Propionate kinase
| Propionate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.2.15 | ||||||||
| CAS no. | 39369-28-3 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Propionate kinase (EC 2.7.2.15, PduW, TdcD, propionate/acetate kinase) is an enzyme with systematic name ATP:propanoate phosphotransferase. It catalyses the following reversible chemical reaction
The enzyme characterised from Escherichia coli requires magnesium ion (Mg2+) and converts propionic acid to propanoyl phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The reaction is part of a sequence which degrades the amino acid L-threonine to propionic acid.[1] The enzyme is also found in Salmonella enterica, which allows that bacterium to grow on propylene glycol.[2][3] It can also act on acetic acid.[4]
Structural studies
X-ray crystallography has been used to determine the structure of the enzyme from Salmonella typhimurium.[5][6]
References
- ↑ Hesslinger C, Fairhurst SA, Sawers G (January 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". Molecular Microbiology. 27 (2): 477–92. doi:10.1046/j.1365-2958.1998.00696.x. PMID 9484901.
- ↑ Palacios S, Starai VJ, Escalante-Semerena JC (May 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". Journal of Bacteriology. 185 (9): 2802–10. doi:10.1128/jb.185.9.2802-2810.2003. PMC 154405. PMID 12700259.
- ↑ Wei Y, Miller CG (October 1999). "Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium". Journal of Bacteriology. 181 (19): 6092–7. doi:10.1128/JB.181.19.6092-6097.1999. PMC 103637. PMID 10498722.
- ↑ Ingram-Smith C, Gorrell A, Lawrence SH, Iyer P, Smith K, Ferry JG (April 2005). "Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase". Journal of Bacteriology. 187 (7): 2386–94. doi:10.1128/jb.187.7.2386-2394.2005. PMC 1065240. PMID 15774882.
- ↑ Simanshu DK, Murthy MR (January 2005). "Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium". Acta Crystallographica Section F. 61 (Pt 1): 52–5. doi:10.1107/s1744309104026429. PMC 1952409. PMID 16508089.
- ↑ Simanshu DK, Savithri HS, Murthy MR (September 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". Journal of Molecular Biology. 352 (4): 876–92. doi:10.1016/j.jmb.2005.07.069. PMID 16139298.
External links
- Propionate+kinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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