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Characterization of TrdL as a 10-hydroxy dehydrogenase and generation of new analogues from a tirandamycin biosynthetic pathway.

Xuhua X Mo, Hongbo H Huang, Junying J Ma, Zhongwen Z Wang, Bo B Wang, Si S Zhang, Changsheng C Zhang, and Jianhua J Ju

Org Lett 13(9):2212-5 (2011) PMID 21456513

TrdL, encoding a flavin-dependent oxidoreductase in the tirandamycin gene cluster, was inactivated to afford a ΔtrdL mutant, the fermentation of which yielded a new intermediate, tirandamycin E (5), and an additional early intermediate, tirandamycin F (6), if XAD-16 resin was introduced. TrdL was overexpressed in E. coli, and the protein was shown to efficiently catalyze the transformations from 5 to tirandamycin A (1) and from 6 to tirandamycin D (4), demonstrating its function as a 10-hydroxy dehydrogenase.

DOI: 10.1021/ol200447h
Version: za2963e q8za5 q8zb2 q8zcc q8zd1 q8zeb q8zf7 q8zgd
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