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Literature summary extracted from
- Crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75.ANG. - Inhibitor-induced conformational changes (2000), Biochemistry, 39, 10082-10089.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.17.1 | crystal structure of carboxypeptidase A complexed with D-cysteine at 1.75 A | Bos taurus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.17.1 | D-Cys | binds tightly to the active site zinc. D-Cys binds the active site zinc with a sulfur ligand and forms additional interactions with surrounding side chains of the enzyme. D-Cys binding induces a concerted motion of the side chains around the sinc ion | Bos taurus |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.17.1 | Bos taurus | P00730 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.17.1 | - |
Bos taurus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.17.1 | CPD | - |
Bos taurus |
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Release 2023.1 (January 2023)
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