Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy
- 5 February 1980
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 19 (3) , 472-477
- https://doi.org/10.1021/bi00544a012
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 14 references indexed in Scilit:
- Evolution of enzyme function and the development of catalytic efficiencyBiochemistry, 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
- Proton Exchange of the Pro‐S Hydrogen at C‐1 in Dihydroxyacetone Phosphate D‐Fructose 1, 6‐Bisphosphate and d‐Fructosehate, d‐Fructose 1,6‐Bisphosphate and Catalysed by Rabbit‐Muscle AldolaseEuropean Journal of Biochemistry, 1976
- Isotope effects in the binding of NADH to equine liver alcohol dehydrogenaseBiochemistry, 1976
- Fructose 1,6-bisphosphate: isomeric composition, kinetics, and substrate specificity for the aldolasesBiochemistry, 1976
- Infrared Studies on the Mechanism of Action of Carbonic AnhydraseJournal of Biological Chemistry, 1968
- Infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin, and heme carbonylsBiochemistry, 1968
- Isotope and solvent effects of deuterium on rabbit-muscle lactate dehydrogenaseBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
- The Mechanism of the Triosephosphate Isomerase ReactionJournal of Biological Chemistry, 1959