Gly-X carboxypeptidase

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
Gly-Xaa carboxypeptidase
Identifiers
EC number3.4.17.4
CAS number9025-25-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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. doi:10.1016/0014-5793(78)80017-9. PMID 352726.
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