Reference : Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Microbiology
http://hdl.handle.net/2268/83091
Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790
English
Coyette, Jacques [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
Perkins, Harnold R. [National Institute for Medical Research > > > > >]
Polacheck, Itzhack [National Institute for Medical Research > > > > >]
Shockman, Gérald D. [National Institute for Medical Research > > > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > > >]
15-May-1974
European Journal of Biochemistry
Blackwell Science
44
2
459-468
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] acyltransferases/*metabolism ; alanine ; amino acid sequence ; binding sites ; carboxypeptidases/*metabolism ; cell membrane/*enzymology ; enterococcus faecalis/*enzymology/growth & development ; hydrogen-ion concentration ; hydrolysis ; lysine ; penicillins/pharmacology ; peptides/metabolism ; peptidoglycan ; surface-active agents
[en] Isolated membranes of Streptococcus faecalis ATCC 9790 exhibit DD-carboxypeptidase activity (standard reaction: Ac2-l-Lys-d-Ala-d-Ala →d-alanine + Ac2-l-Lys-d-Ala) and ld-trans-peptidase activity (standard reaction: Ac2-l-Lys-d-Ala + acceptor →d-alanine + Ac2-l-Lys-acceptor). The DD-carboxypeptidase activity has a considerable specificity for peptides with a C-terminal l-R3-d-Ala-d-Ala sequence where R3 is an amino acid residue and a long side-chain at the l-R3 position. A corresponding DD-transpeptidation reaction yielding the product Ac2-l-Lys-d-Ala-d-[14C]Ala from the system Ac2-l-Lys-d-Ala-d-Ala-f-d-[14C] alanine was not detected. The ld-transpeptidase activity has a considerable specificity for peptide donors that have an Nα-substituted, C-terminal l-R3-d-Ala sequence with a free ω-amino group at the end of a long side-chain at the l-R3 position, and a considerable specificity for amino group acceptors that are located on a d-carbon in α-position to a free carboxyl group. In the absence of acceptor, hydrolysis of the dipeptide Ac2-l-Lys-d-Ala (ld-carboxypeptidase activity) was not observed. Both DD-carboxypeptidase and ld-transpeptidase activities are inhibited by β-lactam antibiotics, but their relative sensitivity differs according to the particular antibiotic used.
Fonds de la Recherche Scientifique (Communauté française de Belgique) - F.R.S.-FNRS ; Fonds de la Recherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/83091
10.1111/j.1432-1033.1974.tb03504.x

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
COYETTE_1974_membrane-bount.pdfPublisher postprint1.83 MBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.