Gly-X carboxypeptidase
| Gly-Xaa carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.4 | ||||||||
| CAS no. | 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 (July 1966). "[Purification and properties of 2 peptidases from baker's yeast]". Biochimica et Biophysica Acta. 122 (1): 127–44. doi:10.1016/0926-6593(66)90096-8. PMID 4961236.
- ^ Wolf DH, Ehmann C (July 1978). "Carboxypetidase S from yeast: regulation of its activity during vegetative growth and differentiation". FEBS Letters. 91 (1): 59–62. doi:10.1016/0014-5793(78)80017-9. PMID 352726.
External links
- Gly-Xaa+carboxypeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
