Structural insights into regioselectivity in the enzymatic chlorination of tryptophan.

ABSTRACT: The regioselectively controlled introduction of chlorine into organic molecules is an important biological and chemical process. This importance derives from the observation that many pharmaceutically active natural products contain a chlorine atom. Flavin-dependent halogenases are one of the principal enzyme families responsible for regioselective halogenation of natural products. Structural studies of two flavin-dependent tryptophan 7-halogenases (PrnA and RebH) have generated important insights into the chemical mechanism of halogenation by this enzyme family. These proteins comprise two modules: a flavin adenine dinucleotide (FAD)-binding module and a tryptophan-binding module. Although the 7-halogenase studies advance a hypothesis for regioselectivity, this has never been experimental

SUBMITTER: Zhu X 

PROVIDER: S-EPMC2713781 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature