Jason J. Reddick
Cornell University
9 Papers
64 Citations
Jason J. Reddick is an academic researcher from Cornell University. The author has contributed to research in topics: Pyrophosphate & Biosynthesis. The author has an hindex of 8, co-authored 9 publications.
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Papers
Thiamin biosynthesis in prokaryotes.
Tadhg P. Begley,Diana M. Downs,Steven E. Ealick,Fred W. McLafferty,Van Loon Ap,Sean V. Taylor,Nino Campobasso,Hsiu-Ju Chiu,Cynthia Kinsland,Jason J. Reddick,Jun Xi +10 more
TL;DR: The X-ray structures of thiamin phosphate synthase and 5-hydroxyethyl-4-methylthiazole kinase have been completed and the genes coding for the thienin transport system (thiBPQ) have been identified.
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Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase.
Diane H. Peapus,Hsiu-Ju Chiu,Nino Campobasso,Jason J. Reddick,Tadhg P. Begley,Steven E. Ealick +5 more
TL;DR: In this article, the active site density of S130A thiamin pyrophosphate synthase is modeled as the electron density of a carbenium ion intermediate, consistent with a carbine ion intermediate.
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Overexpression, purification and characterization of two pyrimidine kinases involved in the biosynthesis of thiamin: 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase and 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate kinase
Jason J. Reddick,Cynthia Kinsland,Robb Nicewonger,Todd Christian,Diana M. Downs,Malcolm E. Winkler,Tadhg P. Begley +6 more
TL;DR: These enzymes are useful reagents for the preparation of intermediates on the thiamin biosynthetic pathway and Surprisingly HMP-P kinase also shows HMP kinase activity.
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Mechanistic studies on thiamin phosphate synthase: evidence for a dissociative mechanism.
TL;DR: It is demonstrated that 4-amino-5-(hydroxymethyl)-2-methoxypyrimidine pyrophosphate (CH(3)O-HMP-PP) is a very poor substrate for thiamin phosphate synthase and that the enzyme catalyzes positional isotope exchange.
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Thiamin phosphate synthase
D.H. Peapus,Hsiu-Ju Chiu,Nino Campobasso,Jason J. Reddick,Tadhg P. Begley,Steven E. Ealick +5 more
- 26 Sep 2001
TL;DR: Seven new crystal structures primarily involving crystals of S130A thiamin phosphate synthase soaked in solutions containing substrates or products are reported, which suggest that the reaction proceeds via a dissociative mechanism.
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