ArticleThe Journal of biological chemistry2009
Bacterial-type phosphoenolpyruvate carboxylase (PEPC) functions as a catalytic and regulatory subunit of the novel class-2 PEPC complex of vascular plants.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 64 citations in OpenAlex.
- Malate matters: disrupting bacterial-type phosphoenolpyruvate carboxylase (BTPC) rewires tomato fruit development.Plant physiology · 2026Article
- Cryptic CAM photosynthesis in Joshua tree (Yucca brevifolia, Y. jaegeriana).The New phytologist · 2025Article
- Comparative Genomics of Chloropicon primus and Chloropicon roscoffensis Provide Insights into the Evolutionary Dynamics and Ecological Success of These Tiny Green Algae in Marine Environments.Genome biology and evolution · 2025Article
- Phosphoenolpyruvate and Related Metabolic Pathways Contribute to the Regulation of Plant Growth and Development.International journal of molecular sciences · 2025Review
- Encoded CPlant signaling & behavior · 2022Review
- Differential timing of gene expression and recruitment in independent origins of CAM in the Agavoideae (Asparagaceae).The New phytologist · 2022Article
- Knock-down of phosphoenolpyruvate carboxylase 3 negatively impacts growth, productivity, and responses to salt stress in sorghum (Sorghum bicolor L.).The Plant journal : for cell and molecular biology · 2022Article
- Differential Expression, Tissue-Specific Distribution, and Posttranslational Controls of Phosphoenolpyruvate Carboxylase.Plants (Basel, Switzerland) · 2021Review
- The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism.FEMS microbiology reviews · 2021Article
- Genome-Wide Identification and Analysis of the Phosphoenolpyruvate Carboxylase Gene Family inFrontiers in plant science · 2021Article
- Identification of Structural Variants in Two Novel Genomes of Maize Inbred Lines Possibly Related to Glyphosate Tolerance.Plants (Basel, Switzerland) · 2020Article
- An integrated omics analysis reveals molecular mechanisms that are associated with differences in seed oil content between Glycine max and Brassica napus.BMC plant biology · 2018Article
- Analysis of Protein Complexes in the Unicellular Cyanobacterium Cyanothece ATCC 51142.Journal of proteome research · 2018Article
- Transcript profiling indicates a widespread role for bacterial-type phosphoenolpyruvate carboxylase in malate-accumulating sink tissues.Journal of experimental botany · 2017Article
- Regulatory Phosphorylation of Bacterial-Type PEP Carboxylase by the CaPlant physiology · 2017Article
- Phosphoenolpyruvate Carboxylase in Arabidopsis Leaves Plays a Crucial Role in Carbon and Nitrogen Metabolism.Plant physiology · 2015Article
- A proteomic strategy for global analysis of plant protein complexes.The Plant cell · 2014Article
- Reciprocal control of anaplerotic phosphoenolpyruvate carboxylase by in vivo monoubiquitination and phosphorylation in developing proteoid roots of phosphate-deficient harsh hakea.Plant physiology · 2013Article
- Tissue-specific expression and post-translational modifications of plant- and bacterial-type phosphoenolpyruvate carboxylase isozymes of the castor oil plant, Ricinus communis L.Journal of experimental botany · 2011Article
- Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate.Proteins · 2011Article
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4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoenolpyruvate carboxylase (PEPC) is a tightly regulated anaplerotic enzyme situated at a major branch point of the plant C metabolism. Two distinct oligomeric classes of PEPC occur in the triglyceride-rich endosperm of developing castor oil seeds (COS). Class-1 PEPC is a typical homotetramer composed of identical 107-kDa plant-type PEPC (PTPC) subunits (encoded by RcPpc3), whereas the novel Class-2 PEPC 910-kDa hetero-octameric complex arises from a tight interaction between Class-1 PEPC and distantly related 118-kDa bacterial-type PEPC (BTPC) polypeptides (encoded by RcPpc4). Here, COS BTPC was expressed from full-length RcPpc4 cDNA in Escherichia coli as an active PEPC that exhibited unusual properties relative to PTPCs, including a tendency to form large aggregates, enhanced thermal stability, a high K(m)((PEP)), and insensitivity to metabolite effectors. A chimeric 900-kDa Class-2 PEPC hetero-octamer having a 1:1 stoichiometry of BTPC:PTPC subunits was isolated from a mixture of clarified extracts containing recombinant RcPPC4 and an Arabidopsis thaliana Class-1 PEPC (the PTPC, AtPPC3). The purified Class-2 PEPC exhibited biphasic PEP saturation kinetics with high and low affinity sites attributed to its AtPPC3 and RcPPC4 subunits, respectively. The RcPPC4 subunits: (i) catalyzed the majority of the Class-2 PEPC V(max), particularly in the presence of the inhibitor l-malate, and (ii) also functioned as Class-2 PEPC regulatory subunits by modulating PEP binding and catalytic potential of its AtPPC3 subunits. BTPCs appear to associate with PTPCs to form stable Class-2 PEPC complexes in vivo that are hypothesized to maintain high flux from PEP under physiological conditions that would otherwise inhibit Class-1 PEPCs.
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