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Information on EC 1.1.1.381 - 3-hydroxy acid dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P39831

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IUBMB Comments
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).
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This record set is specific for:
Escherichia coli
UNIPROT: P39831
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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Synonyms
ymr226c, 3-hydroxy acid dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
YMR226c
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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).
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
the Vmax/KM value is 31% compared to L-allo-threonine
-
-
?
D-glycerate + NADP+
?
show the reaction diagram
the Vmax/KM value is 20% compared to L-allo-threonine
-
-
?
D-serine + NADP+
?
show the reaction diagram
the Vmax/KM value is 15% compared to L-allo-threonine
-
-
?
D-threonine + NADP+
?
show the reaction diagram
the Vmax/KM value is 55% compared to L-allo-threonine
-
-
?
L-3-hydroxyisobutyrate + NADP+
?
show the reaction diagram
the Vmax/KM value is 34% compared to L-allo-threonine
-
-
?
L-allo-threonine + NADP+
aminoacetone + CO2 + NADPH + H+
show the reaction diagram
highest Vmax/Km value of all substrates tested. The hydroxyl group of L-allo-threonine is oxidized by the enzymes to yield L-2-amino-3-ketobutyrate, which is spontaneously decarboxylated into aminoacetone
-
-
?
L-glycerate + NADP+
?
show the reaction diagram
the Vmax/KM value is 18% compared to L-allo-threonine
-
-
?
L-serine + NADP+
?
show the reaction diagram
the Vmax/KM value is 53% compared to L-allo-threonine
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
no activity with NAD+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
61
D-3-hydroxyisobutyrate
pH 9.0, 30°C
50
D-glycerate
pH 9.0, 30°C
69
D-serine
pH 9.0, 30°C
60
D-threonine
pH 9.0, 30°C
60
L-3-hydroxyisobutyrate
pH 9.0, 30°C
29
L-allo-threonine
pH 9.0, 30°C
33
L-Glycerate
pH 9.0, 30°C
40
L-serine
pH 9.0, 30°C
0.54
NADP+
pH 9.0, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.78
D-3-hydroxyisobutyrate
pH 9.0, 30°C
2.01
D-glycerate
pH 9.0, 30°C
3.5
D-serine
pH 9.0, 30°C
6.55
D-threonine
pH 9.0, 30°C
4.03
L-3-hydroxyisobutyrate
pH 9.0, 30°C
5.76
L-allo-threonine
pH 9.0, 30°C
1.17
L-Glycerate
pH 9.0, 30°C
4.2
L-serine
pH 9.0, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.062
D-3-hydroxyisobutyrate
pH 9.0, 30°C
0.04
D-glycerate
pH 9.0, 30°C
0.05
D-serine
pH 9.0, 30°C
0.109
D-threonine
pH 9.0, 30°C
0.067
L-3-hydroxyisobutyrate
pH 9.0, 30°C
0.199
L-allo-threonine
pH 9.0, 30°C
0.036
L-Glycerate
pH 9.0, 30°C
0.105
L-serine
pH 9.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.4
pH 9.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
oxidation of L-serine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
most stable over the pH-range 6.5 to 10.0
639084
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fujisawa, H.; Nagata, S.; Misono, H.
Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C)
Biochim. Biophys. Acta
1645
89-94
2003
Escherichia coli (P39831), Escherichia coli, Saccharomyces cerevisiae (Q05016), Saccharomyces cerevisiae, Saccharomyces cerevisiae ATCC 204508 (Q05016)
Manually annotated by BRENDA team