Báo cáo khoa học: The changing patterns of covalent active site occupancy during catalysis on a modular polyketide synthase multienzyme revealed by ion-trap mass spectrometry
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A catalytically competent, homodimeric diketide synthase comprising thefirst extension module of the erythromycin polyketide synthase was analysedusing MS, after limited proteolysis to release functional domains, to deter-mine the pattern of covalent attachment of substrates and intermediates toactive sites during catalysis.
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Báo cáo khoa học: The changing patterns of covalent active site occupancy during catalysis on a modular polyketide synthase multienzyme revealed by ion-trap mass spectrometry
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Báo cáo khoa học: The changing patterns of covalent active site occupancy during catalysis on a modular polyketide synthase multienzyme revealed by ion-trap mass spectrometry
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