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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+ L -threonine (cf . EC 1.1.1.103 , L -threonine 3-dehydrogenase).
Synonyms
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YMR226c
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L-2-amino-3-oxobutanoate = aminoacetone + CO2
(1b), spontaneous
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L-allo-threonine + NADP+ = aminoacetone + CO2 + NADPH + H+
overall reaction
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L-allo-threonine + NADP+ = L-2-amino-3-oxobutanoate + NADPH + H+
(1a)
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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).
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D-3-hydroxyisobutyrate + NADP+
?
D-glycerate + NADP+
?
Substrates: the Vmax/KM value is 20% compared to L-allo-threonine
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L-3-hydroxybutyrate + NADP+
?
Substrates: the Vmax/KM value is less than 1% compared to L-allo-threonine
?
L-3-hydroxyisobutyrate + NADP+
?
L-allo-threonine + NADP+
aminoacetone + CO2 + NADPH + H+
L-glycerate + NADP+
?
Substrates: the Vmax/KM value is 18% compared to L-allo-threonine
?
D-3-hydroxyisobutyrate + NADP+
?
Substrates: the Vmax/KM value is 31% compared to L-allo-threonine
?
D-3-hydroxyisobutyrate + NADP+
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Substrates: the Vmax/KM value is 1% compared to L-allo-threonine
?
D-serine + NADP+
?
Substrates: the Vmax/KM value is 15% compared to L-allo-threonine
?
D-serine + NADP+
?
Substrates: the Vmax/KM value is less than 1% compared to L-allo-threonine
?
D-serine + NADP+
?
Substrates: the Vmax/KM value is less than 1% compared to L-allo-threonine
?
D-threonine + NADP+
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Substrates: the Vmax/KM value is 55% compared to L-allo-threonine
?
D-threonine + NADP+
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Substrates: the Vmax/KM value is 55% compared to L-allo-threonine
?
D-threonine + NADP+
?
Substrates: the Vmax/KM value is 55% compared to L-allo-threonine
?
L-3-hydroxyisobutyrate + NADP+
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Substrates: the Vmax/KM value is 34% compared to L-allo-threonine
?
L-3-hydroxyisobutyrate + NADP+
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Substrates: the Vmax/KM value is 3.8% compared to L-allo-threonine
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L-3-hydroxyisobutyrate + NADP+
?
Substrates: the Vmax/KM value is 3.8% compared to L-allo-threonine
?
L-allo-threonine + NADP+
aminoacetone + CO2 + NADPH + H+
Substrates: 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
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L-allo-threonine + NADP+
aminoacetone + CO2 + NADPH + H+
Substrates: 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-oxobutyrate, which is spontaneously decarboxylated into aminoacetone
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L-allo-threonine + NADP+
aminoacetone + CO2 + NADPH + H+
Substrates: 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-oxobutyrate, which is spontaneously decarboxylated into aminoacetone
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L-serine + NADP+
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Substrates: the Vmax/KM value is 53% compared to L-allo-threonine
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L-serine + NADP+
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Substrates: the Vmax/KM value is less than 1% compared to L-allo-threonine
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L-serine + NADP+
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Substrates: the Vmax/KM value is less than 1% compared to L-allo-threonine
?
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NADP+
no activity with NAD+
NADP+
no activity with NAD+
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57 - 61
D-3-hydroxyisobutyrate
50
D-glycerate
pH 9.0, 30°C
95
L-3-hydroxybutyrate
pH 9.0, 30°C
36 - 60
L-3-hydroxyisobutyrate
33
L-Glycerate
pH 9.0, 30°C
57
D-3-hydroxyisobutyrate
pH 9.0, 30°C
61
D-3-hydroxyisobutyrate
pH 9.0, 30°C
69
D-serine
pH 9.0, 30°C
7
D-threonine
pH 9.0, 30°C
60
D-threonine
pH 9.0, 30°C
36
L-3-hydroxyisobutyrate
pH 9.0, 30°C
60
L-3-hydroxyisobutyrate
pH 9.0, 30°C
3
L-allo-threonine
pH 9.0, 30°C
29
L-allo-threonine
pH 9.0, 30°C
40
L-serine
pH 9.0, 30°C
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3.78 - 8.61
D-3-hydroxyisobutyrate
2.01
D-glycerate
pH 9.0, 30°C
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
3.78
D-3-hydroxyisobutyrate
pH 9.0, 30°C
8.61
D-3-hydroxyisobutyrate
pH 9.0, 30°C
3.5
D-serine
pH 9.0, 30°C
7.84
D-serine
pH 9.0, 30°C
6.55
D-threonine
pH 9.0, 30°C
52.8
D-threonine
pH 9.0, 30°C
4.03
L-3-hydroxyisobutyrate
pH 9.0, 30°C
20.1
L-3-hydroxyisobutyrate
pH 9.0, 30°C
5.76
L-allo-threonine
pH 9.0, 30°C
43.8
L-allo-threonine
pH 9.0, 30°C
4.2
L-serine
pH 9.0, 30°C
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0.062 - 0.151
D-3-hydroxyisobutyrate
0.04
D-glycerate
pH 9.0, 30°C
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
0.062
D-3-hydroxyisobutyrate
pH 9.0, 30°C
0.151
D-3-hydroxyisobutyrate
pH 9.0, 30°C
0.05
D-serine
pH 9.0, 30°C
0.11
D-serine
pH 9.0, 30°C
0.109
D-threonine
pH 9.0, 30°C
7.5
D-threonine
pH 9.0, 30°C
0.067
L-3-hydroxyisobutyrate
pH 9.0, 30°C
0.558
L-3-hydroxyisobutyrate
pH 9.0, 30°C
0.199
L-allo-threonine
pH 9.0, 30°C
14.6
L-allo-threonine
pH 9.0, 30°C
0.105
L-serine
pH 9.0, 30°C
0.116
L-serine
pH 9.0, 30°C
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8.5
oxidation of L-serine
8.5
oxidation of L-serine
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30
assay at
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SwissProt
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SwissProt
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SwissProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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6.5 - 10
most stable over the pH-range 6.5 to 10.0
7.5 - 10.5
most stable over the pH-range 6.5 to 10.0
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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
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expression in Escherichia coli JM109
expression in Escherichia coli JM109
expression in Escherichia coli JM109
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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)
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