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 [¹⁵N]- and [¹³C]-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 FADH₂-dependent halogenase is involved.