Muramoyltetrapeptide carboxypeptidase explained

Muramoyltetrapeptide carboxypeptidase
Ec Number:	3.4.17.13
Cas Number:	60063-80-1

Muramoyltetrapeptide carboxypeptidase (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.

Notes and References

1. DasGupta H, Fan DP . 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 . July 1979 . 109439 .
2. Rousset A, Nguyen-Distèche M, Minck R, Ghuysen JM . 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 . December 1982 . 6754695 . 221607 .
3. Metz R, Henning S, Hammes WP . 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 . March 1986 . 3521530 . 10.1007/bf00414732 .