Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-threonine + NAD+ | Bacillus subtilis | - |
L-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
L-threonine + NAD+ | Bacillus subtilis 168 | - |
L-2-amino-3-oxobutanoate + NADH + H+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | O31776 | - |
- |
Bacillus subtilis 168 | O31776 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-threonine + NAD+ | - |
Bacillus subtilis | L-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
L-threonine + NAD+ | the product L-2-amino-3-oxobutanoate is unstable. It spontaneously converts to 2,5-dimethylpyrazine in a pH-dependent reaction, via 3,6-dihydro-2,5-dimethylpyrazine. The reaction from aminoacetone to 2,5-dimethylpyrazine is a pH-dependent nonenzymatic reaction. Inactivation of 2-amino-3-ketobutyrate coenzyme A ligase in Bacilus subtilis improves 2,5-dimethylpyrazine production | Bacillus subtilis | L-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
L-threonine + NAD+ | - |
Bacillus subtilis 168 | L-2-amino-3-oxobutanoate + NADH + H+ | - |
? | |
L-threonine + NAD+ | the product L-2-amino-3-oxobutanoate is unstable. It spontaneously converts to 2,5-dimethylpyrazine in a pH-dependent reaction, via 3,6-dihydro-2,5-dimethylpyrazine. The reaction from aminoacetone to 2,5-dimethylpyrazine is a pH-dependent nonenzymatic reaction. Inactivation of 2-amino-3-ketobutyrate coenzyme A ligase in Bacilus subtilis improves 2,5-dimethylpyrazine production | Bacillus subtilis 168 | L-2-amino-3-oxobutanoate + NADH + H+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TDH | - |
Bacillus subtilis |