Identification and characterization of the first ovothiol biosynthetic enzyme

Andrea Braunshausen; Florian P Seebeck

doi:10.1021/ja109378e

Identification and characterization of the first ovothiol biosynthetic enzyme

J Am Chem Soc. 2011 Feb 16;133(6):1757-9. doi: 10.1021/ja109378e. Epub 2011 Jan 19.

Authors

Andrea Braunshausen¹, Florian P Seebeck

Affiliation

¹ Abteilung Physikalische Biochemie, Max Planck Institut für Molekulare Physiologie, Otto-Hahn Strasse 11, 44227 Dortmund, Germany.

PMID: 21247153
DOI: 10.1021/ja109378e

Abstract

Ovothiols are histidine-derived thiols that were first isolated from marine invertebrates. We have identified a 5-histidylcysteine sulfoxide synthase (OvoA) as the first ovothiol biosynthetic enzyme and characterized OvoAs from Erwinia tasmaniensis and Trypanosoma cruzi . Homologous enzymes are encoded in more than 80 genomes ranging from proteobacteria to animalia.

Publication types

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

MeSH terms

Animals
Carbon-Sulfur Ligases / chemistry
Carbon-Sulfur Ligases / genetics
Carbon-Sulfur Ligases / metabolism*
Erwinia / enzymology*
Genome / genetics
Methylhistidines / metabolism*
Protein Structure, Tertiary
Trypanosoma cruzi / enzymology*

Substances

Methylhistidines
ovothiol C
Carbon-Sulfur Ligases