Glycerate 2-kinase
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
ADP + 2-phospho-D-glycerate
A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea.
References
- ↑ Liu, B., Wu, L., Liu, T., Hong, Y., Shen, Y. and Ni, J. (2009). "A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties". Biotechnol. Lett. 31: 1937–1941. doi:10.1007/s10529-009-0089-z. PMID 19690808.
- ↑ Reher, M., Bott, M. and Schonheit, P. (2006). "Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus". FEMS Microbiol. Lett. 259: 113–119. doi:10.1111/j.1574-6968.2006.00264.x. PMID 16684110.
- ↑ Liu, B., Hong, Y., Wu, L., Li, Z., Ni, J., Sheng, D. and Shen, Y. (2007). "A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization". Extremophiles 11: 733–739. doi:10.1007/s00792-007-0079-9. PMID 17563835.
- ↑ Noh, M., Jung, J.H. and 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: 344–350. doi:10.1007/bf03026251.
- ↑ Yoshida, T., Fukuta, K., Mitsunaga, T., Yamada, H. and Izumi, Y. (1992). "Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2". Eur. J. Biochem. 210 (3): 849–854. doi:10.1111/j.1432-1033.1992.tb17488.x. PMID 1336459.
- ↑ Hubbard, B.K., Koch, M., Palmer, D.R., Babbitt, P.C. and Gerlt, J.A. (1998). "Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli". Biochemistry 37: 14369–14375. doi:10.1021/bi981124f. PMID 9772162.
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