Glycerate 2-kinase

From Wikipedia, the free encyclopedia
Jump to: navigation, search
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

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[edit]

  1. ^ Liu, B.; Wu, L.; Liu, T.; Hong, Y.; Shen, Y.; 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. 
  2. ^ Reher, M.; Bott, M.; 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. 
  3. ^ Liu, B.; Hong, Y.; Wu, L.; Li, Z.; Ni, J.; Sheng, D.; 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. 
  4. ^ 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: 344–350. doi:10.1007/bf03026251. 
  5. ^ Yoshida, T.; Fukuta, K.; Mitsunaga, T.; Yamada, H.; 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. 
  6. ^ Hubbard, B.K.; Koch, M.; Palmer, D.R.; Babbitt, P.C.; 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. 

External links[edit]