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Volume 113, Issue 2

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

Abstract

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 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 Mg for activity; Mn could only partially replace Mg. 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. Phospho /pyruvate activated form B. On the basis of these results, different physiological roles for the two forms of fructose bisphosphatase are suggested.

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© Society for General Microbiology, 1979
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1979-08-01
2024-04-18
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Characterization of Two Fructose Bisphosphatase Isoenzymes from the Hydrogen Bacterium Nocardia opaca 1b
Microbiology 113, 347 (1979); https://doi.org/10.1099/00221287-113-2-347
/content/journal/micro/10.1099/00221287-113-2-347
/content/journal/micro/10.1099/00221287-113-2-347
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