EC 3 - Hydrolases
EC 3.4 - Acting on peptide bonds (peptidases)
EC 3.4.17 - Metallocarboxypeptidases
EC 3.4.17.13 - Muramoyltetrapeptide carboxypeptidase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 3.4.17.13
Names
Accepted name:
muramoyltetrapeptide carboxypeptidase
Other
names:
L-lysyl-D-alanine carboxypeptidase
LD-carboxypeptidase
carboxypeptidase II
carboxypeptidase IIW
lysyl-D-alanine carboxypeptidase
LD-carboxypeptidase
carboxypeptidase II
carboxypeptidase IIW
lysyl-D-alanine carboxypeptidase
Systematic name:
-
Reaction
- Hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysylD-alanine.
Comments:
Variants are known from various microorganisms. Involved in peptidoglycan synthesis, catalysing both decarboxylation and transpeptidation. Stimulated by divalent cations such as Mg2+ and Ca2+, but not by Zn2+. Inhibited by thiol-blocking reagents, but unaffected by penicillin.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
MEROPS
,
UniPathway
CAS Registry Number:
60063-80-1
UniProtKB/Swiss-Prot:
LDCA_ECO57
LDCA_ECOL6
LDCA_ECOLI
LDC_PSEAE
MEPS_ECO57
MEPS_ECOL6
MEPS_ECOLI
MEPS_SHIFL
PGPSA_DROME
References
-
Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan.J. Biol. Chem. 254 : 5672-5683 (1979). [PMID: 109439]
-
Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms.J. Bacteriol. 152 : 1042-1048 (1982). [PMID: 6754695]
-
LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12.Arch. Microbiol. 144 : 181-186 (1986).
[EC 3.4.17.13 created 1992]