ArticleNature communications2013
Greater efficiency of photosynthetic carbon fixation due to single amino-acid substitution.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Novel Amino Acid Changes Increase Phosphoenolpyruvate Carboxylase Output in planta.Plant, cell & environment · 2026Article
- Evidence for a COThe New phytologist · 2025Article
- Exploring the Increased Activity of the Blue Light-Dependent Photoenzyme Fatty Acid Photodecarboxylase under Violet Light.ACS catalysis · 2025Article
- Regulation of Crassulacean acid metabolism at the protein level in Kalanchoë laxiflora.Plant physiology · 2025Article
- Soil and climate factors affect the nutrient resorption characteristics of desert shrub roots in Xinjiang, China.Frontiers in plant science · 2025Article
- Leaf transcriptomes from C3, C3-C4 intermediate, and C4Neurachne species give insights into C4 photosynthesis evolution.Plant physiology · 2024Article
- Multiple highly expressed phosphoenolpyruvate carboxylase genes have divergent enzyme kinetic properties in two C4 grasses.Annals of botany · 2023Article
- Gene duplications facilitate C4-CAM compatibility in common purslane.Plant physiology · 2023Article
- A Machine Learning Framework Identifies Plastid-Encoded Proteins Harboring C3 and C4 Distinguishing Sequence Information.Genome biology and evolution · 2023Article
- Genome-wide identification and comparative analyses of key genes involved in CFrontiers in plant science · 2023Article
- Computational Docking Reveals Co-Evolution of C4 Carbon Delivery Enzymes in Diverse Plants.International journal of molecular sciences · 2022Article
- Responses of photosynthetic characteristics of oat flag leaf and spike to drought stress.Frontiers in plant science · 2022Article
- Comparative analysis of farmer practices and high yield experiments: Farmers could get more maize yield from maize-soybean relay intercropping through high density cultivation of maize.Frontiers in plant science · 2022Article
- Microbial Utilization of Next-Generation Feedstocks for the Biomanufacturing of Value-Added Chemicals and Food Ingredients.Frontiers in bioengineering and biotechnology · 2022Review
- Article
- AnBio-protocol · 2021Article
- Improving C4 photosynthesis to increase productivity under optimal and suboptimal conditions.Journal of experimental botany · 2021Article
- The coordination of major events in CScientific reports · 2021Article
- Third-generation sequencing and metabolome analysis reveal candidate genes and metabolites with altered levels in albino jackfruit seedlings.BMC genomics · 2021Article
- Genome-Wide Identification and Analysis of the Phosphoenolpyruvate Carboxylase Gene Family inFrontiers in plant science · 2021Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The C4-photosynthetic carbon cycle is an elaborated addition to the classical C3-photosynthetic pathway, which improves solar conversion efficiency. The key enzyme in this pathway, phosphoenolpyruvate carboxylase, has evolved from an ancestral non-photosynthetic C3 phosphoenolpyruvate carboxylase. During evolution, C4 phosphoenolpyruvate carboxylase has increased its kinetic efficiency and reduced its sensitivity towards the feedback inhibitors malate and aspartate. An open question is the molecular basis of the shift in inhibitor tolerance. Here we show that a single-point mutation is sufficient to account for the drastic differences between the inhibitor tolerances of C3 and C4 phosphoenolpyruvate carboxylases. We solved high-resolution X-ray crystal structures of a C3 phosphoenolpyruvate carboxylase and a closely related C4 phosphoenolpyruvate carboxylase. The comparison of both structures revealed that Arg884 supports tight inhibitor binding in the C3-type enzyme. In the C4 phosphoenolpyruvate carboxylase isoform, this arginine is replaced by glycine. The substitution reduces inhibitor affinity and enables the enzyme to participate in the C4 photosynthesis pathway.
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