On the mechanism of ATP cleavage in the phosphoenolpyruvate synthase reaction of Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference14 articles.
1. Net formation of phosphoenolpyruvate from pyruvate by Escherichia coli
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4. R.A. Cooper and H.L. Kornberg, Proc. Roy. Soc. London, Ser. B, in the press.
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1. Symmetry in the 2.25 MDa homomultimeric phosphoenolpyruvate synthase fromStaphylothermus marinus: Analyses of negatively stained preparations;Micron;1998-04
2. NMR and isotopic exchange studies of the site of bond cleavage in the MutT reaction.;Journal of Biological Chemistry;1992-10
3. Characterization of phosphoenolpyruvate synthase mutants in Salmonella typhimurium;Archives of Microbiology;1989-12
4. The mode of triple phosphoryl group transfer in pyruvate phosphate dikinase catalysis. Demonstration of the intermediacy of pyrophosphorylated and phosphorylated enzyme species;Journal of the American Chemical Society;1989-07
5. Phosphoenolpyruvate synthetase and pyruvate, orthophosphate dikinase: stereochemical consequences at both the .beta.-phospho and .gamma.-phospho groups of ATP;Biochemistry;1985-01
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