Glycerate 2-kinase
| Glycerate 2-kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.165 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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] It catalyses the following chemical reaction
The enzyme first characterised from Hyphomicrobium methylovorum converts D-glyceric acid to 2-phospho-D-glyceric acid by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[2] It has been found in many other organisms, including Escherichia coli,[3] Thermoplasma acidophilum,[4] Pyrococcus horikoshii,[5], Picrophilus torridus,[6] and Sulfolobus tokodaii.[7]
Glycerate 2-kinase is a key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea.[6][7]
References
- ↑ Enzyme 2.7.1.165 at KEGG Pathway Database.
- ↑ Yoshida T, Fukuta K, Mitsunaga T, Yamada H, Izumi Y (December 1992). "Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2". European Journal of Biochemistry. 210 (3): 849–54. doi:10.1111/j.1432-1033.1992.tb17488.x. PMID 1336459.
- ↑ Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA (October 1998). "Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli". Biochemistry. 37 (41): 14369–75. doi:10.1021/bi981124f. PMID 9772162.
- ↑ 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.
- ↑ Liu B, Hong Y, Wu L, Li Z, Ni J, Sheng D, Shen Y (September 2007). "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. doi:10.1007/s00792-007-0079-9. PMID 17563835.
- 1 2 Reher M, Bott M, Schönheit P (June 2006). "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. doi:10.1111/j.1574-6968.2006.00264.x. PMID 16684110.
- 1 2 Liu B, Wu L, Liu T, Hong Y, Shen Y, Ni J (December 2009). "A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties". Biotechnology Letters. 31 (12): 1937–41. doi:10.1007/s10529-009-0089-z. PMID 19690808.
External links
- Glycerate+2-kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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