ArticleBiochemistry2010
Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 19 citations in OpenAlex.
- The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase.Archives of biochemistry and biophysics · 2014Article
- Article
- Insights into the carboxyltransferase reaction of pyruvate carboxylase from the structures of bound product and intermediate analogs.Biochemical and biophysical research communications · 2013Article
- A substrate-induced biotin binding pocket in the carboxyltransferase domain of pyruvate carboxylase.The Journal of biological chemistry · 2013Article
- Structure and function of biotin-dependent carboxylases.Cellular and molecular life sciences : CMLS · 2013Review
- Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA.Archives of biochemistry and biophysics · 2012Review
- Novel insights into the biotin carboxylase domain reactions of pyruvate carboxylase from Rhizobium etli.Biochemistry · 2011Article
- Anaplerotic function of phosphoenolpyruvate carboxylase in Bradyrhizobium japonicum USDA110.Current microbiology · 2011Article
- Probing the allosteric activation of pyruvate carboxylase using 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate as a fluorescent mimic of the allosteric activator acetyl CoA.Archives of biochemistry and biophysics · 2011Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
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Abstract
The roles of Arg548 and Gln552 residues in the active site of the carboxyl transferase domain of Rhizobium etli pyruvate carboxylase were investigated using site-directed mutagenesis. Mutation of Arg548 to alanine or glutamine resulted in the destabilization of the quaternary structure of the enzyme, suggesting that this residue has a structural role. Mutations R548K, Q552N, and Q552A resulted in a loss of the ability to catalyze pyruvate carboxylation, biotin-dependent decarboxylation of oxaloacetate, and the exchange of protons between pyruvate and water. These mutants retained the ability to catalyze reactions that occur at the active site of the biotin carboxylase domain, i.e., bicarbonate-dependent ATP cleavage and ADP phosphorylation by carbamoyl phosphate. The effects of oxamate on the catalysis in the biotin carboxylase domain by the R548K and Q552N mutants were similar to those on the catalysis of reactions by the wild-type enzyme. However, the presence of oxamate had no effect on the reactions catalyzed by the Q552A mutant. We propose that Arg548 and Gln552 facilitate the binding of pyruvate and the subsequent transfer of protons between pyruvate and biotin in the partial reaction catalyzed in the active site of the carboxyl transferase domain of Rhizobium etli pyruvate carboxylase.
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