Published in

Wiley, Angewandte Chemie International Edition, 23(41), p. 4529-4532, 2002

DOI: 10.1002/1521-3773(20021202)41:23<4529::aid-anie4529>3.0.co;2-2

Links

Tools

Export citation

Search in Google Scholar

Mechanistic Studies of HPP Epoxidase: Configuration of the Substrate Governs Its Enzymatic Fate

This paper is available in a repository.
This paper is available in a repository.

Full text: Download

Green circle
Preprint: archiving allowed
Orange circle
Postprint: archiving restricted
Red circle
Published version: archiving forbidden
Data provided by SHERPA/RoMEO

Abstract

The regiospecificity of the initial H-atom abstraction may explain the fact that HPP epoxidase, a non-heme iron-containing enzyme, catalyzes not only the conversion of (S)-HPP ((S)-1) to fosfomycin (2), but also the oxidation of the 1R enantiomer, which leads exclusively to 3 with nearly equal efficiency.