Selective synthesis of depsipeptides by the immobilized multienzyme enniatin synthetase |
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Authors: | Norbert Madry Rainer Zocher Karola Grodzki Horst Kleinkauf |
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Affiliation: | (1) Institut für Biochemie und Molekulare Biologie, Technische Universität Berlin, Franklinstrasse 29, D-1000 Berlin 10 |
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Abstract: | Summary The multifunctional enzyme enniatin synthetase was immobilized by adsorption to propyl agarose. The immobilized multienzyme retained 45% of the activity of the free enzyme; an operational half-life of about 15 h was estimated. Selective synthesis of several different enniatin homologues was achieved with propyl agarose-bound enniatin synthetase. In addition to enniatin A, B, and C formation, a selective synthesis of non-naturally occurring depsipeptides, containing norvaline, norleucine, or -aminobutyric acid as sole amino acid moieties, was observed. |
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