Muramoyltetrapeptide carboxypeptidase

Muramoyltetrapeptide carboxypeptidase
Identifiers
EC number 3.4.17.13
CAS number 60063-80-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

Variants are known from various microorganisms.

References

  1. DasGupta, H.; Fan, D.P. (1979). "Purification and characterization of a carboxypeptidase-transpeptidase of Bacillus megaterium acting on the tetrapeptide moiety of the peptidoglycan". J. Biol. Chem. 254: 5672–5683. PMID 109439.
  2. Rousset, A.; Nguyen-Disteche, M.; Minck, R.; Ghuysen, J.-M. (1982). "Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms". J. Bacteriol. 152: 1042–1048. PMID 6754695.
  3. Metz, R.; Henning, S.; Hammes, W.P. (1986). "LD-Carboxypeptidase activity in Escherichia coli. II. Isolation, purification and characterization of the enzyme from E. coli K 12". Arch. Microbiol. 144: 181–186. doi:10.1007/bf00414732. PMID 3521530.
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