Biosynthetic origin of [R-(Z)]-4-amino-3-chloro-2-pentenedioic acid in Streptomyces viridogenes.
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.
Hutchinson
Robin I
RI
School of Biomolecular and Biomedical Science, Centre for Synthesis and Chemical Biology, Ardmore House, University College Dublin.
Grant
Russell J
RJ
Murphy
Cormac D
CD
D005971:Glutamates / Q000096:biosynthesis; D018629:Spectrometry, Mass, Secondary Ion; D013237:Stereoisomerism; D013302:Streptomyces / Q000378:metabolism*
D005971:Glutamates; C041409:4-amino-3-chloro-2-pentenedioic acid