Glycerate kinase
| Glycerate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.31 | ||||||||
| CAS no. | 9026-61-3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Glycerate kinase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | Glyc_kinase | ||||||
| Pfam | PF02595 | ||||||
| InterPro | IPR004381 | ||||||
| |||||||
Glycerate kinase (EC 2.7.1.31) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from liver and Escherichia coli converts D-glyceric acid to 3-phospho-D-glyceric acid by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2]
This enzyme is a transferases, specifically one transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:(R)-glycerate 3-phosphotransferase. Other names in common use include glycerate kinase (phosphorylating), D-glycerate 3-kinase, D-glycerate kinase, glycerate-3-kinase, GK, D-glyceric acid kinase, and ATP:D-glycerate 2-phosphotransferase. This enzyme participates in 3 metabolic pathways: serine/glycine/threonine metabolism, glycerolipid metabolism, and glyoxylate-dicarboxylate metabolism.[3]
Some related enzymes produce the isomeric 2-phospho-D-glyceric acid.[4]
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1TO6, PDB: 1X3L, and PDB: 2B8N.
References
- ↑ Ichihara A, Greenberg DM (April 1957). "Studies on the purification and properties of D-glyceric acid kinase of liver". The Journal of Biological Chemistry. 225 (2): 949–958. doi:10.1016/S0021-9258(18)64892-6. PMID 13416296.
- ↑ Doughty CC, Hayashi JA, Guenther HL (February 1966). "Purification and properties of D-glycerate 3-kinase from Escherichia coli". The Journal of Biological Chemistry. 241 (3): 568–572. doi:10.1016/S0021-9258(18)96874-2. PMID 5325263.
- ↑ Enzyme 2.7.1.31 at KEGG Pathway Database.
- ↑ Bartsch O, Hagemann M, Bauwe H (September 2008). "Only plant-type (GLYK) glycerate kinases produce d-glycerate 3-phosphate". FEBS Letters. 582 (20): 3025–3028. Bibcode:2008FEBSL.582.3025B. doi:10.1016/j.febslet.2008.07.038. PMID 18675808. S2CID 28262946.
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