A kinetically important phosphoryl-enzyme intermediary in the intrinsic purine nucleoside-5′-diphosphokinase activity of Escherichia coli acetate kinase
- 1 May 1976
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 174 (1) , 120-128
- https://doi.org/10.1016/0003-9861(76)90330-1
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Studies on the kinetic mechanism and the phosphoryl-enzyme compound of the Escherichia coli acetate kinase reactionArchives of Biochemistry and Biophysics, 1976
- Evidence for the formation of a γ-phosphorylated glutamyl residue in the Escherichia coli acetate kinase reactionBiochemical and Biophysical Research Communications, 1974
- The Inhibition of Acetate, Pyruvate, and 3-Phosphoglycerate Kinase by Chromium Adenosine TriphosphatePublished by Elsevier ,1974
- Preparation and properties of chromium(III)-nucleotide complexes for use in the study of enzyme mechanismsBiochemistry, 1973
- Phosphorylated Acetate KinasePublished by Elsevier ,1972
- Evaluation of the phosphoryl-enzyme intermediate concept in the acetate kinase and hexokinase reactions from kinetic studiesArchives of Biochemistry and Biophysics, 1972
- Molecular species of a soluble nucleoside diphosphokinase related to the Na+, K+-ATPaseBiochemical and Biophysical Research Communications, 1971
- Preparation of Crystalline Nucleoside Diphosphate Kinase from Baker's Yeast and Identification of 1‐[32P]Phosphohistidine as the Main Phosphorylated Product of an Alkaline Hydrolysate of Enzyme Incubated with Adenosine [32P]TriphosphateEuropean Journal of Biochemistry, 1969
- Identification of a Phosphate-incorporating Protein from Bovine Liver as Nucleoside Diphosphate Kinase and Isolation of l-32P-Phosphohistidine, 3-32P-Phosphohistidine, and N-ε-32-P-Phospholysine from Erythrocytic Nucleoside Diphosphate Kinase, Incubated with Adenosine Triphosphate-32PPublished by Elsevier ,1968
- The Relationship between Michaelis Constants, Maximum Velocities and the Equilibrium Constant for an Enzyme-catalyzed ReactionJournal of the American Chemical Society, 1953