Gly-X carboxypeptidase

Last updated
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
Search
PMC articles
PubMed articles
NCBI proteins

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

  1. 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.
  2. 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. Bibcode:1978FEBSL..91...59W. doi:10.1016/0014-5793(78)80017-9. PMID   352726. S2CID   84374615.