ArticleBiochemistry2009
Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Conformational Selection Governs Carrier Domain Positioning inBiochemistry · 2022Article
- Pyruvate carboxylase and cancer progression.Cancer & metabolism · 2021Review
- Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.Nature communications · 2018Article
- The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase.Archives of biochemistry and biophysics · 2014Article
- Coordinating role of His216 in MgATP binding and cleavage in pyruvate carboxylase.Biochemistry · 2014Article
- 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
- Oxamate is an alternative substrate for pyruvate carboxylase from Rhizobium etli.Biochemistry · 2013Article
- Structure and function of biotin-dependent carboxylases.Cellular and molecular life sciences : CMLS · 2013Review
- Production of extracellular biopolymers and identification of intracellular proteins and Rhizobium tropici.Current microbiology · 2012Article
- Searching for resistance genes to Bursaphelenchus xylophilus using high throughput screening.BMC genomics · 2012Article
- The enzymes of biotin dependent CO₂ metabolism: what structures reveal about their reaction mechanisms.Protein science : a publication of the Protein Society · 2012Review
- Roles of Arg427 and Arg472 in the binding and allosteric effects of acetyl CoA in pyruvate carboxylase.Biochemistry · 2012Article
- Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction.The Journal of biological chemistry · 2012Article
- Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA.Archives of biochemistry and biophysics · 2012Review
- Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli.Biochemistry · 2011Article
- Novel insights into the biotin carboxylase domain reactions of pyruvate carboxylase from Rhizobium etli.Biochemistry · 2011Article
- Activation and inhibition of pyruvate carboxylase from Rhizobium etli.Biochemistry · 2011Article
- My favorite pyruvate carboxylase.IUBMB life · 2010Article
- Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis.Biochemistry · 2010Article
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Authors and funding
6 authors at 5 institutions in 3 countries.
Funding
Abstract
The effects of mutations in the active site of the carboxyl transferase domain of Rhizobium etli pyruvate carboxylase have been determined for the forward reaction to form oxaloacetate, the reverse reaction to form MgATP, the oxamate-induced decarboxylation of oxaloacetate, the phosphorylation of MgADP by carbamoyl phosphate, and the bicarbonate-dependent ATPase reaction. Additional studies with these mutants examined the effect of pyruvate and oxamate on the reactions of the biotin carboxylase domain. From these mutagenic studies, putative roles for catalytically relevant active site residues were assigned and a more accurate description of the mechanism of the carboxyl transferase domain is presented. The T882A mutant showed no catalytic activity for reactions involving the carboxyl transferase domain but surprisingly showed 7- and 3.5-fold increases in activity, as compared to that of the wild-type enzyme, for the ADP phosphorylation and bicarbonate-dependent ATPase reactions, respectively. Furthermore, the partial inhibition of the T882A-catalyzed BC domain reactions by oxamate and pyruvate further supports the critical role of Thr882 in the proton transfer between biotin and pyruvate in the carboxyl transferase domain. The catalytic mechanism appears to involve the decarboxylation of carboxybiotin and removal of a proton from Thr882 by the resulting biotin enolate with either a concerted or subsequent transfer of a proton from pyruvate to Thr882. The resulting enolpyruvate then reacts with CO(2) to form oxaloacetate and complete the reaction.
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