Information on EC 1.1.1.381 - 3-hydroxy acid dehydrogenase

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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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-
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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
-
SwissProt
Manually annotated by BRENDA team
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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
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
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, 30C
69 - 71
D-serine
7 - 60
D-threonine
95
L-3-hydroxybutyrate
pH 9.0, 30C
36 - 60
L-3-hydroxyisobutyrate
3 - 29
L-allo-threonine
33
L-Glycerate
pH 9.0, 30C
40 - 95
L-serine
0.54
NADP+
pH 9.0, 30C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.78 - 8.61
D-3-hydroxyisobutyrate
2.01
D-glycerate
Escherichia coli
P39831
pH 9.0, 30C
3.5 - 7.84
D-serine
6.55 - 52.8
D-threonine
9.38
L-3-hydroxybutyrate
Saccharomyces cerevisiae
Q05016
pH 9.0, 30C
4.03 - 20.1
L-3-hydroxyisobutyrate
5.76 - 43.8
L-allo-threonine
1.17
L-Glycerate
Escherichia coli
P39831
pH 9.0, 30C
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
21571
0.04
D-glycerate
Escherichia coli
P39831
pH 9.0, 30C
521
0.05 - 0.11
D-serine
481
0.109 - 7.5
D-threonine
1718
0.099
L-3-hydroxybutyrate
Saccharomyces cerevisiae
Q05016
pH 9.0, 30C
4825
0.067 - 0.558
L-3-hydroxyisobutyrate
5711
0.199 - 14.6
L-allo-threonine
2967
0.036
L-Glycerate
Escherichia coli
P39831
pH 9.0, 30C
8241
0.105 - 0.116
L-serine
95
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.4
pH 9.0, 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
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 40C
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 55C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli JM109