Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00157Glucose-6-phosphate isomerase (GPI) family signatures and profile
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00157
Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) or phosphoglucose isomerase (PGI) [1,2] is a dimeric enzyme that catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. PGI is involved in different pathways: in most higher organisms it is involved in glycolysis; in mammals it is involved in gluconeogenesis; in plants in carbohydrate biosynthesis; in some bacteria it provides a gateway for fructose into the Entner-Doudouroff pathway. Besides it's role as a glycolytic enzyme, mammalian PGI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. Mammalian PGI is also neuroleukin [3], a neurotrophic factor which supports the survival of various types of neurons.
The sequence of PGI is conserved among diverse species ranging from bacteria to mammals and structures form a similar fold (see <PDB:1IAT>) [4,5], comprised of two subdomains that each form an α-β-α sandwich, with the active site located in the cleft between the subdomains and on the dimer interface. A glutamate and a lysine residue as well as a histidine from the other protomer in the dimer are implicated in the catalytic mechanism. The structure resembles that of the SIS domain (see <PDOC51464>).
As signature patterns for this enzyme we selected two conserved regions, the first region is located in the central section of PGI, while the second one is located in its C-terminal section. We also developed a profile that covers the entire PGI.
Last update:September 2009 / Text revised; profile added.
-------------------------------------------------------------------------------
PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Achari A. Marshall S.E. Muirhead H. Palmieri R.H. Noltmann E.A. |
| Title | Glucose-6-phosphate isomerase. | |
| Source | Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:145-157(1981). | |
| PubMed ID | 6115414 |
| 2 | Authors | Smith M.W. Doolittle R.F. |
| Title | Anomalous phylogeny involving the enzyme glucose-6-phosphate isomerase. | |
| Source | J. Mol. Evol. 34:544-545(1992). | |
| PubMed ID | 1593646 |
| 3 | Authors | Faik P. Walker J.I.H. Redmill A.A.M. Morgan M.J. |
| Title | Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3' sequences. | |
| Source | Nature 332:455-457(1988). | |
| PubMed ID | 3352745 | |
| DOI | 10.1038/332455a0 |
| 4 | Authors | Read J. Pearce J. Li X. Muirhead H. Chirgwin J. Davies C. |
| Title | The crystal structure of human phosphoglucose isomerase at 1.6 A resolution: implications for catalytic mechanism, cytokine activity and haemolytic anaemia. | |
| Source | J. Mol. Biol. 309:447-463(2001). | |
| PubMed ID | 11371164 | |
| DOI | 10.1006/jmbi.2001.4680 |
| 5 | Authors | Yamamoto H. Miwa H. Kunishima N. |
| Title | Crystal structure of glucose-6-phosphate isomerase from Thermus thermophilus HB8 showing a snapshot of active dimeric state. | |
| Source | J. Mol. Biol. 382:747-762(2008). | |
| PubMed ID | 18675274 | |
| DOI | 10.1016/j.jmb.2008.07.041 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.