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  • Title: Secretion by overexpression and purification of the water-soluble Streptomyces K15 DD-transpeptidase/penicillin-binding protein.
    Author: Palomeque-Messia P, Quittre V, Leyh-Bouille M, Nguyen-Distèche M, Gershater CJ, Dacey IK, Dusart J, Van Beeumen J, Ghuysen JM.
    Journal: Biochem J; 1992 Nov 15; 288 ( Pt 1)(Pt 1):87-91. PubMed ID: 1445284.
    Abstract:
    Though synthesized with a cleavable signal peptide and devoid of membrane anchors, the 262-amino-acid-residue Streptomyces K15 DD-transpeptidase/penicillin-binding protein is membrane-bound. Overexpression in Streptomyces lividans resulted in the export of an appreciable amount of the synthesized protein (4 mg/litre of culture supernatant). The water-soluble enzyme was purified close to protein homogeneity with a yield of 75%. It requires the presence of 0.5 M-NaCl to remain soluble. It is indistinguishable from the detergent-extract wild-type enzyme with respect to molecular mass, thermostability, transpeptidase activity and penicillin-binding capacity.
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