title: Biosynthetic origin of [R-(Z)]-4-amino-3-chloro-2-pentenedioic acid in Streptomyces viridogenes.
abstract: The biosynthesis of the chlorinated amino acid [R-(Z)]-4-amino-3-chloro-2-pentenedioic acid (ACPA) was investigated. Feeding studies with Streptomyces viridogenes were conducted in resting cells. Substantial incorporation from [(15)N]- and [(13)C]-enriched glutamate and proline indicated that the biosynthetic origin of ACPA is one of these amino acids. Experiments with deuterated glutamate and proline imply that chlorination does not occur via a radical mechanism, but rather suggest that a FADH(2)-dependent halogenase is involved.
authors.affiliation: School of Biomolecular and Biomedical Science, Centre for Synthesis and Chemical Biology, Ardmore House, University College Dublin.
authors.forename: Robin I
authors.initials: RI
authors.lastname: Hutchinson
authors.forename: Russell J
authors.initials: RJ
authors.lastname: Grant
authors.forename: Cormac D
authors.initials: CD
authors.lastname: Murphy
mesh_terms: D005971:Glutamates / Q000096:biosynthesis; D018629:Spectrometry, Mass, Secondary Ion; D013237:Stereoisomerism; D013302:Streptomyces / Q000378:metabolism*
chemical_list: D005971:Glutamates; C041409:4-amino-3-chloro-2-pentenedioic acid