Formyl phosphate: a proposed intermediate in the reaction catalyzed by Escherichia coli PurT GAR transformylase

Biochemistry
A MarolewskiS J Benkovic

Abstract

The Escherichia coli purT encoded glycinamide ribonucleotide transformylase (GAR transformylase) serves as an alternate enzyme in the production of formyl GAR for use in de novo purine biosynthesis. This enzyme differs from the previously known purN encoded enzyme in size, sequence, and substrates; ATP and formate are required as opposed to formyl tetrahydrofolate. Kinetic studies of the wild-type PurT enzyme described here demonstrate that formyl phosphate behaves as a chemically and kinetically competent intermediate. The requirement for ATP and GAR in these reactions is consistent with previous steady-state kinetic results, which demonstrated that all substrates must be bound before catalysis. Kinetic characterization of a mutant, which releases formyl phosphate into solution, and positional isotope exchange studies also support the assignment of formyl phosphate as a plausible intermediate.

References

Sep 1, 1973·CRC Critical Reviews in Biochemistry·R H Himes, J A Harmony
Jun 1, 1993·Journal of Bacteriology·P Nygaard, J M Smith

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Citations

Aug 21, 2008·Cellular and Molecular Life Sciences : CMLS·Y ZhangS E Ealick
Sep 28, 2000·Current Opinion in Chemical Biology·T J KappockJ Stubbe
Jan 27, 2007·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·William Martin, Michael J Russell
Sep 17, 2011·Bioorganic Chemistry·Maria V FawazSteven M Firestine
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Apr 23, 2009·Protein Science : a Publication of the Protein Society·Hui LiStephen J Benkovic
Oct 16, 2012·Biochimica Et Biophysica Acta·Elbert Branscomb, Michael J Russell
Sep 1, 2008·EcoSal Plus·Kaj Frank JensenMartin WillemoËs

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