Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase

Abhishek Chatterjee, N. Dinuka Abeydeera, Shridhar Bale, Pei-Jing Pai, Pieter C. Dorrestein, David H. Russell, Steven E. Ealick () and Tadhg P. Begley ()
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Abhishek Chatterjee: Cornell University
N. Dinuka Abeydeera: Texas A&M University, College Station, Texas 77843, USA
Shridhar Bale: Cornell University
Pei-Jing Pai: Texas A&M University, College Station, Texas 77843, USA
Pieter C. Dorrestein: Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, California 92093, USA
David H. Russell: Texas A&M University, College Station, Texas 77843, USA
Steven E. Ealick: Cornell University
Tadhg P. Begley: Texas A&M University, College Station, Texas 77843, USA

Nature, 2011, vol. 478, issue 7370, 542-546

Abstract: Suicidal enzyme involved in vitamin B1 synthesis Vitamin B1 (thiamin) was the first vitamin to be discovered more than a century ago, but some of the details of its biosynthesis remain unclear because of the complexity and novelty of this process. In yeast, the protein THI4p catalyses the assembly of the thiazole moiety of vitamin B1 in a complex reaction involving the conversion of NAD, glycine and sulphide to an adenylated carboxythiazole phosphate. The source of the sulphide and the mechanism by which it is incorporated into the thiazole is not known. Chatterjee et al. now report the first full reconstitution of THI4p-catalysed thiamin thiazole biosynthesis. They show that a conserved cysteine residue of THI4p acts as the source of sulphur, meaning that this protein is in fact a co-substrate of the biosynthetic pathway. THI4p can do this only once, so that it is a cofactor or 'suicide enzyme' rather that a true multi-turnover enzyme.

Date: 2011
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DOI: 10.1038/nature10503

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