Biosynthetic Origin of [R-(Z)]-4-Amino-3-chloro-2-pentenedioic Acid in Streptomyces viridogenes
The biosynthesis of the chlorinated amino acid [<I>R</I>-(<I>Z</I>)]-4-amino-3-chloro-2-pentenedioic acid (ACPA) was investigated. Feeding studies with <I>Streptomyces viridogenes</I> were conducted in resting cells. Substantial incorporation from [<SUP>15</SUP>N]- and [<SUP>13</SUP>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 <I>via</I> a radical mechanism, but rather suggest that a FADH<SUB>2</SUB>-dependent halogenase is involved.
- Bioscience, biotechnology, and biochemistry
Bioscience, biotechnology, and biochemistry 70(12), 3046-3049, 2006-12-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry