KEGG   ENZYME: 3.4.17.14Help
Entry
EC 3.4.17.14                Enzyme                                 

Name
zinc D-Ala-D-Ala carboxypeptidase;
Zn2+ G peptidase, D-alanyl-D-alanine hydrolase;
D-alanyl-D-alanine-cleaving carboxypeptidase;
DD-carboxypeptidase;
G enzyme;
DD-carboxypeptidase-transpeptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metallocarboxypeptidases
BRITE hierarchy
Reaction(IUBMB)
Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl!D-alanine
Comment
A zinc enzyme. Catalyses carboxypeptidation but not transpeptidation reactions involved in bacterial cell wall metabolism. Weakly inhibited by beta-lactams. In peptidase family M15. Distinct from EC 3.4.16.4, serine-type D-Ala-D-Ala carboxypeptidase.
History
EC 3.4.17.14 created 1992
Orthology
K08640  
zinc D-Ala-D-Ala carboxypeptidase
Genes
SCO: 
SCO5467(SC2A11.01)
SGR: 
SSX: 
SFA: 
SDV: 
SALB: 
STRP: 
SFI: 
SLV: 
SGU: 
KFL: 
AOI: 
AJA: 
SESP: 
VMA: 
SNA: 
 » show all
Taxonomy
Reference
1  [PMID:7121588]
  Authors
Dideberg O, Charlier P, Dive G, Joris B, Frere JM, Ghuysen JM.
  Title
Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution.
  Journal
Nature. 299 (1982) 469-70.
  Sequence
[salb:XNR_1349]
Reference
2  [PMID:6825689]
  Authors
Joris B, Van Beeumen J, Casagrande F, Gerday C, Frere JM, Ghuysen JM.
  Title
The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G.
  Journal
Eur. J. Biochem. 130 (1983) 53-69.
  Sequence
[salb:XNR_1349]
Reference
3  [PMID:6597561]
  Authors
Ghuysen JM, Frere JM, Leyh-Bouille M, Nguyen-Disteche M, Coyette J, Dusart J, Joris B, Duez C, Dideberg O, Charlier P, et al.
  Title
Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics.
  Journal
Scand. J. Infect. Dis. Suppl. 42 (1984) 17-37.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
213189-85-6

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