Mutarotase equilibrium exchange kinetics studied by 13C-NMR.
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.
Kuchel
P W
PW
Department of Biochemistry, University of Sydney, NSW, Australia.
Bulliman
B T
BT
Chapman
B E
BE
D002238:Carbohydrate Epimerases / Q000378:metabolism*; D002247:Carbon Isotopes; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008433:Mathematics; D008962:Models, Theoretical
D002247:Carbon Isotopes; D002238:Carbohydrate Epimerases; C019646:aldose 1-epimerase