A Kinetic Study of Enzyme Catalyzed Glucose Mutarotation at Variable Pressure and pH.

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Abstract
The enzyme mutarotase (5.1.3.3) [pig kidney] acting on the .alpha./.beta.-anomerization of glucose was studied at pressure from 1-1000 bar and over the pH range from 5.50-6.75. In contrast to the spontaneous, acid-base catalyzed mutarotation, the enzymatic mutarotation was independent of pressure, invalidating the generally accepted view that the 2 reactions are identical in mechanism. The pH sensitivity of the Michaelis parameters Km and Vmax supports the idea of histidine as a necessary component of the active center in the enzyme.