Thiamin Biosynthesis in Bacillus subtilis: Structure of the Thiazole Synthase

Thiazole synthase complexed with the sulfur carrier protein consists of a tetramer of ThiS/thiazole synthase heterodimers. ThiS is a 7.2 kDa protein with a ubiquitin-like fold, and thiazole synthase is a 26.9 kDa protein. The mechanism of the early steps catalyzed by thiazole synthase have been elucidated, and an imine between the DXP substrate and lysine 96 has been characterized. The thiazole synthase sequence is highly conserved in bacteria and shows similarity to thiamin phosphate synthase, a member of the flavin mononucleotide dependent oxidoreductase and phosphate binding (FMOP) superfamilies of ( )8 barrel enzymes.

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