ArticleFrontiers in plant science2015
The structure of Medicago truncatula δ(1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.
Article in Frontiers in plant science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 46 citations in OpenAlex.
- Targeting a Unique Cysteine Residue to Achieve Isoform-Selective Inhibition of the Proline Biosynthetic Enzyme Pyrroline-5-Carboxylate Reductase 2.ACS chemical biology · 2026Article
- Integrated transcriptome and metabolome analysis revealed differential drought stress response mechanisms of wheat seedlings with varying drought tolerance.BMC plant biology · 2025Article
- Article
- Proline Tagging for Stress Tolerance in Plants.International journal of genomics · 2025Review
- Article
- Functional Dissection of the Physiological Traits Promoting Durum Wheat (Plants (Basel, Switzerland) · 2023Article
- Exogenous acetone O-(4-chlorophenylsulfonyl) oxime alleviates Cd stress-induced photosynthetic damage and oxidative stress by regulating the antioxidant defense mechanism inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2022Article
- Functional Characterization ofMicroorganisms · 2022Article
- The Emerging Role of Proline in the Establishment and Functioning of Legume-Frontiers in plant science · 2022Review
- Balanced below- and above-ground growth improved yield and water productivity by cultivar renewal for winter wheat.Frontiers in plant science · 2022Article
- Intriguing Role of Proline in Redox Potential Conferring High Temperature Stress Tolerance.Frontiers in plant science · 2022Review
- Phenyl-substituted aminomethylene-bisphosphonates inhibit human P5C reductase and show antiproliferative activity against proline-hyperproducing tumour cells.Journal of enzyme inhibition and medicinal chemistry · 2021Article
- Review
- Peculiar substrate specificity of δMolecular biology reports · 2021Article
- Disease variants of human ΔArchives of biochemistry and biophysics · 2021Article
- Enzymology and Regulation of δFrontiers in plant science · 2021Article
- Physiological and proteomics responses of nitrogen assimilation and glutamine/glutamine family of amino acids metabolism in mulberry (Plant signaling & behavior · 2020Article
- A Specific and Sensitive Enzymatic Assay for the Quantitation of L-Proline.Frontiers in plant science · 2020Article
- Plant growth regulators improve growth, photosynthesis, mineral nutrient and antioxidant system under cadmium stress in menthol mint (Physiology and molecular biology of plants : an international journal of functional plant biology · 2020Article
- Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.The Journal of biological chemistry · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The two pathways for proline biosynthesis in higher plants share the last step, the conversion of δ(1)-pyrroline-5-carboxylate (P5C) to L-proline, which is catalyzed by P5C reductase (P5CR, EC 1.5.1.2) with the use of NAD(P)H as a coenzyme. There is increasing amount of evidence to suggest a complex regulation of P5CR activity at the post-translational level, yet the molecular basis of these mechanisms is unknown. Here we report the three-dimensional structure of the P5CR enzyme from the model legume Medicago truncatula (Mt). The crystal structures of unliganded MtP5CR decamer, and its complexes with the products NAD(+), NADP(+), and L-proline were refined using x-ray diffraction data (at 1.7, 1.85, 1.95, and 2.1 Å resolution, respectively). Based on the presented structural data, the coenzyme preference for NADPH over NADH was explained, and NADPH is suggested to be the only coenzyme used by MtP5CR in vivo. Furthermore, the insensitivity of MtP5CR to feed-back inhibition by proline, revealed by enzymatic analysis, was correlated with structural features. Additionally, a mechanism for the modulation of enzyme activity by chloride anions is discussed, as well as the rationale for the possible development of effective enzyme inhibitors.
Indexed as
Identifiers
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.