The catalytic activity of muscle phosphoglucomutase in the crystalline phase.

A suspension of microcrystals of phosphoglucomutase in 60% ammonium sulfate exhibits a maximal catalytic activity in substrate-velocity studies that is about 0.2 of that obtained with the soluble enzyme under the same conditions. The apparent Michaelis constants for the reaction in the crystal phase are altered to an even smaller extent, relative to that in solution, although the parameters for the monophosphate and bisphosphate are increased more than 3 and more than 5 orders of magnitude, respectively, by the sulfate present. The compatibility of larger crystals with a reaction that constitutes part of the catalytic process also is demonstrated.