Escherichia coli acetate kinase mechanism studied by net initial rate, equilibrium, and independent isotopic exchange kinetics.
Open Access
- 1 November 1976
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 251 (21) , 6775-6783
- https://doi.org/10.1016/s0021-9258(17)33012-0
Abstract
No abstract availableThis publication has 33 references indexed in Scilit:
- Evidence for the formation of a γ-phosphorylated glutamyl residue in the Escherichia coli acetate kinase reactionBiochemical and Biophysical Research Communications, 1974
- Equilibrium kinetic study of bovine liver glutamate dehydrogenase at high pHBiochemistry, 1974
- Preparation and properties of chromium(III)-nucleotide complexes for use in the study of enzyme mechanismsBiochemistry, 1973
- Evaluation of the phosphoryl-enzyme intermediate concept in the acetate kinase and hexokinase reactions from kinetic studiesArchives of Biochemistry and Biophysics, 1972
- Equilibrium kinetic study of enzyme modifier actionBiochimica et Biophysica Acta (BBA) - Enzymology, 1970
- Kinetic study of yeast nucleosidediphosphate kinaseBiochemistry, 1969
- The kinetics of enzyme-catalyzed reactions with two or more substrates or productsBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1963
- Equilibrium Reaction Rates and Enzyme Mechanisms.Acta Chemica Scandinavica, 1963
- Protein chromatography on calcium phosphate columnsArchives of Biochemistry and Biophysics, 1956
- STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONSBiological Reviews, 1953