Propionate kinase
Propionate kinase (EC 2.7.2.15, PduW, TdcD, propionate/acetate kinase) is an enzyme with systematic name ATP:propanoate phosphotransferase.[1][2][3][4][5][6] This enzyme catalyses the following chemical reaction
- ATP + propanoate
ADP + propanoyl phosphate
This enzyme requires Mg2+.
References
- ↑ Heßlinger, C., Fairhurst, S.A. and Sawers, G. (1998). "Novel keto acid formate-lyase and propionate kinase enzymes are components of an anaerobic pathway in Escherichia coli that degrades L-threonine to propionate". Mol. Microbiol. 27: 477–492. doi:10.1046/j.1365-2958.1998.00696.x. PMID 9484901.
- ↑ Palacios, S., Starai, V.J. and Escalante-Semerena, J.C. (2003). "Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol". J. Bacteriol. 185: 2802–2810. doi:10.1128/jb.185.9.2802-2810.2003. PMID 12700259.
- ↑ Wei, Y. and Miller, C.G. (1999). "Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium". J. Bacteriol. 181: 6092–6097. PMID 10498722.
- ↑ Ingram-Smith, C., Gorrell, A., Lawrence, S.H., Iyer, P., Smith, K. and Ferry, J.G. (2005). "Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase". J. Bacteriol. 187: 2386–2394. doi:10.1128/jb.187.7.2386-2394.2005. PMID 15774882.
- ↑ Simanshu, D.K. (2005). "Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium". Acta Crystallogr. F Struct. Biol. Cryst. Commun. 61: 52–55. doi:10.1107/s1744309104026429. PMID 16508089.
- ↑ Simanshu, D.K., Savithri, H.S. and Murthy, M.R. (2005). "Crystal structures of ADP and AMPPNP-bound propionate kinase (TdcD) from Salmonella typhimurium: comparison with members of acetate and sugar kinase/heat shock cognate 70/actin superfamily". J. Mol. Biol. 352: 876–892. doi:10.1016/j.jmb.2005.07.069. PMID 16139298.
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