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J. Biol. Chem., Vol. 269, Issue 15, 10996-11001, Apr, 1994
H Wurst and A Kornberg
A soluble polyphosphatase of Saccharomyces cerevisiae, purified to apparent
homogeneity, is monomeric with a molecular mass of 40 kDa. It acts as an
exoenzyme in a processive mode releasing orthophosphate residues from long
polyphosphate chains until pyrophosphate is reached. Polyphosphates of all
the lengths examined are used as substrates with a preference for those of
about 250 residues. These are degraded with a kcat/Km near the limit for
diffusion-controlled reactions. At 37 degrees C, the enzyme releases about
500 phosphate residues/s. It does not act on pyrophosphate, ATP, or the
cyclic form of tripolyphosphate. For optimal activity the enzyme requires
magnesium, manganese, or cobalt.
A soluble exopolyphosphatase of Saccharomyces cerevisiae. Purification and characterization
Department of Biochemistry, Stanford University School of Medicine, California 94305-5307.
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