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Summary: Two distinct forms of fructose 1,6-bisphosphatase, designated form A and form B, have been partially purified from autotrophically grown cells of the hydrogen bacterium Nocardia opaca 1b. Form A was present when the organism was grown under autotrophic conditions but was not synthesized during heterotrophic growth. Form B was detected in both autotrophically and heterotrophically grown organisms, suggesting that it is a constitutive enzyme. The molecular weights were estimated to be 140000 for form A and 190000 for form B. Both purified enzymes showed fructose bisphosphatase as well as sedoheptulose bisphosphatase activity, with pH optima of 8.2 and 8.8 to 9.0 for forms A and B, respectively. The ratio of fructose bisphosphatase to sedoheptulose bisphosphatase activity was 0.6 for form A and about 4.5 for form B. The enzymes required Mg2+ for activity; Mm2+ could only partially replace Mg2+. Form A was inhibited by ATP and ribulose bisphosphate. AMP exerted a strong allosteric inhibition on form B which was also inhibited by NAD+ and NADH. Phosphoeno/pyruvate activated form B. On the basis of these results, different physiological roles for the two forms of fructose bisphosphatase are suggested.

Characterization of Two Fructose Bisphosphatase Isoenzymes from the Hydrogen Bacterium Nocardia opaca 1b