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

abstract

• 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.

authors

• Begley, Tadhg

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

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Amino Acid Sequence
• Bacillus Subtilis
• Catalysis
• Deuterium Exchange Measurement
• Imines
• Molecular Sequence Data
• Nuclear Magnetic Resonance, Biomolecular
• Organophosphates
• Oxygen
• Pentosephosphates
• Thiamine
• Thiazoles
• Transferases

PubMed Central ID

• 15012138

Digital Object Identifier (DOI)

• 10.1021/ja039616p

start page

• 3091

end page

• 3096

volume

• 126

issue

• 10

URL

• http%3A%2F%2Fdx.doi.org%2F10.1021%2Fja039616p