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Mathemeier, Paul F. (Oregon State University, Corvallis), andRichard Y. Morita . Influence of substrate-cofactor ratios on partially purified inorganic pyrophosphatase activity at elevated temperatures. J. Bacteriol.88: 1661–1666. 1964.—Inorganic pyrophosphatase ofBacillus stearothermophilus was studied for optimal substrate-cofactor ratios at 60 to 100 C. Mg++ was the primary cofactor, and Co++ resulted in 50% enzyme activity at 60 C. The pH optima differed for the Mg++ activated and Co++ activated pyrophosphatase. At 80 C and above, Co++ replaced Mg++ as the optimal cofactor in the enzyme reaction. The optimal ratio of pyrophosphate to Mg++ varied from 2 to 0.25, dependent on enzyme concentration. The optimal pyrophosphate-cobalt ratio was constant at 1.0. The enzyme catalyzed appreciable pyrophosphate hydrolysis at 95 C.

INFLUENCE OF SUBSTRATE-COFACTOR RATIOS ON PARTIALLY PURIFIED INORGANIC PYROPHOSPHATASE ACTIVITY AT ELEVATED TEMPERATURES