Muramoyltetrapeptide carboxypeptidase

Muramoyltetrapeptide carboxypeptidase
Identifiers
EC no.3.4.17.13
CAS no.60063-80-1
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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 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.