Biology:Glycerate 2-kinase
From HandWiki
| Glycerate 2-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.7.1.165 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Glycerate 2-kinase (EC 2.7.1.165, D-glycerate-2-kinase, glycerate kinase (2-phosphoglycerate forming), ATP:(R)-glycerate 2-phosphotransferase) is an enzyme with systematic name ATP:D-glycerate 2-phosphotransferase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- ATP + D-glycerate [math]\displaystyle{ \rightleftharpoons }[/math] ADP + 2-phospho-D-glycerate
A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea.
References
- ↑ "A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties". Biotechnology Letters 31 (12): 1937–41. December 2009. doi:10.1007/s10529-009-0089-z. PMID 19690808.
- ↑ "Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus". FEMS Microbiology Letters 259 (1): 113–9. June 2006. doi:10.1111/j.1574-6968.2006.00264.x. PMID 16684110.
- ↑ "A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization". Extremophiles 11 (5): 733–9. September 2007. doi:10.1007/s00792-007-0079-9. PMID 17563835.
- ↑ Noh, M.; Jung, J.H.; Lee, S.B. (2006). "Purification and characterization of glycerate kinase from the thermoacidophilic archaeon Thermoplasma acidophilum: an enzyme belonging to the second glycerate kinase family". Biotechnol. Bioprocess Eng. 11 (4): 344–350. doi:10.1007/bf03026251.
- ↑ "Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2". European Journal of Biochemistry 210 (3): 849–54. December 1992. doi:10.1111/j.1432-1033.1992.tb17488.x. PMID 1336459.
- ↑ "Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli". Biochemistry 37 (41): 14369–75. October 1998. doi:10.1021/bi981124f. PMID 9772162.
External links
- Glycerate+2-kinase at the US National Library of Medicine Medical Subject Headings (MeSH)
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