Open AccessOn the dd ‐Carboxypeptidase Enzyme System of Streptomyces Strain K15
Author(s) -
LEYHBOUILLE Melina,
NGUYENDISTÈCHE Martine,
GHUYSEN JeanMarie
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb06242.x
Subject(s) - strain (injury) , carboxypeptidase , streptomyces , enzyme , biochemistry , microbiology and biotechnology , chemistry , biology , genetics , bacteria , anatomy
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 one single penicillin‐binding protein. The exocellular 54000‐ M r enzyme is extremely sensitive to benzylpenicillin and performs low transpeptidase activity on the carbonyl‐donor/amino‐acceptor tetrapeptide A cl Lys(Gly)‐ d Ala‐ d Ala‐ The exocellular 40000‐ M r enzyme and the two lysozyme‐releasable 40000‐ M r and 38000‐ M r enzymes are moderately sensitive to benzylpenicillin and have a high propensity to catalyse dimer formation from the aforementioned tetrapeptide monomer.