Enzymatic Catalysis of Proton Transfer at Carbon: Activation of Triosephosphate Isomerase by Phosphite Dianion
- 20 April 2007
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 46 (19) , 5841-5854
- https://doi.org/10.1021/bi700409b
Abstract
No abstract availableKeywords
This publication has 80 references indexed in Scilit:
- Solution NMR and Computer Simulation Studies of Active Site Loop Motion in Triosephosphate IsomeraseBiochemistry, 2006
- Activation of Orotidine 5‘-Monophosphate Decarboxylase by Phosphite Dianion: The Whole Substrate is the Sum of Two PartsJournal of the American Chemical Society, 2005
- Crystal Structure of Triosephosphate Isomerase Complexed with 2-Phosphoglycolate at 0.83-Å ResolutionJournal of Biological Chemistry, 2003
- Proton Transfer in the Mechanism of Triosephosphate IsomeraseBiochemistry, 1998
- Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomeraseJournal of Molecular Biology, 1992
- Refined 1.83 Å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4 m-ammonium sulphateJournal of Molecular Biology, 1991
- The form of 2-phosphoglycollic acid bound by triosephosphate isomeraseBiochemical and Biophysical Research Communications, 1978
- Apparent equivalence of the active-site glutamyl residue and the essential group with pKa 6.0 in triosephosphate isomeraseBiochemical and Biophysical Research Communications, 1977
- Phosphorus-31 nuclear magnetic resonance of dihydroxyacetone phosphate in the presence of triosephosphate isomerase. The question of nonproductive binding of the substrate hydrateBiochemistry, 1977
- Changes in absorption spectrum and crystal structure of triose phosphate isomerase brought about by 2-phosphoglycollate, a potential transition state analogueJournal of Molecular Biology, 1970