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Gene Review

prpB  -  2-methylisocitrate lyase

Escherichia coli UTI89

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Disease relevance of prpB

  • The expression and regulatory properties of a propionate-regulated overexpression system (Salmonella enterica prpBCDE promoter (P(prpB)) and positive regulator (prpR)) were evaluated in wild-type S. enterica serovar Typhimurium TR6583 and prpB(-) or prpD(-) versions of this strain and compared with the arabinose-regulated T7 expression system [1].
  • In addition, both PrpA and PrpB modulate the phosphorylated status of some other phosphoproteins in E. coli [2].
  • Based on the structure of ligand-bound isocitrate lyase from Mycobacterium tuberculosis a model of the substrate-bound PrpB enzyme in its closed conformation was created which provides hints towards the substrate specificity of this enzyme [3].
  • PrpB exhibits 34% sequence identity with carboxyphosphoenolpyruvate phosphonomutase from Streptomyces hygroscopicus, in which the essential cysteine residue is conserved [4].

High impact information on prpB

  • A possible impact of this observation with respect to the different responses of isocitrate lyases and PrpB upon treatment with the common inhibitor 3-bromopyruvate is discussed [3].
  • Since in the presented structure, PrpB contains, apart from a Mg(2+), no ligand, the active site loop is found in an open conformation [3].
  • The levels of PrpC and PrpB activity were much lower in propionate-negative mutant IPT189 obtained from IPT101(T) and were heterologously expressed in Escherichia coli [5].
  • The apparent K(a) of PrpA for Mn(2+) of 65 microM was comparable to that for other bacterial phosphatases, but PrpB had a much higher affinity for Mn(2+) (1.3 microM) [6].
  • Here we report the X-ray crystal structure of the native and the pyruvate/Mg(2+) bound PrpB from S. typhimurium, determined at 2.1 and 2.3A, respectively [7].

Chemical compound and disease context of prpB


Biological context of prpB


  1. A Salmonella-based, propionate-inducible, expression system for Salmonella enterica. Lee, S.K., Keasling, J.D. Gene (2006) [Pubmed]
  2. Signal transduction pathways in response to protein misfolding in the extracytoplasmic compartments of E. coli: role of two new phosphoprotein phosphatases PrpA and PrpB. Missiakas, D., Raina, S. EMBO J. (1997) [Pubmed]
  3. Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre. Grimm, C., Evers, A., Brock, M., Maerker, C., Klebe, G., Buckel, W., Reuter, K. J. Mol. Biol. (2003) [Pubmed]
  4. 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes. Brock, M., Darley, D., Textor, S., Buckel, W. Eur. J. Biochem. (2001) [Pubmed]
  5. Identification of the 2-methylcitrate pathway involved in the catabolism of propionate in the polyhydroxyalkanoate-producing strain Burkholderia sacchari IPT101(T) and analysis of a mutant accumulating a copolyester with higher 3-hydroxyvalerate content. Brämer, C.O., Silva, L.F., Gomez, J.G., Priefert, H., Steinbüchel, A. Appl. Environ. Microbiol. (2002) [Pubmed]
  6. The PPP-family protein phosphatases PrpA and PrpB of Salmonella enterica serovar Typhimurium possess distinct biochemical properties. Shi, L., Kehres, D.G., Maguire, M.E. J. Bacteriol. (2001) [Pubmed]
  7. Crystal structure of Salmonella typhimurium 2-methylisocitrate lyase (PrpB) and its complex with pyruvate and Mg(2+). Simanshu, D.K., Satheshkumar, P.S., Savithri, H.S., Murthy, M.R. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
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