| Entry |
|
| Name |
phenylalanine racemase (ATP-hydrolysing);
phenylalanine racemase;
phenylalanine racemase (adenosine triphosphate-hydrolysing);
gramicidin S synthetase I |
| Class |
Isomerases;
Racemases and epimerases;
Acting on amino acids and derivatives
 |
| Sysname |
phenylalanine racemase (ATP-hydrolysing) |
| Reaction(IUBMB) |
ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine
[RN:R00686] |
| Reaction(KEGG) |
R00686
 |
| Substrate |
ATP [CPD:C00002];
L-phenylalanine [CPD:C00079];
H2O [CPD:C00001] |
| Product |
AMP [CPD:C00020];
diphosphate [CPD:C00013];
D-phenylalanine [CPD:C02265] |
| Pathway |
PATH: ec00360 Phenylalanine metabolism |
| Structures |
PDB: 1AMU |
Reference Authors Title
Journal Organism
|
1 [PMID:5354026]
Yamada M, Kurahashi K.
Further purification and properties of adenosine
triphosphate-dependent phenylalanine racemase of Bacillus brevis
Nagano.
J. Biochem. (Tokyo). 66 (1969) 529-40.
Bacillus brevis |
| Other DBs |
ExplorEnz - The Enzyme Database: 5.1.1.11
IUBMB Enzyme Nomenclature: 5.1.1.11
ExPASy - ENZYME nomenclature database: 5.1.1.11
BRENDA, the Enzyme Database: 5.1.1.11
CAS: 37290-95-2 |