ArticleScientific reports2017
Structural basis for redox sensitivity in Corynebacterium glutamicum diaminopimelate epimerase: an enzyme involved in l-lysine biosynthesis.
Article in Scientific reports, 2017. 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.
- Classification of Protein Disulfide Bonds.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Natural variation in ZmDapF1 enhances maize drought resilience.Nature plants · 2025Article
- Structure and inhibition of diaminopimelic acid epimerase by slow-binding α-methyl amino acids.Protein science : a publication of the Protein Society · 2025Article
- Intracellular self-assembly and metabolite analysis of key enzymes for L-lysine synthesis based on key components of cellulosomes.Frontiers in microbiology · 2025Article
- Genetic analysis of QTLs for lysine content in four maize DH populations.BMC genomics · 2024Article
- Computational Modelling, Functional Characterization and Molecular Docking to Lead Compounds of Bordetella pertussis Diaminopimelate Epimerase.Applied biochemistry and biotechnology · 2023Article
- Reconstruction of the Diaminopimelic Acid Pathway to Promote L-lysine Production inInternational journal of molecular sciences · 2021Article
- Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.Chemical Society reviews · 2021Review
- Metabolic engineering of carbohydrate metabolism systems in Corynebacterium glutamicum for improving the efficiency of L-lysine production from mixed sugar.Microbial cell factories · 2020Article
- Metabolic engineering of glucose uptake systems in Corynebacterium glutamicum for improving the efficiency of L-lysine production.Journal of industrial microbiology & biotechnology · 2019Article
- Allosteric disulphide bonds as reversible mechano-sensitive switches that control protein functions in the vasculature.Biophysical reviews · 2019Review
- Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation.The Journal of biological chemistry · 2019Review
- Overexpression of thermostable meso-diaminopimelate dehydrogenase to redirect diaminopimelate pathway for increasing L-lysine production in Escherichia coli.Scientific reports · 2019Article
- Nutty-like flavor production byJournal of advanced research · 2018Article
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2 authors.
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Abstract
Diaminopimelate epimerase (DapF) is one of the crucial enzymes involved in l-lysine biosynthesis, where it converts l,l-diaminopimelate (l,l-DAP) into d,l-DAP. DapF is also considered as an attractive target for the development of antibacterial drugs. Here, we report the crystal structure of DapF from Corynebacterium glutamicum (CgDapF). Structures of CgDapF obtained under both oxidized and reduced conditions reveal that the function of CgDapF is regulated by redox-switch modulation via reversible disulfide bond formation between two catalytic cysteine residues. Under oxidized condition, two catalytic cysteine residues form a disulfide bond; these same cysteine residues exist in reduced form under reduced condition. Disulfide bond formation also induces a subsequent structural change in the dynamic catalytic loop at the active site, which results in open/closed conformational change at the active site. We also determined the crystal structure of CgDapF in complex with its product d,l-DAP, and elucidated how the enzyme recognizes its substrate l,l-DAP as a substrate. Moreover, the structure in complex with the d,l-DAP product reveals that CgDapF undergoes a large open/closed domain movement upon substrate binding, resulting in a completely buried active site with the substrate bound.
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