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Binds Zn2+. The enzyme catalyses the adenylation of ThiS, a sulfur carrier protein involved in the biosynthesis of thiamine.
The enzyme shows significant structural similarity to ubiquitin-activating enzyme [3,4]. In Escherichia coli, but not in Bacillus subtilis, the enzyme forms a cross link from Cys-184 to the ThiS carboxy terminus (the position that is also thiolated) via an acyldisulfide .
inactive, C184S is equally effective in catalyzing the formation of [ThiS]-COSH as the wild type enzyme. Cys184 is directly involved in the crosslinking of ThiF to ThiS but is not essential for the formation of [ThiS]-COSH