"Phosphofructokinase-1" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
An allosteric enzyme that regulates glycolysis by catalyzing the transfer of a phosphate group from ATP to fructose-6-phosphate to yield fructose-1,6-bisphosphate. D-tagatose- 6-phosphate and sedoheptulose-7-phosphate also are acceptors. UTP, CTP, and ITP also are donors. In human phosphofructokinase-1, three types of subunits have been identified. They are PHOSPHOFRUCTOKINASE-1, MUSCLE TYPE; PHOSPHOFRUCTOKINASE-1, LIVER TYPE; and PHOSPHOFRUCTOKINASE-1, TYPE C; found in platelets, brain, and other tissues.
| Descriptor ID |
D010732
|
| MeSH Number(s) |
D08.811.913.696.620.225.850.500
|
| Concept/Terms |
Phosphofructokinase-1- Phosphofructokinase-1
- Phosphofructokinase 1
- 6-Phosphofructokinase
- 6 Phosphofructokinase
- Fructose-6-phosphate 1-Phosphotransferase
- 6-Phosphofructo-1-kinase
- Fructose-6-P 1-Kinase
|
Below are MeSH descriptors whose meaning is more general than "Phosphofructokinase-1".
Below are MeSH descriptors whose meaning is more specific than "Phosphofructokinase-1".
This graph shows the total number of publications written about "Phosphofructokinase-1" by people in this website by year, and whether "Phosphofructokinase-1" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 2 | 0 | 2 |
| 1996 | 1 | 0 | 1 |
| 1999 | 1 | 0 | 1 |
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Below are the most recent publications written about "Phosphofructokinase-1" by people in Profiles.
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Kinetic characterization of a T-state of Ascaris suum phosphofructokinase with heterotropic negative cooperativity by ATP eliminated. Arch Biochem Biophys. 1999 May 15; 365(2):335-43.
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Isotope partitioning with Ascaris suum phosphofructokinase is consistent with an ordered kinetic mechanism. Biochemistry. 1996 Apr 30; 35(17):5451-7.
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A pH-dependent allosteric transition in Ascaris suum phosphofructokinase distinct from that observed with fructose 2,6-bisphosphate. Arch Biochem Biophys. 1995 Oct 01; 322(2):410-6.
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Acid-base catalytic mechanism and pH dependence of fructose 2,6-bisphosphate activation of the Ascaris suum phosphofructokinase. Biochemistry. 1995 Jun 20; 34(24):7781-7.
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Lanthanide pyrophosphates as substrates for the pyrophosphate-dependent phosphofructokinases from Propionibacterium freudenreichii and Phaseolus aureus: evidence for a second metal ion required for reaction. Biochemistry. 1994 Feb 22; 33(7):1663-7.
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Modification of the ATP inhibitory site of the Ascaris suum phosphofructokinase results in the stabilization of an inactive T state. Biochemistry. 1991 Oct 15; 30(41):9998-10004.
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Fructose 2,6-bisphosphate and AMP increase the affinity of the Ascaris suum phosphofructokinase for fructose 6-phosphate in a process separate from the relief of ATP inhibition. J Biol Chem. 1991 May 15; 266(14):8891-6.
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Effector-induced conformational transitions in Ascaris suum phosphofructokinase. A fluorescence and circular dichroism study. J Biol Chem. 1991 May 15; 266(14):8884-90.
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pH dependence of the kinetic parameters for the pyrophosphate-dependent phosphofructokinase reaction supports a proton-shuttle mechanism. Biochemistry. 1989 May 16; 28(10):4155-60.
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Isotope exchange as a probe of the kinetic mechanism of pyrophosphate-dependent phosphofructokinase. Biochemistry. 1988 May 03; 27(9):3320-5.