Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis
文献信息
Stuart W. Haynes, Paulina K. Sydor, Anna E. Stanley, Lijiang Song, Gregory L. Challis
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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Chemical Communications

ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry














