ReviewArchives of biochemistry and biophysics2012
Regulation of the structure and activity of pyruvate carboxylase by acetyl CoA.
Review in Archives of biochemistry and biophysics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed, 82 citations in OpenAlex.
- A pilot study of alternative substrates in the critically Ill subject using a ketogenic feed.Nature communications · 2023Trial
- Rethinking Human Energy Metabolism.Current issues in molecular biology · 2026Review
- Metabolic Symbiosis Between Cancer Cells and Endothelial Cells: A Key Driver of Tumor Angiogenesis.Advances in experimental medicine and biology · 2026Review
- Sepsis-induced changes in pyruvate metabolism: insights and potential therapeutic approaches.EMBO molecular medicine · 2024Review
- 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 Site at the Biotin Carboxylase Dimer Interface Mediates Activation and Inhibition inBiochemistry · 2023Article
- Role of soil nutrient elements transport on Camellia oleifera yield under different soil types.BMC plant biology · 2023Article
- Mechanism of metamifop resistance inFrontiers in plant science · 2023Article
- Long noncoding RNA ZFP36L2-AS functions as a metabolic modulator to regulate muscle development.Cell death & disease · 2022Article
- Integrating systemic and molecular levels to infer key drivers sustaining metabolic adaptations.PLoS computational biology · 2021Article
- PahT regulates carbon fluxes in Novosphingobium sp. HR1a and influences its survival in soil and rhizospheres.Environmental microbiology · 2021Article
- Article
- Efficient whole-cell catalysis for 5-aminovalerate production from L-lysine by using engineered Escherichia coli with ethanol pretreatment.Scientific reports · 2020Article
- Mitochondrial Metabolism in Astrocytes Regulates Brain Bioenergetics, Neurotransmission and Redox Balance.Frontiers in neuroscience · 2020Review
- Essentiality of fatty acid synthase in the 2D to anchorage-independent growth transition in transforming cells.Nature communications · 2019Article
- Metabolic Intermediates in Tumorigenesis and Progression.International journal of biological sciences · 2019Review
- Allosteric regulation alters carrier domain translocation in pyruvate carboxylase.Nature communications · 2018Article
- Hepatic transcriptional changes in critical genes for gluconeogenesis following castration of bulls.Asian-Australasian journal of animal sciences · 2018Article
- Roles of pyruvate carboxylase in human diseases: from diabetes to cancers and infection.Journal of molecular medicine (Berlin, Germany) · 2018Review
- Cold acclimation reduces hepatic protein Kinase B and AMP-activated protein kinase phosphorylation and increases gluconeogenesis in Rats.Physiological reports · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
In this review we examine the effects of the allosteric activator, acetyl CoA on both the structure and catalytic activities of pyruvate carboxylase. We describe how the binding of acetyl CoA produces gross changes to the quaternary and tertiary structures of the enzyme that are visible in the electron microscope. These changes serve to stabilize the tetrameric structure of the enzyme. The main locus of activation of the enzyme by acetyl CoA is the biotin carboxylation domain of the enzyme where ATP-cleavage and carboxylation of the biotin prosthetic group occur. As well as enhancing reaction rates, acetyl CoA also enhances the binding of some substrates, especially HCO3-, and there is also a complex interaction with the binding of the cofactor Mg2. The activation of pyruvate carboxylase by acetyl CoA is generally a cooperative processes, although there is a large degree of variability in the degree of cooperativity exhibited by the enzyme from different organisms. The X-ray crystallographic holoenzyme structures of pyruvate carboxylases from Rhizobium etli and Staphylococcus aureus have shown the allosteric acetyl CoA binding domain to be located at the interfaces of the biotin carboxylation and carboxyl transfer and the carboxyl transfer and biotin carboxyl carrier protein domains.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.