EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
5.1.1.11 | ATP + 4-fluoro-DL-Phe + H2O |
- |
Brevibacillus brevis |
? |
- |
? |
5.1.1.11 | ATP + L-Phe + H2O |
- |
Brevibacillus brevis |
AMP + diphosphate + D-Phe |
- |
? |
5.1.1.11 | ATP + L-Phe + H2O |
equilibrium ratio of L-Phe to D-Phe is 3:7 |
Brevibacillus brevis |
AMP + diphosphate + D-Phe |
- |
? |
5.1.1.11 | ATP + L-phenylalanine + H2O |
there are three activated intermediates: L-phenylalanyl-adenosine-5'-monophosphate diester, L-Phe-S-4'-phosphopantetheine and D-Phe-S-4'-phosphopantetheine-acyl enzyme |
Brevibacillus brevis |
AMP + diphosphate + D-phenylalanine |
- |
? |
5.1.1.11 | ATP + L-phenylalanine + H2O |
the three-domain initiation module PheATE of gramicidin S synthetase catalyzes the activation, thiolation and epimerization of L-phenylalanine, the first amino acid incorporated into the decapeptide antibiotic gramicidin S |
Brevibacillus brevis |
AMP + diphosphate + D-phenylalanine |
- |
? |
5.1.1.11 | 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 |
? |
- |
? |
5.1.1.11 | ATP + L-phenylalanine + H2O |
phenylalanine racemase, the light component of gramicidin S synthetase, racemizes Phe and activates it to the aminoacyl adenylate and in a second step to the thioester |
Brevibacillus brevis |
? |
- |
? |
5.1.1.11 | ATP + L-Tyr + H2O |
- |
Brevibacillus brevis |
AMP + diphosphate + D-Tyr |
- |
? |
5.1.1.11 | ATP + p-fluoro-L-Phe + H2O |
- |
Brevibacillus brevis |
AMP + diphosphate + p-fluoro-D-Phe |
- |
? |
5.1.1.11 | more |
the enzyme catalyzes Phe racemization and activation. Catalyzes ATP-AMP exchange reaction, L-Phe dependent ATP-AMP exchange reaction |
Brevibacillus brevis |
? |
- |
? |