Gly-X carboxypeptidase
| Gly-Xaa carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.17.4 | ||||||||
| CAS number | 9025-25-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Gly-Xaa carboxypeptidase (EC 3.4.17.4, glycine carboxypeptidase, carboxypeptidase a, carboxypeptidase S, peptidase alpha, yeast carboxypeptidase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly!Leu
This enzyme is isolated from yeast.
References
- ↑ Félix, F.; Brouillet, N. (1966). "Purification et proprietes de deux peptidases de levure de brasserie". Biochim. Biophys. Acta. 122: 127–144. doi:10.1016/0926-6593(66)90096-8. PMID 4961236.
- ↑ Wolf, D.H.; Ehmann, C. (1978). "Carboxypeptidase S from yeast: regulation of its activity during vegetative growth and differentiation". FEBS Lett. 91: 59–62. doi:10.1016/0014-5793(78)80017-9. PMID 352726.
External links
- Gly-Xaa carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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