EC Number   |
Substrates |
Organism |
Products |
Reversibility  |
|---|
    2.6.1.62 | more |
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate |
Psychrobacter cryohalolentis |
? |
- |
- |
| 2.6.1.62 | more |
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis |
Corynebacterium glutamicum |
? |
- |
- |
| 2.6.1.62 | more |
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis |
Corynebacterium glutamicum LMG 3730 |
? |
- |
- |
| 2.6.1.62 | more |
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis |
Corynebacterium glutamicum BCRC 11384 |
? |
- |
- |
| 2.6.1.62 | more |
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate |
Psychrobacter cryohalolentis DSM 17306 |
? |
- |
- |
| 2.6.1.62 | more |
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate |
Psychrobacter cryohalolentis K5 |
? |
- |
- |
| 2.6.1.62 | more |
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate |
Psychrobacter cryohalolentis VKM B-2378 |
? |
- |
- |
| 2.6.1.62 | more |
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis |
Corynebacterium glutamicum ATCC 13032 |
? |
- |
- |
| 2.6.1.62 | more |
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate |
Psychrobacter cryohalolentis ATCC BAA-1226 |
? |
- |
- |
| 2.6.1.62 | more |
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis |
Corynebacterium glutamicum JCM 1318 |
? |
- |
- |
