ArticlePlant molecular biology2013
Structural, kinetic and computational investigation of Vitis vinifera DHDPS reveals new insight into the mechanism of lysine-mediated allosteric inhibition.
Article in Plant molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 34 citations in OpenAlex.
- Comprehensive Review of L-Lysine: Chemistry, Occurrence, and Physiological Roles.Current protein & peptide science · 2026Review
- Genome-Wide Association Study for Seed Dormancy Using Re-Sequenced Germplasm under Multiple Conditions in Rice.International journal of molecular sciences · 2023Article
- ColorimetricHeliyon · 2023Article
- The Hidden Potential of High-Throughput RNA-Seq Re-Analysis, a Case Study for DHDPS, Key Enzyme of the Aspartate-Derived Lysine Biosynthesis Pathway and Its Role in Abiotic and Biotic Stress Responses in Soybean.Plants (Basel, Switzerland) · 2022Article
- Host-genotype-dependent cecal microbes are linked to breast muscle metabolites in Chinese chickens.iScience · 2022Article
- Engineering a feedback inhibition-insensitive plant dihydrodipicolinate synthase to increase lysine content in Camelina sativa seeds.Transgenic research · 2022Article
- Article
- Characterization of recombinant dihydrodipicolinate synthase from the bread wheat Triticum aestivum.Planta · 2018Article
- Molecular evolution of an oligomeric biocatalyst functioning in lysine biosynthesis.Biophysical reviews · 2018Review
- Structure and Function of Cyanobacterial DHDPS and DHDPR.Scientific reports · 2016Article
- Dimerization of Bacterial Diaminopimelate Decarboxylase Is Essential for Catalysis.The Journal of biological chemistry · 2016Article
- Dynamic Modelling Reveals 'Hotspots' on the Pathway to Enzyme-Substrate Complex Formation.PLoS computational biology · 2016Article
- Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- From knock-out phenotype to three-dimensional structure of a promising antibiotic target from Streptococcus pneumoniae.PloS one · 2013Article
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysine is one of the most limiting amino acids in plants and its biosynthesis is carefully regulated through inhibition of the first committed step in the pathway catalyzed by dihydrodipicolinate synthase (DHDPS). This is mediated via a feedback mechanism involving the binding of lysine to the allosteric cleft of DHDPS. However, the precise allosteric mechanism is yet to be defined. We present a thorough enzyme kinetic and thermodynamic analysis of lysine inhibition of DHDPS from the common grapevine, Vitis vinifera (Vv). Our studies demonstrate that lysine binding is both tight (relative to bacterial DHDPS orthologs) and cooperative. The crystal structure of the enzyme bound to lysine (2.4 Å) identifies the allosteric binding site and clearly shows a conformational change of several residues within the allosteric and active sites. Molecular dynamics simulations comparing the lysine-bound (PDB ID 4HNN) and lysine free (PDB ID 3TUU) structures show that Tyr132, a key catalytic site residue, undergoes significant rotational motion upon lysine binding. This suggests proton relay through the catalytic triad is attenuated in the presence of lysine. Our study reveals for the first time the structural mechanism for allosteric inhibition of DHDPS from the common grapevine.
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