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Fructose 1,6-bisphosphate


Fructose 1,6-bisphosphate, known in older publications as Harden-Young ester, is fructose sugar phosphorylated on carbons 1 and 6 (i.e., is a fructosephosphate). The β-D-form of this compound is common in cells. Upon entering the cell, most glucose and fructose is converted to fructose 1,6-bisphosphate.

In glycolysis

Fructose 1,6-bisphosphate lies within the glycolysis metabolic pathway and is produced by phosphorylation of fructose 6-phosphate. It is, in turn, broken down into two compounds: glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. It is an allosteric activator of pyruvate kinase through distinct interactions of binding and allostery at the enzyme's catalytic site

Isomerism

Main article: Fructose

Fructose 1,6-bisphosphate has only one biologically active isomer, the β-D-form. There are many other isomers, analogous to those of fructose.

Iron chelation

Fructose 1,6-bis(phosphate) has also been implicated in the ability to bind and sequester Fe(II), a soluble form of iron whose oxidation to the insoluble Fe(III) is capable of generating reactive oxygen species via Fenton chemistry. The ability of fructose 1,6-bis(phosphate) to bind Fe(II) may prevent such electron transfers, and thus act as an antioxidant within the body. Certain neurodegenerative diseases, like Alzheimer's and Parkinson's, have been linked to metal deposits with high iron content, although it is uncertain whether Fenton chemistry plays a substantial role in these diseases, or whether fructose 1,6-bis(phosphate) is capable of mitigating those effects.

Notes

References

References

  1. (18 December 2014). "Glycolysis, tumor metabolism, cancer growth and dissemination. A new pH-based etiopathogenic perspective and therapeutic approach to an old cancer question". Oncoscience.
  2. Berg, Jeremy M.. (2002). "Biochemistry". [[W.H. Freeman and Company]].
  3. Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. {{ISBN. 1-57259-153-6.
  4. (2015). "Distinguishing the Interactions in the Fructose 1,6-Bisphosphate Binding Site of Human Liver Pyruvate Kinase That Contribute to Allostery". Biochemistry.
  5. Bajic, Aleksandar. (2011). "Relevance of the ability of fructose 1,6-bis(phosphate) to sequester ferrous but not ferric ions". Carbohydrate Research.
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