1977
DOI: 10.1128/iai.17.3.510-512.1977
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Regulation of invertase of Actinomyces viscosus

Abstract: The regulation of diethylaminoethyl-partially purified invertase (EC 3.2.1.26; ,8-D-fructofuranoside fructohydrolase) from the 37,000 x g-soluble intracellular fluid of Actinomyces viscosus serotype 2 strain M-100 was studied. Glycolytic intermediates, mono-, di-, and triphosphate nucleotides, inorganic phosphate, and various divalent cations were tested for regulatory effects. Fructose-6-phosphate (F6P) and fructose-1,6-diphosphate (FDP) were found to act as noncompetitive inhibitors of invertase. The Ki valu… Show more

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Cited by 8 publications
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“…A feedback regulation of the glycolytic products on the invertase activity is possible, but not proven in reports on invertases from cariogenic streptococci (19,28,30). Only one report on invertase from Aetinomyces viscosus (18) has shown that the enzyme activity was inhibited by fructose-6-phosphate and fructose-1,6-diphosphate. So thedeliberate elimination of the glycolytic pathway is presumably unimportant to the invertase activity measured, but necessary for an exact assay.…”
Section: Discussionmentioning
confidence: 99%
“…A feedback regulation of the glycolytic products on the invertase activity is possible, but not proven in reports on invertases from cariogenic streptococci (19,28,30). Only one report on invertase from Aetinomyces viscosus (18) has shown that the enzyme activity was inhibited by fructose-6-phosphate and fructose-1,6-diphosphate. So thedeliberate elimination of the glycolytic pathway is presumably unimportant to the invertase activity measured, but necessary for an exact assay.…”
Section: Discussionmentioning
confidence: 99%