All of the following enzymes catalyse a reaction involving substrate level phosphorylation, EXCEPT:
High-Yield Explanation
Substrate level phosphorylation is the biochemical process whereby ATP is produced from ADP through direct transfer of a high energy phosphoryl group from a reaction substrate to ADP. Enzymes which are involved in substrate level phosphorylation are pyruvate kinase, succinate thiokinase and phosphoglycerate kinase. Hexokinase is an enzyme involved in glycolysis which catalyse the conversion of glucose to glucose 6 phosphate using ATP as the phosphate donor. Under physiologic conditions this reaction is irreversible. Hexokinase is inhibited allosterically by its product, glucose 6-phosphate. Ref: Bender D.A., Mayes P.A. (2011). Chapter 17. The Citric Acid Cycle: The Catabolism of Acetyl-CoA. In D.A. Bender, K.M. Botham, P.A. Weil, P.J. Kennelly, R.K. Murray, V.W. Rodwell (Eds), Harper's Illustrated Biochemistry, 29e. Bender D.A., Mayes P.A. (2011). Chapter 18. Glycolysis & the Oxidation of Pyruvate. In D.A. Bender, K.M. Botham, P.A. Weil, P.J. Kennelly, R.K. Murray, V.W. Rodwell (Eds), Harper's Illustrated Biochemistry, 29e