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Literature summary extracted from
- Racemization of phenylalanine by adenosine triphosphate-dependent phenylalanine racemase of Bacillus brevis Nagano (1971), J. Biochem., 69, 973-976.
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.11 | Brevibacillus brevis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 5.1.1.11 | - |
Brevibacillus brevis |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.1.1.11 | ATP + L-phenylalanine + H2O = AMP + diphosphate + D-phenylalanine | the enzyme activates both L-Phe and D-Phe to form L-phenylalanyl adenylate and D-phenylalanyl adenylate bound to the enzyme, respectively, and then transfers the L-Phe and D-Phe moiety to the thiol group of the enzyme followed by conversion of its configuration, the D-isomer being the more favorable configuration | Brevibacillus brevis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.11 | ATP + L-Phe + H2O | - |
Brevibacillus brevis | AMP + diphosphate + D-Phe | - |
? |  |
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Release 2023.1 (January 2023)
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