Novel Mycolactone from a Clinical Isolate of Mycobacterium ulcerans Provides Evidence for Additional Toxin Heterogeneity as a Result of Specific Changes in the Modular Polyketide Synthase

• Published in: Chembiochem : a European journal of chemical biology Vol. 6; no. 4; pp. 643 - 648
• Main Authors: Hong, Hui, Spencer, Jonathan B, Porter, Jessica L, Leadlay, Peter F, Stinear, Tim
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley-VCH Verlag 01.04.2005; WILEY-VCH Verlag; WILEY‐VCH Verlag
• Subjects: Acyltransferases - genetics; Acyltransferases - metabolism; Amino Acid Sequence; Bacterial Toxins - biosynthesis; Bacterial Toxins - chemistry; biosynthesis; Buruli ulcer; Lactones - chemistry; Macrolides; Mass Spectrometry; Molecular Sequence Data; Molecular Structure; Mycobacterium; Mycobacterium ulcerans; Mycobacterium ulcerans - enzymology; Mycobacterium ulcerans - genetics; Mycobacterium ulcerans - metabolism; mycolactone; Polyketide Synthases - genetics; Polyketide Synthases - metabolism; polyketides; Sequence Homology, Amino Acid; Substrate Specificity
• ISSN: 1439-4227; 1439-7633; 1439-4227
• DOI: 10.1002/cbic.200400339

New analogues of the toxin mycolactone have been identified in a pathogenic Chinese strain of Mycobacterium ulcerans. They possess an extra methyl group at C2′ (shown in red) compared to mycolactone A as a result of the recruitment of a single catalytic domain of altered specificity in the mycolactone polyketide synthase.