EC 3.4.16.4 - Serine-type D-Ala-D-Ala carboxypeptidase

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IntEnz Enzyme Nomenclature
EC 3.4.16.4

Names

Accepted name:
serine-type D-Ala-D-Ala carboxypeptidase
Other names:
D-alanine carboxypeptidase
D-alanyl carboxypeptidase
D-alanyl-D-alanine-carboxypeptidase
D-alanyl-D-alanine-cleaving peptidase
D-alanyl-D-alanine-cleaving-peptidase
DD-carboxypeptidase
DD-peptidase
DD-transpeptidase
D-alanyl-D-alanine carboxypeptidase
Systematic name:
-

Reaction

Comments:

A membrane-bound, bacterial enzyme inhibited by penicillin and other β-lactam antibiotics, which acylate the active site serine. Examples are known from peptidase families S11, S12 and S13. Distinct from zinc D-Ala-D-Ala carboxypeptidase, EC 3.4.17.14.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , MEROPS , MEROPS , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0009002
CAS Registry Number: 9077-67-2
UniProtKB/Swiss-Prot: (20) [show] [UniProt]

References

  1. Ghuysen, J.-M., Frère, J.-M., Leyh-Bouille, M., Nguyen-Distèche, M., Coyette, J., Dusart, J., Joris, B., Duez, C., Dideberg, O., Charlier, P., Dive, G., and Lamotte-Brasseur, J.
    Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics.
    Scand. J. Infect. Dis. 42: 17-37 (1984). [PMID: 6597561]
  2. Frère, J.M. and Joris, B.
    Penicillin-sensitive enzymes in peptidoglycan biosynthesis.
    CRC Crit. Rev. Microbiol. 11: 306-331 (1985). [PMID: 3888533]

[EC 3.4.16.4 created 1989]