Stereochemical course of tryptophan dehydrogenation during biosynthesis of the calcium-dependent lipopeptide antibiotics.
[reaction: see text] Hydrogen atoms are abstracted from the C2' and C3'-pro-S positions of an (S)-tryptophanyl precursor, with overall syn stereochemistry, during the biosynthesis of the C-terminal Z-2',3'-dehydrotryptophan residue of the calcium-dependent lipopeptide antibiotics (CDAs) in Streptomyces coelicolor. The absence of beta-hydroxytryptophanyl, or other possible intermediates, further suggests a direct dehydrogenation mechanism similar to that proposed for the l-tryptophan 2',3'-oxidase from Chromobacterium violaceum.
Amir-Heidari
Bagher
B
School of Chemistry and Manchester Interdisciplinary Biocentre, The University of Manchester, 131 Princess Street, Manchester M1 7ND, UK.
Thirlway
Jenny
J
Micklefield
Jason
J
D000900:Anti-Bacterial Agents / Q000096:biosynthesis* / Q000737:chemistry*; D002118:Calcium / Q000737:chemistry; D050356:Lipid Metabolism; D008055:Lipids / Q000737:chemistry*; D013058:Mass Spectrometry; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D013237:Stereoisomerism; D014364:Tryptophan / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
D000900:Anti-Bacterial Agents; D008055:Lipids; D010455:Peptides; D014867:Water; D014364:Tryptophan; D002118:Calcium