title: Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis.
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.
authors.affiliation: Department of Chemistry, University of Warwick, Coventry, UK CV4 7AL.
authors.forename: Stuart W
authors.initials: SW
authors.lastname: Haynes
authors.forename: Paulina K
authors.initials: PK
authors.lastname: Sydor
authors.forename: Anna E
authors.initials: AE
authors.lastname: Stanley
authors.forename: Lijiang
authors.initials: L
authors.lastname: Song
authors.forename: Gregory L
authors.initials: GL
authors.lastname: Challis
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D013058:Mass Spectrometry; D015394:Molecular Structure; D005810:Multigene Family / Q000235:genetics; D009154:Mutation / Q000235:genetics; D011353:Prodigiosin / Q000031:analogs & derivatives* / Q000096:biosynthesis; D048372:Streptomyces coelicolor / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; C528938:undecylprodiginine; D011353:Prodigiosin