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Literature summary for 2.4.2.60 extracted from

  • Chatterjee, A.; Jurgenson, C.; Schroeder, F.; Ealick, S.; Begley, T.
    Thiamin biosynthesis in eukaryotes Characterization of the enzyme-bound product of thiazole synthase from Saccharomyces cerevisiae and its implications in thiazole biosynthesis (2006), J. Am. Chem. Soc., 128, 7158-7159 .
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P32318
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Saccharomyces cerevisiae ATCC 204508 P32318
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mechanism starts with cleavage of the N-glycosyl bond of NAD followed by ring opening, tautomerization and loss of water. Reaction continues with imine formation, tautomerization, sulfide addition and cyclization. Elimination of two water molecules followed by a tautomerization completes the formation of the thiazole moiety Saccharomyces cerevisiae ?
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additional information mechanism starts with cleavage of the N-glycosyl bond of NAD followed by ring opening, tautomerization and loss of water. Reaction continues with imine formation, tautomerization, sulfide addition and cyclization. Elimination of two water molecules followed by a tautomerization completes the formation of the thiazole moiety Saccharomyces cerevisiae ATCC 204508 ?
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General Information

General Information Comment Organism
physiological function protein Thi4 from Saccharomyces cerevisiae fails to catalyze the formation of the thiazole moiety from cysteine (or sulfide), glycine and a variety of C5 carbohydrates. Thi4 also fails to complement an Escherichia coli thiazole biosynthetic mutant ThiF. The ADP adduct of 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid is present at the active site of Thi4 and the carboxylic acid of the thiazole forms hydrogen bonding and electrostatic interactions with Arg301 Saccharomyces cerevisiae