On the dd-Carboxypeptidase Enzyme System of Streptomyces Strain K15

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Abstract
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‐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 40000‐Mr enzyme and the two lysozyme‐releasable 40000‐Mr and 38000‐Mr enzymes are moderately sensitive to benzylpenicillin and have a high propensity to catalyse dimer formation from the aforementioned tetrapeptide monomer.