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Literature summary for 2.8.1.10 extracted from

  • Jurgenson, C.T.; Chatterjee, A.; Begley, T.P.; Ealick, S.E.
    Structural insights into the function of the thiamin biosynthetic enzyme Thi4 from Saccharomyces cerevisiae (2006), Biochemistry, 45, 11061-11070.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P32318
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-

Reaction

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

Synonyms Comment Organism
Thi4
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Saccharomyces cerevisiae