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Phosphopentomutases

I. IDENTIFICATION OF TWO ACTIVITIES IN RABBIT TISSUES

From the ¹ From the Space Sciences Laboratory, University of California, Berkeley, California 94720

Crystalline rabbit muscle phosphoglucomutase (PG-mutase) was found to possess a low intrinsic activity for pentose phosphates. This activity was associated with each of the molecular forms of the enzyme protein.

The distribution of phosphopentomutase activity in rabbit tissues did not parallel the distribution of PG-mutase activity, but was tissue-specific, thus suggesting the occurrence of additional types of phosphopentomutase.

Two distinct phosphopentomutase activities were resolved by chromatography of tissue extracts on diethylaminoethyl cellulose at pH 7.0. These differed in catalytic properties and in molecular size.

One of the phosphopentomutase activities (Peak A) was probably a subsidiary function of PG-mutase protein. The other phosphopentomutase (Peak B) was much more active with pentose phosphates than with glucose phosphates, and represented a previously unrecognized enzyme, distinct from PG-mutase. Peak B phosphopentomutase was the predominant type found in most rabbit tissues, but was almost totally absent from muscle.

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				P. Maliekal, T. Sokolova, D. Vertommen, M. Veiga-da-Cunha, and E. Van Schaftingen Molecular Identification of Mammalian Phosphopentomutase and Glucose-1,6-bisphosphate Synthase, Two Members of the {alpha}-D-Phosphohexomutase Family J. Biol. Chem., November 2, 2007; 282(44): 31844 - 31851. [Abstract] [Full Text] [PDF]