Reference : On the DD-carboxypeptidase enzyme system of Streptomyces strain K15
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83030
On the DD-carboxypeptidase enzyme system of Streptomyces strain K15
English
Leyh-Bouille, Mélina [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie > > >]
Nguyen-Distèche, Martine mailto [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Faculté de Médecine > Service de Microbiologie > > >]
1-Apr-1981
European Journal of Biochemistry
Blackwell Science
115
3
579-584
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] carboxypeptidases/*metabolism ; cell wall ; molecular weight ; muramoylpentapeptide carboxypeptidase/isolation & purification/*metabolism ; penicillin g ; streptomyces/*enzymology ; substrate specificity
[en] Streptomyces K15 possesses a set of exocellular and cell-bound D-alanyl-D-alanine carboxypeptidases. Four of them have been isolated to the stage where each enzyme preparation contains on single penicillin-binding protein. The exocellular 54000-Mr enzyme is extremely sensitive to benzylpenicillin and performs low transpeptidase activity on the carbonyl-donor/amino-acceptor tetrapeptide ACLLys(Gly)-DAla-DAla. The exocellular 40 000-Mr enzyme and the two lysozyme-releasable 40 000-Mr and 38 000-Mr enzymes are moderately sensitive to benzylpenicillin and have a high propensity to catalyse dimer formation from the aforementioned tetrapeptide monomer.
National Institutes of Health - NIH ; Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/83030

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