoethanol and 10% glycerol, the enzyme is stable at up to 40°C
55
when heated for 10 min in 0.1 M potassium phosphate buffer (pH 7.4) containing 0.01% 2-mercaptoethanol and 10% glycerol, the enzyme is stable at up to 55°C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli JM109