EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.1.1.381 | L-3-hydroxybutyrate + NADP+ |
the Vmax/KM value is less than 1% compared to L-allo-threonine |
Saccharomyces cerevisiae |
? |
- |
? |
1.1.1.381 | L-3-hydroxybutyrate + NADP+ |
the Vmax/KM value is less than 1% compared to L-allo-threonine |
Saccharomyces cerevisiae ATCC 204508 |
? |
- |
? |
1.1.1.381 | L-3-hydroxyisobutyrate + NADP+ |
the Vmax/KM value is 3.8% compared to L-allo-threonine |
Saccharomyces cerevisiae |
? |
- |
? |
1.1.1.381 | L-3-hydroxyisobutyrate + NADP+ |
the Vmax/KM value is 34% compared to L-allo-threonine |
Escherichia coli |
? |
- |
? |
1.1.1.381 | L-3-hydroxyisobutyrate + NADP+ |
the Vmax/KM value is 3.8% compared to L-allo-threonine |
Saccharomyces cerevisiae ATCC 204508 |
? |
- |
? |
1.1.1.381 | L-allo-threonine + NADP+ |
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 |
Escherichia coli |
aminoacetone + CO2 + NADPH + H+ |
- |
? |
1.1.1.381 | L-allo-threonine + NADP+ |
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 |
Saccharomyces cerevisiae |
aminoacetone + CO2 + NADPH + H+ |
- |
? |
1.1.1.381 | L-glycerate + NADP+ |
the Vmax/KM value is 18% compared to L-allo-threonine |
Escherichia coli |
? |
- |
? |
1.1.1.381 | L-serine + NADP+ |
the Vmax/KM value is 53% compared to L-allo-threonine |
Escherichia coli |
? |
- |
? |
1.1.1.381 | L-serine + NADP+ |
the Vmax/KM value is less than 1% compared to L-allo-threonine |
Saccharomyces cerevisiae |
? |
- |
? |