Open AccessThe Peptidoglycan Crosslinking Enzyme System in Streptomyces Strains R61, K15 and rimosus
Author(s) -
LEYHBOUILLE Mélina,
DUSART Jean,
NGUYENDISTÈCHE Martine,
GHUYSEN JeanMarie,
REYNOLDS Peter E.,
PERKINS Harold R.
Publication year - 1977
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1977.tb11922.x
Subject(s) - carboxypeptidase , lysozyme , biochemistry , enzyme , streptomyces , peptidoglycan , enzyme assay , chemistry , strain (injury) , biology , bacteria , anatomy , genetics
The dd ‐carboxypeptidase‐transpeptidase enzyme system in Streptomyces strain K15 consists of: (1) a membrane‐bound transpeptidase capable of performing low dd ‐carboxypeptidase activity; and (2) a set of dd ‐carboxypeptidases: (a) membrane‐bound, (b) lysozyme‐releasable and (c) exocellular, having low transpeptidase activities in aqueous media and at low acceptor concentrations. The dd ‐carboxypeptidases are related to each other and may belong to the same pathway leading to enzyme excretion. A similar enzyme system occurs in Streptomyces strain R61 except that the membrane‐bound dd ‐carboxypeptidase activity is low when compared with the membrane‐bound transpeptidase activity. In Streptomyces rimosus the enzyme system consists almost exclusively of the membrane‐bound transpeptidase and the levels of membrane‐bound, lysozyme‐releasable and exocellular dd ‐carboxypeptidases are very low.