Substrate specificity of an oxygen dependent sulfoxide synthase in ovothiol biosynthesis

Gabriel T M Mashabela; Florian P Seebeck

doi:10.1039/c3cc42594k

Substrate specificity of an oxygen dependent sulfoxide synthase in ovothiol biosynthesis

Chem Commun (Camb). 2013 Sep 11;49(70):7714-6. doi: 10.1039/c3cc42594k.

Authors

Gabriel T M Mashabela¹, Florian P Seebeck

Affiliation

¹ Department for Chemistry, University of Basel, St. Johanns-Ring 19, Basel, Switzerland.

PMID: 23877651
DOI: 10.1039/c3cc42594k

Abstract

OvoA is an iron(II) dependent sulfoxide synthase which catalyzes the first step in ovothiol A biosynthesis. This enzyme sulphurizes the C5 position of the imidazole side chain of L-histidine. We report the substrate specificity profile of this catalyst and present data which indicate that OvoA catalysis follows an thiol-ene type mechanism.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Bacterial Proteins / metabolism*
Biocatalysis
Erwinia / enzymology
Imidazoles / chemistry
Iron / chemistry
Kinetics
Methylhistidines / chemistry
Methylhistidines / metabolism*
Oxidoreductases Acting on Sulfur Group Donors / metabolism*
Oxygen / chemistry*
Oxygen / metabolism
Substrate Specificity

Substances

Bacterial Proteins
Imidazoles
Methylhistidines
ovothiol A
imidazole
Iron
Oxidoreductases Acting on Sulfur Group Donors
Oxygen