EC 126.96.36.199 - Carboxypeptidase D
IntEnz Enzyme Nomenclature
cereal serine carboxypeptidase II
gene KEX1 serine carboxypeptidase
serine carboxypeptidase [misleading]
- Preferential release of a C-terminal arginine or lysine residue.
A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in ). In peptidase family S10 (carboxypeptidase C family). Formerly EC 188.8.131.52 and 184.108.40.206, and included in EC 220.127.116.11.
Links to other databases
Serine carboxypeptidases. A review.Carlsberg Res. Commun. 51 : 83-128 (1986).
Primary structure and enzymatic properties of carboxypeptidase II from wheat bran.Carlsberg Res. Commun. 52 : 297-311 (1987).
Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and α-factor precursor processing.Cell 50 : 573-584 (1987). [PMID: 3301004]
Refined atomic model of wheat serine carboxypeptidase II at 2.2-Å resolution.Biochemistry 31 : 9796-9812 (1992). [PMID: 1390755]
[EC 18.104.22.168 created 1972 as EC 22.214.171.124, transferred 1978 to EC 126.96.36.199, part transferred 1993 to EC 188.8.131.52, modified 2011]