Glucose-6-Phosphate Isomerase
"Glucose-6-Phosphate Isomerase" 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 aldose-ketose isomerase that catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate. In prokaryotic and eukaryotic organisms it plays an essential role in glycolytic and gluconeogenic pathways. In mammalian systems the enzyme is found in the cytoplasm and as a secreted protein. This secreted form of glucose-6-phosphate isomerase has been referred to as autocrine motility factor or neuroleukin, and acts as a cytokine which binds to the AUTOCRINE MOTILITY FACTOR RECEPTOR. Deficiency of the enzyme in humans is an autosomal recessive trait, which results in CONGENITAL NONSPHEROCYTIC HEMOLYTIC ANEMIA.
| Descriptor ID |
D005956
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| MeSH Number(s) |
D08.811.399.475.200.350
|
| Concept/Terms |
Glucose-6-Phosphate Isomerase- Glucose-6-Phosphate Isomerase
- Glucose 6 Phosphate Isomerase
- Isomerase, Glucose-6-Phosphate
- Isomerase, Glucose 6 Phosphate
- Phosphohexose Isomerase
- Isomerase, Phosphohexose
- Glucosephosphate Isomerase
- Isomerase, Glucosephosphate
- Phosphoglucose Isomerase
- Isomerase, Phosphoglucose
Autocrine Motility Factor- Autocrine Motility Factor
- Motility Factor, Autocrine
- Tumor Autocrine Motility Factor
- Tumor-Cell Autocrine Motility Factor
- Tumor Cell Autocrine Motility Factor
- Neuroleukin
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This graph shows the total number of publications written about "Glucose-6-Phosphate Isomerase" by people in this website by year, and whether "Glucose-6-Phosphate Isomerase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 1998 | 0 | 1 | 1 |
| 2001 | 1 | 0 | 1 |
| 2003 | 4 | 0 | 4 |
| 2004 | 3 | 0 | 3 |
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Below are the most recent publications written about "Glucose-6-Phosphate Isomerase" by people in Profiles.
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Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes. Biochemistry. 2004 Nov 09; 43(44):14088-95.
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The crystal structure of mouse phosphoglucose isomerase at 1.6A resolution and its complex with glucose 6-phosphate reveals the catalytic mechanism of sugar ring opening. J Mol Biol. 2004 Sep 17; 342(3):847-60.
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A novel phosphoglucose isomerase (PGI)/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16-A resolution. J Biol Chem. 2004 Sep 17; 279(38):39838-45.
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Crystallization and preliminary X-ray diffraction analysis of phosphoglucose isomerase from Pyrococcus furiosus. Protein Pept Lett. 2003 Oct; 10(5):517-20.
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Structural evidence for a hydride transfer mechanism of catalysis in phosphoglucose isomerase from Pyrococcus furiosus. J Biol Chem. 2003 Nov 21; 278(47):47261-8.
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The structure of human phosphoglucose isomerase complexed with a transition-state analogue. Acta Crystallogr D Biol Crystallogr. 2003 Jun; 59(Pt 6):1111-3.
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Structure of native phosphoglucose isomerase from rabbit: conformational changes associated with catalytic function. Acta Crystallogr D Biol Crystallogr. 2003 Mar; 59(Pt 3):453-65.
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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 01; 309(2):447-63.
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Molecular basis of neurological dysfunction coupled with haemolytic anaemia in human glucose-6-phosphate isomerase (GPI) deficiency. Hum Genet. 1998 Oct; 103(4):450-4.