Cloned (Comment) | Organism |
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expression in Escherichia coli | Saccharomyces cerevisiae |
Crystallization (Comment) | Organism |
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native protein to 1.8 A resolution. Thi4 exists as an homooctamer with the disordered and largely hydrophilic N-terminal regions located on the exterior of the molecule. The octamer has the shape of a ring with flattened sides. Adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid is bound to the Thi4 active site, which is located near the inner ring of the octameric complex.. NAD is the most likely precursor | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P32318 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + thiocarboxy-[sulfur-carrier protein ThiS] = 2-[(2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + [sulfur-carrier protein ThiS] + 2 H2O | the cofactor nicotinamide adenine dinucleotide is converted into adenosine diphospho-5-(beta-ethyl)-4-methylthiazole-2-carboxylic acid. The ADT ligand is tightly bound and can be released in vitro only upon protein denaturation. In this mechanism, cleavage of the N-glycosyl bond of NAD gives ADP-ribose.The first step in thiazole formation is similar to the chemistry used in ADP ribosylation | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
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Thi4 | - |
Saccharomyces cerevisiae |