title: Characterization of TrdL as a 10-hydroxy dehydrogenase and generation of new analogues from a tirandamycin biosynthetic pathway.
abstract: 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.
authors: CAS Key Laboratory of Marine Bio-resources Sustainable Utilization, RNAM Center for Marine Microbiology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, 164 West Xingang Road, Guangzhou 510301, PR China.
authors: Xuhua
authors: X
authors: Mo
authors: Hongbo
authors: H
authors: Huang
authors: Junying
authors: J
authors: Ma
authors: Zhongwen
authors: Z
authors: Wang
authors: Bo
authors: B
authors: Wang
authors: Si
authors: S
authors: Zhang
authors: Changsheng
authors: C
authors: Zhang
authors: Jianhua
authors: J
authors: Ju
mesh_terms: D000617:Aminoglycosides / Q000138:chemical synthesis* / Q000378:metabolism; D055162:Biocatalysis; D015394:Molecular Structure; D009154:Mutation; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D000617:Aminoglycosides; D010088:Oxidoreductases