ArticlePlant molecular biology2008
Arabidopsis thaliana NADP-malic enzyme isoforms: high degree of identity but clearly distinct properties.
Article in Plant molecular biology, 2008. 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, 90 citations in OpenAlex.
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- Cucumber malate decarboxylase, CsNADP-ME2, functions in the balance of carbon and amino acid metabolism in fruit.Horticulture research · 2023Article
- Overexpression of chloroplastic Zea mays NADP-malic enzyme (ZmNADP-ME) confers tolerance to salt stress in Arabidopsis thaliana.Photosynthesis research · 2023Article
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- Proteomic and Metabolic Analysis ofInternational journal of molecular sciences · 2023Article
- Respiratory and C4-photosynthetic NAD-malic enzyme coexist in bundle sheath cell mitochondria and evolved via association of differentially adapted subunits.The Plant cell · 2022Article
- Structural insights into the allosteric site of Arabidopsis NADP-malic enzyme 2: role of the second sphere residues in the regulatory signal transmission.Plant molecular biology · 2021Article
- Photorespiration: The Futile Cycle?Plants (Basel, Switzerland) · 2021Review
- Central Metabolism in Mammals and Plants as a Hub for Controlling Cell Fate.Antioxidants & redox signaling · 2021Review
- The Role of Yeasts and Lactic Acid Bacteria on the Metabolism of Organic Acids during Winemaking.Foods (Basel, Switzerland) · 2020Review
- Identification and evolution of CBMC plant biology · 2020Article
- Independent Recruitment of Duplicated β-Subunit-Coding NAD-ME Genes Aided the Evolution of C4 Photosynthesis in Cleomaceae.Frontiers in plant science · 2020Article
- NADP-Dependent Malic Enzyme 1 Participates in the Abscisic Acid Response inFrontiers in plant science · 2018Article
- Chimeric Structure of Plant Malic Enzyme Family: Different Evolutionary Scenarios for NAD- and NADP-Dependent Isoforms.Frontiers in plant science · 2018Article
- Soybean NADP-Malic Enzyme Functions in Malate and Citrate Metabolism and Contributes to Their Efflux under Al Stress.Frontiers in plant science · 2017Article
- Genome-wide identification, classification, and analysis of NADP-ME family members from 12 crucifer species.Molecular genetics and genomics : MGG · 2016Article
- The dilemma for lipid productivity in green microalgae: importance of substrate provision in improving oil yield without sacrificing growth.Biotechnology for biofuels · 2016Review
- 2-Hydroxy Acids in Plant Metabolism.The arabidopsis book · 2015Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Arabidopsis thaliana genome contains four NADP-malic enzymes genes (NADP-ME1-4). NADP-ME4 is localized to plastids whereas the other isoforms are cytosolic. NADP-ME2 and 4 are constitutively expressed, while NADP-ME1 is restricted to secondary roots and NADP-ME3 to trichomes and pollen. Although the four isoforms share remarkably high degree of identity (75-90%), recombinant NADP-ME1 through 4 show distinct kinetic properties, both in the forward (malate oxidative decarboxylation) and reverse (pyruvate reductive carboxylation) reactions. The four isoforms behave differently in terms of reversibility, with NADP-ME2 presenting the highest reverse catalytic efficiency. When analyzing the activity of each isoform in the presence of metabolic effectors, NADP-ME2 was the most highly regulated isoform, especially in its activation by certain effectors. Several metabolites modulate both the forward and reverse reactions, exhibiting dual effects in some cases. Therefore, pyruvate reductive carboxylation may be relevant in vivo, especially in some cellular compartments and conditions. In order to identify residues or segments of the NADP-ME primary structure that could be involved in the differences among the isoforms, NADP-ME2 mutants and deletions were analysed. The results obtained show that Arg115 is involved in fumarate activation, while the amino-terminal part is critical for aspartate and CoA activation, as well as for the reverse reaction. As a whole, these studies show that minimal changes in the primary structure are responsible for the different kinetic behaviour of each AtNADP-ME isoform. In this way, the co-expression of some isoforms in the same cellular compartment would not imply redundancy but represents specificity of function.
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