Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis

Chemical Communications : Chem Comm
Stuart W HaynesGregory L Challis

Abstract

The function of RedH from Streptomyces coelicolor as an enzyme that catalyses the condensation of 4-methoxy-2,2'-bipyrrole-5-carboxaldehyde (MBC) and 2-undecylpyrrole to form the natural product undecylprodiginine has been experimentally proven, and the substrate specificity of RedH has been probed in vivo by examining its ability to condense chemically-synthesised MBC analogues with 2-undecylpyrrole to afford undecylprodiginine analogues.

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Citations

Feb 25, 2014·Applied Microbiology and Biotechnology·Nada StankovicJasmina Nikodinovic-Runic
Mar 5, 2013·Journal of the American Chemical Society·James H Frederich, Patrick G Harran
Jun 18, 2016·Chemical Reviews·Dennis X HuRegan J Thomson
Dec 13, 2016·Chemical Reviews·Man-Cheng TangYi Tang
Mar 18, 2017·Chemical Communications : Chem Comm·Tomohiro HigashinoHiroshi Imahori
Nov 19, 2013·ACS Catalysis·Sarah M Barry, Gregory L Challis
Sep 6, 2018·Natural Product Reports·Yi-Ling Du, Katherine S Ryan
Nov 11, 2019·Applied and Environmental Microbiology·Qingshan LongMeifeng Tao
Apr 21, 2011·Nature Chemistry·Steven D Bruner
Nov 20, 2020·ChemMedChem·Lea WinandMarkus Nett
Dec 30, 2020·Journal of Natural Products·Mirelle TakakiRoberto G S Berlinck
May 30, 2015·Journal of the American Chemical Society·David M WithallGregory L Challis
Dec 21, 2010·Journal of the American Chemical Society·Stuart W HaynesGregory L Challis
Mar 22, 2019·ACS Chemical Biology·Onur ErbilginBenjamin P Bowen

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