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Phosphoglucoisomerase

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Phosphoglucoisomerase

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Phosphoglucoisomerase (alternatively known as phosphoglucose isomerase or Glucose-6-phosphate isomerase) are a group of enzymes of the isomerase family (EC 5.3.1.9), so named for their main function in glycolysis and gluconeogenesis. In both these pathways phosphoglucose isomerase (PGI) is used to inter-convert glucose-6-phosphate and fructose 6-phosphate, reaction driven by the relative concentrations of these sugars in the cytoplasmic matrix of the cell.

Phosphoglucoisomerase is also know for a list of activities outside the cells:

  • Neuroleukin (NLK)- nerve growth factor secreted by T cells, also used to stimulate the production of immunoglobulin.
  • Autocrine motility factor (AMF)- product of tumor cells, it promotes cell migration and viewed as a possible cause in cancer metastasis.
  • Maturation factor(MF)
  • Myofibril-bound serine protese inhibitor (MBSPI)

Contents

Structure

Template:STRUCTURE 1hox


Mechanism

Image:Mech.png

Links

-Crystal Structure of rabbit phosphoglucose isomerase complexed fructose 6-phosphate (PDB=1hox[1])

-Crystal Structure of human phosphoglucose isomerase (PDB=1iat[2])

-Other available structures 1dqr, 1g98, 1gzd, 1gzv, 1hm5, 1iri, 1jiq, 1jlh, 1koj, 1n8t, 1nuh, 1xtb.

References

  1. ↑ Lee JH, Chang KZ, Patel V, Jeffery CJ. Crystal structure of rabbit phosphoglucose isomerase complexed with its substrate D-fructose 6-phosphate. Biochemistry. 2001 Jul 3;40(26):7799-805. PMID:11425306
  2. ↑ Read J, Pearce J, Li X, Muirhead H, Chirgwin J, Davies C. The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia. J Mol Biol. 2001 Jun 1;309(2):447-63. PMID:11371164 doi:10.1006/jmbi.2001.4680
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