Apparent equivalence of the active-site glutamyl residue and the essential group with pKa 6.0 in triosephosphate isomerase
- 1 July 1977
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 77 (2) , 746-752
- https://doi.org/10.1016/s0006-291x(77)80041-7
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Energetics of triosephosphate isomerase: deuterium isotope effects in the enzyme-catalyzed reactionBiochemistry, 1976
- Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate glyceraldehyde 3-phosphate and in productBiochemistry, 1976
- Free-energy profile for the reaction catalyzed by triosephosphate isomeraseBiochemistry, 1976
- Energetics of triosephosphate isomerase: the nature of the proton transfer between the catalytic base and solvent waterBiochemistry, 1976
- Energetics of triosephosphate isomerase: the fate of the 1(R)-3H label of tritiated dihydroxyacetone phosphate in the isomerase reactionBiochemistry, 1976
- Energetics of triosephosphate isomerase: the appearance of solvent tritium in substrate dihydroxyacetone phosphate and in productBiochemistry, 1976
- Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosineBiochemical Journal, 1972
- pH-dependence of the triose phosphate isomerase reactionBiochemical Journal, 1972
- The active centre of rabbit muscle triose phosphate isomerase. The site that is labelled by glycidol phosphateBiochemical Journal, 1971
- Haloacetol phosphates. Characterization of the active site of rabbit muscle triose phosphate isomeraseBiochemistry, 1971