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  • Title: On the DD-carboxypeptidase enzyme system of Streptomyces strain K15.
    Author: Leyh-Bouille M, Nguyen-Distèche M, Ghuysen JM.
    Journal: Eur J Biochem; 1981 Apr; 115(3):579-84. PubMed ID: 7238522.
    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 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.
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