EC 1.1.1.381: 3-hydroxy acid dehydrogenase
This is an abbreviated version!
For detailed information about 3-hydroxy acid dehydrogenase, go to the full flat file.
Reaction
Synonyms
ydfG, YMR226c
ECTree
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| Results | in table |
|---|---|
| 2602 | AA Sequence |
| 2 | Cloned(Commentary) |
| 2 | Cofactor |
| 15 | kcat/KM [mM/s] |
| 16 | KM Value [mM] |
| 3 | Organism |
| 2 | Pathway |
| 2 | pH Optimum |
| 2 | pH Stability |
| 2 | Purification (Commentary) |
| 3 | Reaction |
| 3 | Reference |
| 2 | Specific Activity [micromol/min/mg] |
| 20 | Substrates and Products (Substrate) |
| 4 | Synonyms |
| 1 | Systematic Name |
| 2 | Temperature Optimum [°C] |
| 2 | Temperature Stability [°C] |
| 15 | Turnover Number [1/s] |
Substrates Products
Substrates Products on EC 1.1.1.381 - 3-hydroxy acid dehydrogenase
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REACTION DIAGRAM
D-glycerate + NADP+
?
Substrates: the Vmax/KM value is 20% compared to L-allo-threonine
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L-3-hydroxybutyrate + NADP+
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Substrates: the Vmax/KM value is less than 1% compared to L-allo-threonine
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L-glycerate + NADP+
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Substrates: the Vmax/KM value is 18% compared to L-allo-threonine
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?
Substrates: the Vmax/KM value is 31% compared to L-allo-threonine
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D-3-hydroxyisobutyrate + NADP+
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Substrates: the Vmax/KM value is 1% compared to L-allo-threonine
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Substrates: the Vmax/KM value is 15% compared to L-allo-threonine
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D-serine + NADP+
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Substrates: the Vmax/KM value is less than 1% compared to L-allo-threonine
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D-serine + NADP+
?
Substrates: the Vmax/KM value is less than 1% compared to L-allo-threonine
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?
?
Substrates: the Vmax/KM value is 55% compared to L-allo-threonine
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D-threonine + NADP+
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Substrates: the Vmax/KM value is 55% compared to L-allo-threonine
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D-threonine + NADP+
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Substrates: the Vmax/KM value is 55% compared to L-allo-threonine
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?
Substrates: the Vmax/KM value is 34% compared to L-allo-threonine
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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+
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Substrates: the Vmax/KM value is 3.8% compared to L-allo-threonine
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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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?
?
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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Products: -
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