Mechanistic and structural studies on thiamin biosynthetic enzymes

ORGN 256

Tadhg Begley, tpb2@cornell.edu, Department of Chemistry and Chemical Biology, Cornell University, Baker Laboratory, Ithaca, NY 14853
Thiamin pyrophosphate is an essential cofactor in all-living systems and consists of a pyrimidine covalently linked to a thiazole. The biosynthesis of thiamin is complex and different from any of the characterized chemical or biochemical routes to these heterocycles. The thiazole is formed from deoxy-D-xylulose-5-phosphate, glycine and a protein thiocarboxylate in a reaction catalyzed by four enzymes, while the pyrimidine is formed by a remarkable rearrangement of aminoimidazole ribotide. This lecture will describe the current status of our mechanistic and structural studies on the thiamin biosynthetic enzymes in bacteria.