Phosphoglucoisomerase: Difference between revisions
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<applet load="1iat" size="300" color="white" frame="true" align="right" caption="Phosphoglucoisomerase" /> | |||
'''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in converting glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis. | '''Phosphoglucoisomerase''' (alternatively known as '''phosphoglucose isomerase''' or '''Glucose-6-phosphate isomerase''') are a group of enzymes of the isomerase family ([http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.9 EC 5.3.1.9]), so named for their main function in converting glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis. | ||
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=='''Structure'''== | =='''Structure'''== | ||
{{STRUCTURE_1hox | PDB=1hox| SCENE= }} | |||
=='''Mechanism'''== | =='''Mechanism'''== | ||
Revision as of 22:37, 26 February 2010
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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 converting glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis.
Structure
Mechanism
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
- ↑ 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
- ↑ 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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