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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39366

Title: Biosynthesis of streptolidine involved two unexpected intermediates produced by a dihydroxylase and a cyclase through unusual mechanisms
Authors: Chinyuan Chang;Syue-Yi Lyu;Yu-Chen Liu;Ning-Shian Hsu;Chih-Chung Wu;Cheng-Fong Tang;Kuan-Hung Lin;Jin-Yuan Ho;Chang-Jer Wu;Ming-Daw Tsai;Tsung-Lin Li
Contributors: 國立臺灣海洋大學:食品科學系
Date: 2014-02
Issue Date: 2016-12-07T06:57:57Z
Publisher: Angewandte Chemie International Edition
Abstract: Abstract: Streptothricin-F (STT-F), one of the early-discovered antibiotics, consists of three components, a β-lysine homopolymer, an aminosugar D-gulosamine, and an unusual bicyclic streptolidine. The biosynthesis of streptolidine is a long-lasting but unresolved puzzle. Herein, a combination of genetic/biochemical/structural approaches was used to unravel this problem. The STT gene cluster was first sequenced from a Streptomyces variant BCRC 12163, wherein two gene products OrfP and OrfR were characterized in vitro to be a dihydroxylase and a cyclase, respectively. Thirteen high-resolution crystal structures for both enzymes in different reaction intermediate states were snapshotted to help elucidate their catalytic mechanisms. OrfP catalyzes an Fe(II) -dependent double hydroxylation reaction converting L-Arg into (3R,4R)-(OH)2 -L-Arg via (3S)-OH-L-Arg, while OrfR catalyzes an unusual PLP-dependent elimination/addition reaction cyclizing (3R,4R)-(OH)2 -L-Arg to the six-membered (4R)-OH-capreomycidine. The biosynthetic mystery finally comes to light as the latter product was incorporation into STT-F by a feeding experiment.
Relation: 53(7)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/39366
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