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PMID: 97082 Published · ppublish English Journal Article

Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC9790. Properties of the purified enzyme.

European journal of biochemistry ·Vol. 88 ·No. 1 ·1978-07-17 ·Pages 297-305

Coyette J, Ghuysen JM, Fontana R

Abstract

Streptococcus faecalis ATCC 9790 possesses six membrane-bound, penicillin-binding proteins. That numbered 6 (Mr 43000) is the most abundant one and is the DD-carboxypeptidase studied previously. The enzyme has been solubilized and purified to the stage where one single protein band can be detected by gel electrophoresis. The purification procedure does not alter the properties that the enzyme exhibits when it is membrane-bound. The DD-carboxypeptidase itself may be a killing target for penicillin in S. faecalis.

MeSH Terms
Carboxypeptidases/metabolism Carrier Proteins/isolation & purification Cell Membrane/enzymology Cloxacillin/metabolism Enterococcus faecalis/drug effects,enzymology Muramoylpentapeptide Carboxypeptidase/isolation & purification,metabolism Oligopeptides/metabolism Penicillin G/metabolism Penicillins/metabolism Solubility
Chemicals
Carrier Proteins Oligopeptides Penicillins Carboxypeptidases Muramoylpentapeptide Carboxypeptidase Cloxacillin Penicillin G
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Coyette J
Ghuysen J M
Fontana R
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1978-07-17
Pages
297-305
Language
English
Region
England
NLM ID
0107600
Subset
IM
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