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PMID: 590266 Published · ppublish English Journal Article

The peptidoglycan crosslinking enzyme system in Streptomyces strains R61, K15 and rimosus.

European journal of biochemistry ·Vol. 81 ·No. 1 ·1977-11-15 ·Pages 19-28

Leyh-Bouille M, Dusart J, Nguyen-Distèche M, Ghuysen JM, Reynolds PE, Perkins HR

Abstract

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.

MeSH Terms
Carboxypeptidases/metabolism Cell Membrane/enzymology Kinetics Lysosomes/enzymology Muramoylpentapeptide Carboxypeptidase/isolation & purification,metabolism Peptidoglycan/metabolism Species Specificity Streptomyces/enzymology
Chemicals
Peptidoglycan Carboxypeptidases Muramoylpentapeptide Carboxypeptidase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Leyh-Bouille M
Dusart J
Nguyen-Distèche M
Ghuysen J M
Reynolds P E
Perkins H R
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1977-11-15
Pages
19-28
Language
English
Region
England
NLM ID
0107600
Subset
IM
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