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6-phosphofructokinase

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6-phos·pho·fruc·to·ki·nase

(fos'fō-frŭk'tō-kī'nās),
Phosphofructokinase I; an enzyme that catalyzes the phosphorylation of d-fructose 6-phosphate by ATP (or other NTP) to fructose 1,6-bisphosphate and ADP (or other NDP); this enzyme catalyzes a step in glycolysis; it is inhibited by elevated levels of either ATP or citrate; a deficiency of this enzyme can lead to hemolytic anemia.
Synonym(s): phosphohexokinase
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References in periodicals archive
According to the results, four unigenes designated as 6G-fructosyltransferase (Figure 7(a)), d-2-hydroxyglutarate dehydrogenase (Figure 7(b)), gluconokinase (Figure 7(c)), and 6-phosphofructokinase (Figure 7(d)), could match Swiss-Model sequences with identity > 30%, coverage > 75%, and appropriate description (Supplementary Table 2).
Caption: Figure 7: Protein structure model of 6G-fructosyltransferase (a), d-2-hydroxyglutarate dehydrogenase (b), gluconokinase (c), and 6-phosphofructokinase (d) in three Agave species by using Swiss-Model [33].
Yet, in a study of trained cyclists exercising at 2300 m, there was a reduction in the activity of 6-phosphofructokinase (PFK), a glycolytic rate-limiting enzyme (4).
The majority of these expressed proteins were involved in glycolysis (enolase, fructose-bisphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, L-lactate dehydrogenase, 6-phosphofructokinase, glucose-6-phosphate isomerase, phosphoglycerate kinase, phosphopyruvate hydratase, pyruvate kinase, triosephosphate isomerase, and 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase) and the remaining proteins were involved in fer-mentation (alcohol-acetaldehyde dehydrogenase, formate ace-tyltransferase, and pyruvate-formate lyase), the pentose phosphate pathway (6-phosphogluconate dehydrogenase [decarboxylating]), pyruvate decarboxylation (pyruvate dehydrogenase complex E2 component), and the urea cycle (ornithine carbamoyltransferase).
Due to the absence of 6-phosphofructokinase for Embden-Meyerhof-Parnas (EMP) route, glucose metabolism in P.
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