title: Mutarotase equilibrium exchange kinetics studied by 13C-NMR.
abstract: The rates of exchange between the alpha- and beta-anomers of D-[1-13C]glucose, at equilibrium catalyzed by porcine kidney mutarotase (EC 5.1.3.3), were measured using 13C-NMR spin-transfer procedures. This entailed inversion-transfer and saturation-transfer experiments, and two-dimensional exchange spectroscopy (2D EXSY). The concentration and temperature dependences of the fluxes were studied; equilibrium exchange Michaelis constants, and the activation energy of the catalyzed reaction were thereby measured.
authors.affiliation: Department of Biochemistry, University of Sydney, NSW, Australia.
authors.forename: P W
authors.initials: PW
authors.lastname: Kuchel
authors.forename: B T
authors.initials: BT
authors.lastname: Bulliman
authors.forename: B E
authors.initials: BE
authors.lastname: Chapman
mesh_terms: D002238:Carbohydrate Epimerases / Q000378:metabolism*; D002247:Carbon Isotopes; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008433:Mathematics; D008962:Models, Theoretical
chemical_list: D002247:Carbon Isotopes; D002238:Carbohydrate Epimerases; C019646:aldose 1-epimerase