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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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 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 values for F6P and FDP were found to be 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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PMID:Regulation of invertase of Actinomyces viscosus. 90 75

The synthesis of the glycoprotein enzymes, invertase and acid phosphatase, by protoplasts of Saccharomyces mutant 1016, is inhibited by 2-deoxy-d-glucose (2-dG) after a 20- to 30-min lag period under conditions (external sugar to 2-dG ratio of 40:1) which cause only a slight decrease in total protein synthesis. Formation of one intracellular enzyme, alpha-glucosidase, is also sensitive, but production of another, alkaline phosphatase, is unaffected. A nonmetabolized glucose analogue, 6-deoxy-d-glucose, had no inhibitory effect. The total uptake of external fructose and maltose was decreased by 2-dG after a lag period of about the same duration as that before the inhibition of synthesis of enzymes or of mannan and glucan; during this time 2-dG was taken up by the protoplasts and accumulated primarily as 2-dG-6-phosphate (2-dG-6-P). Studies in vitro showed that 2-dG-6-P inhibits both yeast phosphoglucose isomerase and phosphomannose isomerase. The intracellular levels of the 6-phosphates of glucose, fructose, and mannose did not increase in the presence of 2-dG. We suggest that the high internal level of 2-dG-6-P blocks synthesis of the cell wall polysaccharides and glycoproteins in two ways. It directly inhibits the conversion of fructose-6-P to glucose-6-P and to mannose-6-P. At the same time, it restricts the transport of fructose and maltose into the cell; however, the continuing limited uptake of the sugars still provides sufficient energy for protein synthesis. The cessation of alpha-glucosidase synthesis is probably a result of depletion of the internal pool of maltose (the inducer). Our findings support the suggestion that restriction of synthesis of the carbohydrate moiety of glycoproteins reduces formation of the active enzyme.
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PMID:Inhibition by 2-deoxy-D-glucose of synthesis of glycoprotein enzymes by protoplasts of Saccharomyces: relation to inhibition of sugar uptake and metabolism. 505 66

Plants and most cyanobacteria metabolize sucrose (Suc) with a similar set of enzymes. In Synechococcus sp. PCC 7002, a marine cyanobacterium strain, genes involved in Suc synthesis (spsA and sppA) have been characterized; however, its breakdown was still unknown. Indeed, neither invertase nor sucrose synthase genes, usually found in plants and cyanobacteria, were found in that Synechococcus genome. In the present study, we functionally characterized the amsA gene that codes for an amylosucrase (AMS), a glycoside-hydrolase family 13 enzyme described in bacteria, which may catabolyze Suc in Synechococcus. Additionally, we identified and characterized the frkA gene that codes for a fructokinase (FRK), enzyme that yields fructose-6P, one of the substrates for Suc synthesis. Interestingly, we demonstrate that spsA, sppA, frkA and amsA are grouped in a transcriptional unit that were named Suc cluster, whose expression is increased in response to a salt treatment. This is the first report on the characterization of an AMS and FRK in an oxygenic photosynthetic microorganism, which could be associated with Suc metabolism.
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PMID:Functional characterization of Synechococcus amylosucrase and fructokinase encoding genes discovers two novel actors on the stage of cyanobacterial sucrose metabolism. 2490 10