Muramoyltetrapeptide carboxypeptidase

Muramoyltetrapeptide carboxypeptidase (EC 3.4.17.13, carboxypeptidase IIW, carboxypeptidase II, lysyl-D-alanine carboxypeptidase, L-lysyl-D-alanine carboxypeptidase, LD-carboxypeptidase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction

Hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl--D-alanine
Muramoyltetrapeptide carboxypeptidase
Identifiers
EC number3.4.17.13
CAS number60063-80-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Variants are known from various microorganisms.

References

  1. DasGupta H, Fan DP (July 1979). "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan". The Journal of Biological Chemistry. 254 (13): 5672–83. PMID 109439.
  2. Rousset A, Nguyen-Distèche M, Minck R, Ghuysen JM (December 1982). "Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms". Journal of Bacteriology. 152 (3): 1042–8. PMC 221607. PMID 6754695.
  3. Metz R, Henning S, Hammes WP (March 1986). "LD-carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12". Archives of Microbiology. 144 (2): 181–6. doi:10.1007/bf00414732. PMID 3521530.
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