The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1): the early steps catalyzed by thiazole synthase. Academic Article uri icon


  • Thiazole synthase (ThiG) catalyzes an Amadori-type rearrangement of 1-deoxy-d-xylulose-5-phosphate (DXP) via an imine intermediate. In support of this, we have demonstrated enzyme-catalyzed exchange of the C2 carbonyl of DXP. Borohydride reduction of the enzyme DXP imine followed by top-down mass spectrometric analysis localized the imine to lysine 96. On the basis of these observations, a new mechanism for the biosynthesis of the thiazole phosphate moiety of thiamin pyrophosphate in Bacillus subtilis is proposed. This mechanism involves the generation of a ketone at C3 of DXP by an Amadori-type rearrangement of the imine followed by nucleophillic addition of the sulfur carrier protein (ThiS-thiocarboxylate) to this carbonyl group.

published proceedings

  • J Am Chem Soc

altmetric score

  • 4.5

author list (cited authors)

  • Dorrestein, P. C., Zhai, H., Taylor, S. V., McLafferty, F. W., & Begley, T. P.

citation count

  • 40

complete list of authors

  • Dorrestein, Pieter C||Zhai, Huili||Taylor, Sean V||McLafferty, Fred W||Begley, Tadhg P

publication date

  • March 2004