Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Phenylglyoxal | inhibition of Phe activation. Both ATP and Phe prevent the inactivation. ATP is competitive with phenylglyoxal, whereas Phe is not. A single arginine residue of GS 1 is essential for Phe activation in binding the phosphate moiety of ATP | Brevibacillus brevis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-phenylalanine + H2O | Brevibacillus brevis | phenylalanine racemase, i.e. gramicidin-S synthetase 1, activates and transfers D-Phe to the heavy enzyme, gramicidin S-synthetase 2, which activates the other constituent amino acids on the thioester template | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Brevibacillus brevis | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-Phe + H2O | - |
Brevibacillus brevis | AMP + diphosphate + D-Phe | - |
? | |
ATP + L-phenylalanine + H2O | phenylalanine racemase, i.e. gramicidin-S synthetase 1, activates and transfers D-Phe to the heavy enzyme, gramicidin S-synthetase 2, which activates the other constituent amino acids on the thioester template | Brevibacillus brevis | ? | - |
? |