Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis.
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.
Haynes
Stuart W
SW
Department of Chemistry, University of Warwick, Coventry, UK CV4 7AL.
Sydor
Paulina K
PK
Stanley
Anna E
AE
Song
Lijiang
L
Challis
Gregory L
GL
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
D001426:Bacterial Proteins; C528938:undecylprodiginine; D011353:Prodigiosin