ArticleNature communications2023
Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 52 citations in OpenAlex.
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- An Alternative DNA Endonuclease Activity is Associated with the LINE-1 ORF2-encoded Protein.bioRxiv : the preprint server for biology · 2026Article
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- Mechanism of synergistic ultrasound-ethanol treatment in salted egg yolk: Rapid texture optimization and flavor enhancement.Food chemistry: X · 2025Article
- Challenges in Mechanistic Investigation of a Flexible Aminocatalyst as Demonstrated through Enamine Formation.ChemistryOpen · 2025Article
- Is a Malleable Active Site Loop the Key to High Substrate Promiscuity? Hybrid, Biocatalytic Route to Structurally Diverse Taxoid Side Chains with Remarkable Dual Stereocontrol.Angewandte Chemie (International ed. in English) · 2025Article
- A SlMYB78-regulated bifunctional gene cluster for phenolamide and salicylic acid biosynthesis during tomato domestication, reducing disease resistance.Journal of integrative plant biology · 2025Article
- Structural insights into the dual CaNature communications · 2025Article
- Article
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- Enzymolysis Modes Trigger Diversity in Inhibitor-α-Amylase Aggregating Behaviors and Activity Inhibition: A New Insight Into Enzyme Inhibition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Lipase-mediated detoxification of host-derived antimicrobial fatty acids by Staphylococcus aureus.Communications biology · 2024Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although enzyme catalysis is typified by high specificity, enzymes can catalyze various substrates (substrate promiscuity) and/or different reaction types (catalytic promiscuity) using a single active site. This interesting phenomenon is widely distributed in enzyme catalysis, with both fundamental and applied importance. To date, the mechanistic understanding of enzyme promiscuity is very limited. Herein, we report the structural mechanism underlying the substrate and catalytic promiscuity of Vibrio dual lipase/transferase (VDLT). Crystal structures of the VDLT from Vibrio alginolyticus (ValDLT) and its fatty acid complexes were solved, revealing prominent structural flexibility. In particular, the "Ser-His-Asp" catalytic triad machinery of ValDLT contains an intrinsically flexible oxyanion hole. Analysis of ligand-bound structures and mutagenesis showed that the flexible oxyanion hole and other binding residues can undergo distinct conformational changes to facilitate substrate and catalytic promiscuity. Our study reveals a previously unknown flexible form of the famous catalytic triad machinery and proposes a "catalytic site tuning" mechanism to expand the mechanistic paradigm of enzyme promiscuity.
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