twitter

Escherichia coli K-12 substr. MG1655 Reaction: 2.7.2.15

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.7.2.15

Enzymes and Genes:
acetate kinase Inferred from experiment : ackA
propionate kinase Inferred from experiment : tdcD

In Pathway: L-threonine degradation I

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: propionate kinase

Enzyme Commission Synonyms: PduW, TdcD, propionate/acetate kinase

Summary:
This is the final reaction in the anaerobic L-threonine degradation pathway.

Requires Mg2+. Both propanoate and acetate can act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [Hesslinger98]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important roles in the production of propanoate.

Requires Mg2+. Both propanoate and acetate can act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [Hesslinger98]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important roles in the production of propanoate.

Enzyme Commission Summary:
Requires Mg2+. Both propanoate and acetate can act as a substrate. Involved in the anaerobic degradation of L-threonine in bacteria [Hesslinger98]. Both this enzyme and EC 2.7.2.1, acetate kinase, play important roles in the production of propanoate [Hesslinger98].

Citations: [Palacios03, Wei99, IngramSmith05, Simanshu05, Simanshu05a]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.7.2.15 , ENZYME:EC:2.7.2.15 , IUBMB-ExplorEnz:EC:2.7.2.15


References

Hesslinger98: Hesslinger C, Fairhurst SA, 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 1998;27(2);477-92. PMID: 9484901

IngramSmith05: Ingram-Smith C, Gorrell A, Lawrence SH, Iyer P, Smith K, Ferry JG (2005). "Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase." J Bacteriol 187(7);2386-94. PMID: 15774882

Palacios03: Palacios S, Starai VJ, Escalante-Semerena JC (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(9);2802-10. PMID: 12700259

Simanshu05: Simanshu DK, Murthy MR (2005). "Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of propionate kinase (TdcD) from Salmonella typhimurium." Acta Crystallogr Sect F Struct Biol Cryst Commun 61(Pt 1);52-5. PMID: 16508089

Simanshu05a: Simanshu DK, Savithri HS, Murthy MR (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(4);876-92. PMID: 16139298

Wei99: Wei Y, Miller CG (1999). "Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium." J Bacteriol 181(19);6092-7. PMID: 10498722


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Sat Aug 1, 2015, biocyc11.