ArticleArchives of biochemistry and biophysics2014
The role of biotin and oxamate in the carboxyltransferase reaction of pyruvate carboxylase.
Article in Archives of biochemistry and biophysics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Hydrolysis of the acetyl-CoA allosteric activator by Staphylococcus aureus pyruvate carboxylase.Archives of biochemistry and biophysics · 2025Article
- Insights Into Phylogeny, Diversity and Functional Potential of Poseidoniales Viruses.Environmental microbiology · 2025Article
- Structural insight into synergistic activation of human 3-methylcrotonyl-CoA carboxylase.Nature structural & molecular biology · 2025Article
- Vertical stratification of P pools in subtropical plantation soils under fertilization and dry-season irrigation: multiomics regulatory strategies.Frontiers in microbiology · 2025Article
- Anemoside B4, a new pyruvate carboxylase inhibitor, alleviates colitis by reprogramming macrophage function.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024Article
- Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.Nature communications · 2018Article
- Comparative analysis of the Corynebacterium glutamicum transcriptome in response to changes in dissolved oxygen levels.Journal of industrial microbiology & biotechnology · 2017Article
- Transcriptome analysis of Corynebacterium glutamicum in the process of recombinant protein expression in bioreactors.PloS one · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Pyruvate carboxylase (PC) is a biotin-dependent enzyme that catalyzes the MgATP-dependent carboxylation of pyruvate to oxaloacetate, an important anaplerotic reaction in central metabolism. During catalysis, carboxybiotin is translocated to the carboxyltransferase domain where the carboxyl group is transferred to the acceptor substrate, pyruvate. Many studies on the carboxyltransferase domain of PC have demonstrated an enhanced oxaloacetate decarboxylation activity in the presence of oxamate and it has been shown that oxamate accepts a carboxyl group from carboxybiotin during oxaloacetate decarboxylation. The X-ray crystal structure of the carboxyltransferase domain from Rhizobium etli PC reveals that oxamate is positioned in the active site in an identical manner to the substrate, pyruvate, and kinetic data are consistent with the oxamate-stimulated decarboxylation of oxaloacetate proceeding through a simple ping-pong bi bi mechanism in the absence of the biotin carboxylase domain. Additionally, analysis of truncated PC enzymes indicates that the BCCP domain devoid of biotin does not contribute directly to the enzymatic reaction and conclusively demonstrates a biotin-independent oxaloacetate decarboxylation activity in PC. These findings advance the description of catalysis in PC and can be extended to the study of related biotin-dependent enzymes.
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