Saccharomyces cerevisiae THI4p is a suicide thiamine thiazole synthase

Article

关键词: ESCHERICHIA-COLI;    BIOSYNTHESIS;    ENZYME;    EUKARYOTES;    GENE;    IDENTIFICATION;    PROTEIN;   

DOI  :  10.1038/nature10503

来源: SCIE

【 摘 要 】

Thiamine pyrophosphate 1 is an essential cofactor in all living systems(1). Its biosynthesis involves the separate syntheses of the pyrimidine 2 and thiazole 3 precursors, which are then coupled(2). Two biosynthetic routes to the thiamine thiazole have been identified. In prokaryotes, five enzymes act on three substrates to produce the thiazole via a complex oxidative condensation reaction, the mechanistic details of which are now well established(2-6). In contrast, only one gene product is involved in thiazole biosynthesis in eukaryotes (THI4p in Saccharomyces cerevisiae)(7). Here we report the preparation of fully active recombinant wild-type THI4p, the identification of an iron-dependent sulphide transfer reaction from a conserved cysteine residue of the protein to a reaction intermediate and the demonstration that THI4p is a suicide enzyme undergoing only a single turnover.

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