title: Synthetic Utility of Yeast Hexokinase. Substrate Specificity, Cofactor Regeneration, and Product Isolation.
abstract: Yeast hexokinase (EC 2.7.1.1) catalyzes the phosphorylation of pyranose and furanose analogs of glucose at 0.01-125% of the rate of glucose. The enzyme is highly tolerant of structural changes at C-2 and C-3 of glucopyranose and less tolerant of changes at C-1 and C-4. Preparative phosphorylations were performed on compounds having 0.01-100% of the activity of glucose, using phosphoenolpyruvate and pyruvate kinase to regenerate ATP. The effects of inhibition of hexokinase by phosphoenolpyruvate and acetyl phosphate on cofactor regeneration are discussed.
authors.affiliation: Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716.
authors.forename: H. Keith
authors.initials: HK
authors.lastname: Chenault
authors.forename: Robert F.
authors.initials: RF
authors.lastname: Mandes
authors.forename: Keith R.
authors.initials: KR
authors.lastname: Hornberger