Abstract
Overexpression of the liver subunit of 6-phosphofructo-1-kinase in Chinese hamster ovary K1 cells was shown to increase the steady-state level of the enzyme's product, fructose 1, 6-bisphosphate, and to produce a small but significant decrease in the concentration of fructose 2,6-bisphosphate, which is an allosteric activator of the enzyme. However, overexpression of the enzyme had no effect on glycolytic flux under a variety of different substrate conditions. This latter observation is consistent with similar studies in fungi and in potato tubers which indicate that 6-phosphofructo-1-kinase has very little control over flux in glycolysis.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Allosteric Regulation
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Animals
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CHO Cells
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Cell Division
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Cricetinae
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Fructosediphosphates / metabolism
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Gene Expression
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Glucose / metabolism
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Glucose-6-Phosphate / metabolism
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Glycolysis*
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Kinetics
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Liver / enzymology*
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Phosphofructokinase-1 / chemistry*
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Phosphofructokinase-1 / genetics
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Phosphofructokinase-1 / metabolism*
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Protein Subunits
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
Substances
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Fructosediphosphates
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Protein Subunits
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Recombinant Proteins
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Glucose-6-Phosphate
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fructose 2,6-diphosphate
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Phosphofructokinase-1
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Glucose
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fructose-1,6-diphosphate