ArticleFrontiers in plant science2015
Evolution of plant δ(1)-pyrroline-5-carboxylate reductases from phylogenetic and structural perspectives.
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 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Functional Characterization ofMicroorganisms · 2022Article
- Deciphering the structure ofComputational and structural biotechnology journal · 2022Article
- 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
- Peculiar substrate specificity of δMolecular biology reports · 2021Article
- Disease variants of human ΔArchives of biochemistry and biophysics · 2021Article
- A Specific and Sensitive Enzymatic Assay for the Quantitation of L-Proline.Frontiers in plant science · 2020Article
- Functional Characterization of Four Putative δFrontiers in microbiology · 2017Article
- Structural Investigations of N-carbamoylputrescine Amidohydrolase from Medicago truncatula: Insights into the Ultimate Step of Putrescine Biosynthesis in Plants.Frontiers in plant science · 2016Article
- Functional properties and structural characterization of rice δ(1)-pyrroline-5-carboxylate reductase.Frontiers in plant science · 2015Article
- The structure of Medicago truncatula δ(1)-pyrroline-5-carboxylate reductase provides new insights into regulation of proline biosynthesis in plants.Frontiers in plant science · 2015Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proline plays a crucial role in cell growth and stress responses, and its accumulation is essential for the tolerance of adverse environmental conditions in plants. Two routes are used to biosynthesize proline in plants. The main route uses glutamate as a precursor, while in the other route proline is derived from ornithine. The terminal step of both pathways, the conversion of δ(1)-pyrroline-5-carboxylate (P5C) to L-proline, is catalyzed by P5C reductase (P5CR) using NADH or NADPH as a cofactor. Since P5CRs are important housekeeping enzymes, they are conserved across all domains of life and appear to be relatively unaffected throughout evolution. However, global analysis of these enzymes unveiled significant functional diversity in the preference for cofactors (NADPH vs. NADH), variation in metal dependence and the differences in the oligomeric state. In our study we investigated evolutionary patterns through phylogenetic and structural analysis of P5CR representatives from all kingdoms of life, with emphasis on the plant species. We also attempted to correlate local sequence/structure variation among the functionally and structurally characterized members of the family.
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