EC 3.4.16.6 - Carboxypeptidase D

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 3.4.16.6

Names

Accepted name:
carboxypeptidase D
Other names:
Saccharomyces cerevisiae KEX1 gene product
CPDW-II
KEX1 carboxypeptidase
KEX1 proteinase
KEX1DELTAp
carboxypeptidase Kex1
cereal serine carboxypeptidase II
gene KEX1 serine carboxypeptidase
carboxypeptidase S1
carboxypeptidase KEX1
serine carboxypeptidase [misleading]
Phaseolus proteinase
Systematic name:
-

Reaction

Comments:

A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in [1]). In peptidase family S10 (carboxypeptidase C family). Formerly EC 3.4.12.1 and 3.4.21.13, and included in EC 3.4.16.1.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00122
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004187
CAS Registry Number: 153967-26-1
UniProtKB/Swiss-Prot: (82) [show] [UniProt]

References

  1. Breddam, K.
    Serine carboxypeptidases. A review.
    Carlsberg Res. Commun. 51: 83-128 (1986).
  2. Breddam, K., Sørensen, S.B. and Svendsen, I.
    Primary structure and enzymatic properties of carboxypeptidase II from wheat bran.
    Carlsberg Res. Commun. 52: 297-311 (1987).
  3. Dmochowska, A., Dignard, D., Henning, D., Thomas, D.Y. and Bussey, H.
    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]
  4. Liao, D.-I., Breddam, K., Sweet, R.M., Bullock, T. and Remington, S.J.
    Refined atomic model of wheat serine carboxypeptidase II at 2.2-Å resolution.
    Biochemistry 31: 9796-9812 (1992). [PMID: 1390755]

[EC 3.4.16.6 created 1972 as EC 3.4.12.1, transferred 1978 to EC 3.4.16.1, part transferred 1993 to EC 3.4.16.6, modified 2011]