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Regulation of invertase ec 3.2.1.26 of actinomyces viscosus


, : Regulation of invertase ec 3.2.1.26 of actinomyces viscosus. Infection and Immunity 17(3): 510-512

The regulation of DEAE-partially purified invertase (EC 3.2.1.26; .beta.-D-fructofuranoside fructohydrolase) from the 37,000 .times. g-soluble intracellular fluid of A. viscosus serotype 2 strain M-100 was studied. Glycolytic intermediates; mono-, di and triphosphate nucleotides; Pi; and various divalent cations were tested for regulatory effects. Fructose-6-phosphate (F6P) and fructose-1,6-diphosphate (FDP) acted as noncompetitive inhibitors of invertase. The Ki [inhibition constant] values for F6P and FDP were 3.4 and 5.1 mM, respectively. The Hill coefficient for sucrose was 1.03 and remained unchanged in the presence of varying amounts of F6P or FDP.

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Related references

Kiel, R.A.; Tanzer, J.M., 1977: Regulation of invertase of Actinomyces viscosus. The regulation of diethylaminoethyl-partially purified invertase (EC 3.2.1.26; beta-D-fructofuranoside fructohydrolase) from the 37,000 X g-soluble intracellular fluid of Actinomyces viscosus serotype 2 strain M-100 was studied. Glycolytic interme...

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Brown A.T.; Christian C.P.; Eifert R.L., 1975: Regulation of lactate dehydrogenase and pyruvate carboxylase activity in actinomyces viscosus. Abstracts of the Annual Meeting of the American Society for Microbiology 75: 179