Biosynthetic Origin of [R-(Z)]-4-Amino-3-chloro-2-pentenedioic Acid inStreptomyces viridogenes | Zendy

Robin I. HUTCHINSON | Zendy; Russell J. Grant | Zendy; Cormac D. Murphy | Zendy

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Biosynthetic Origin of [R-(Z)]-4-Amino-3-chloro-2-pentenedioic Acid inStreptomyces viridogenes

Author(s) -

Robin I. HUTCHINSON,

Russell J. Grant,

Cormac D. Murphy

Publication year - 2006

Publication title -

bioscience biotechnology and biochemistry

Language(s) - Uncategorized

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.60372

Subject(s) - proline , biosynthesis , amino acid , streptomyces , stereochemistry , chemistry , biochemistry , deuterium , bacteria , biology , enzyme , physics , quantum mechanics , genetics

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.

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