ArticleFEMS microbiology reviews2021
The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism.
Article in FEMS microbiology reviews, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 67 citations in OpenAlex.
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- Lipid metabolism mechanisms underlying seed oil content differences in Toxicodendron vernicifluum based on transcriptomics and lipidomics.BMC plant biology · 2026Article
- The activation of the metabolic oxaloacetate-pyruvate axis restores influenza A virus replication during impaired glycolysis.Virology journal · 2026Article
- Untargeted-targeted metabolomics: energy metabolism characteristics in heart failure staging and discovery of novel biomarkers.Journal of translational medicine · 2026Article
- Phenylalanine homeostasis in metabolic disorders: epidemiological trends, pathophysiological mechanisms, and clinical treatment.Frontiers in endocrinology · 2026Review
- Reference-guided computational framework identifies microenvironment metabolic subtypes and targets using pan-cancer single-cell datasets.Genome medicine · 2025Article
- VadK, a Non-Canonical Kinase that Regulates the Methylcitrate Cycle and is Essential forbioRxiv : the preprint server for biology · 2025Article
- Pyruvate kinase splice variants in fibroblasts influence cardiac remodeling after myocardial infarction in male mice.Journal of molecular and cellular cardiology · 2025Article
- Quantitative decoding of coupled carbon and energy metabolism in Pseudomonas putida for lignin carbon utilization.Communications biology · 2025Article
- FAHD1 and mitochondrial metabolism: a decade of pioneering discoveries.The FEBS journal · 2025Review
- Effects of lithium on mortality and metabolite profiles in Drosophila lithium-inducible SLC6 transporter mutants.Environmental toxicology and pharmacology · 2025Article
- Article
- Mechanisms underlining Kelp (Saccharina japonica) adaptation to relative high seawater temperature.BMC genomics · 2025Article
- Array of metabolic pathways in a kleptoplastidic foraminiferan protist supports chemoautotrophy in dark, euxinic seafloor sediments.The ISME journal · 2025Article
- Article
- Pinpointing Conditions for a Metabolic Origin of Life: Underlying Mechanisms and the Role of Coenzymes.Accounts of chemical research · 2024Article
- Citrate serves as a signal molecule to modulate carbon metabolism and iron homeostasis in Staphylococcus aureus.PLoS pathogens · 2024Article
- Core Transcriptome of Hydrogen Producing Marine Vibrios Reveals Contribution of Glycolysis in Their Efficient Hydrogen Production.Current microbiology · 2024Article
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3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
At the junction between the glycolysis and the tricarboxylic acid cycle-as well as various other metabolic pathways-lies the phosphoenolpyruvate (PEP)-pyruvate-oxaloacetate node (PPO-node). These three metabolites form the core of a network involving at least eleven different types of enzymes, each with numerous subtypes. Obviously, no single organism maintains each of these eleven enzymes; instead, different organisms possess different subsets in their PPO-node, which results in a remarkable degree of variation, despite connecting such deeply conserved metabolic pathways as the glycolysis and the tricarboxylic acid cycle. The PPO-node enzymes play a crucial role in cellular energetics, with most of them involved in (de)phosphorylation of nucleotide phosphates, while those responsible for malate conversion are important redox enzymes. Variations in PPO-node therefore reflect the different energetic niches that organisms can occupy. In this review, we give an overview of the biochemistry of these eleven PPO-node enzymes. We attempt to highlight the variation that exists, both in PPO-node compositions, as well as in the roles that the enzymes can have within those different settings, through various recent discoveries in both bacteria and archaea that reveal deviations from canonical functions.
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