Disease relevance of pck

• Single crystals of phosphoenolpyruvate carboxykinase from Escherichia coli K12 have been grown in the orthorhombic crystal system [1].
• PCK possesses a novel nucleotide-binding fold, particularly in the adenine-binding region, where the formation of a cis backbone torsion angle in a loop glycine residue promotes intimate contacts between the adenine-binding loop and adenine, while stabilizing a syn conformation of the base [2].
• Effect of overexpression of Actinobacillus succinogenes phosphoenolpyruvate carboxykinase on succinate production in Escherichia coli [3].

High impact information on pck

• A cyclic pathway between phosphoenolpyruvate and oxaloacetate was created in Escherichia coli by simultaneous overexpression of phosphoenolpyruvate carboxykinase (encoded by pck) and phosphoenopyruvate carboxylase (encoded by ppc) from a multicopy plasmid under the control of the tac promoter [4].
• Therefore, two complexes of PCK, one with AlF(3), Mg(2+) and ADP (complex I), the other with AlF(3), Mg(2+), ADP and pyruvate (complex II) were crystallized [5].
• The phosphoryl-transfer mechanism of Escherichia coli phosphoenolpyruvate carboxykinase from the use of AlF(3) [5].
• Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold [6].
• Partial trypsin digestion abolishes Ca(2+) activation (desensitizes PCK) [7].

Chemical compound and disease context of pck

• We found that the growth rates of E. coli in minimal medium supplemented with succinate and with pyruvate are limited by the levels of Pck and Pps, respectively [8].
• A mutant phosphoenolpyruvate carboxykinase in Escherichia coli conferring oxaloacetate decarboxylase activity [9].
• In E. coli K-12, PEPCK overexpression had no effect on succinate fermentation [3].
• The 1.8-A resolution structure of the ATP-Mg(2+)-Ca(2+)-pyruvate quinary complex of Escherichia coli phosphoenolpyruvate carboxykinase (PCK) is isomorphous to the published complex ATP-Mg(2+)-Mn(2+)-pyruvate-PCK, except for the Ca(2+) and Mn(2+) binding sites [7].

Biological context of pck

• The potential calcium binding site of the E. coli enzyme is conserved in the partial predicted sequence of the S. typhimurium phosphoenolpyruvate carboxykinase, consistent with the observation that calcium activation of the S. typhimurium phosphoenolpyruvate carboxykinase is very similar to that observed for the E. coli enzyme [10].
• The anaplerotic pathway catalyzed by malic enzyme was identified in the mutant, which was accompanied with an up-regulation of phosphoenolpyruvate carboxylase and down-regulation of phosphoenolpyruvate carboxykinase [11].
• On the other hand, overexpression of phosphoenolpyruvate carboxykinase increased glucose consumption and decreased oxygen consumption relative to those levels required for growth [12].
• Comparison of the predicted amino acid sequence of A. suum PEPCK with other PEPCKs showed that this enzyme is most closely related to the H. contortus enzyme [13].

Associations of pck with chemical compounds

• Mutation Arg336 to Lys in Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase originates an enzyme with increased oxaloacetate decarboxylase activity [14].
• Mutants doubly deficient in phosphoenolpyruvate carboxykinase (pck) and phosphoenolpyruvate synthetase (pps) were unable to grow with succinate as the sole carbon source [15].
• We attempted to modulate the metabolic flow between phosphoenolpyruvate and oxaloacetate by overexpressing phosphoenolpyruvate carboxylase and phosphoenolpyruvate carboxykinase from a multicopy plasmid under the control of the tac promoter [12].
• Separate roles of Mg(2+), which binds the nucleotide, and Ca(2+), which bridges the nucleotide and the anionic substrate, are implied, and the catalytic mechanism of PCK is better explained by studies of the Ca(2+)-bound structure [7].

Other interactions of pck

• Further increases in either Pck or Pps above the optimal levels become growth inhibitory, and the growth yield for oxygen is reduced, indicating less efficient growth [8].
• The transcription start point for argH mRNA was determined by primer extension analysis and found to be within the coding sequence of the upstream gene, identified as the phosphoenolpyruvate carboxykinase gene (ppc) [16].

Analytical, diagnostic and therapeutic context of pck

• Crystallization of the calcium-activated phosphoenolpyruvate carboxykinase from Escherichia coli K12 [1].

References