ArticlePloS one2015
Active site loop conformation regulates promiscuous activity in a lactonase from Geobacillus kaustophilus HTA426.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- The characterization of a new stabilized lactonase from the endophytic fungi Aspergillus pseudonomiae with anti-bacterial and anti-fungal properties.Protein science : a publication of the Protein Society · 2026Article
- Evaluation of Genome-Scale Model Reconstruction Strategies forMetabolites · 2025Article
- Mining Marine Metagenomes Revealed a Quorum-Quenching Lactonase with Improved Biochemical Properties That Inhibits the Food Spoilage Bacterium Pseudomonas fluorescens.Applied and environmental microbiology · 2022Article
- Review
- Enzymatic Bioremediation of Organophosphate Compounds-Progress and Remaining Challenges.Frontiers in bioengineering and biotechnology · 2019Review
- β-Glucuronidases of opportunistic bacteria are the major contributors to xenobiotic-induced toxicity in the gut.Scientific reports · 2018Article
- Loop of Streptomyces Feruloyl Esterase Plays an Important Role in the Enzyme's Catalyzing the Release of Ferulic Acid from Biomass.Applied and environmental microbiology · 2018Article
- Active Site Hydrophobicity and the Convergent Evolution of Paraoxonase Activity in Structurally Divergent Enzymes: The Case of Serum Paraoxonase 1.Journal of the American Chemical Society · 2017Article
- Integrated (Meta) Genomic and Synthetic Biology Approaches to Develop New Biocatalysts.Marine drugs · 2016Review
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzyme promiscuity is a prerequisite for fast divergent evolution of biocatalysts. A phosphotriesterase-like lactonase (PLL) from Geobacillus kaustophilus HTA426 (GkaP) exhibits main lactonase and promiscuous phosphotriesterase activities. To understand its catalytic and evolutionary mechanisms, we investigated a "hot spot" in the active site by saturation mutagenesis as well as X-ray crystallographic analyses. We found that position 99 in the active site was involved in substrate discrimination. One mutant, Y99L, exhibited 11-fold improvement over wild-type in reactivity (kcat/Km) toward the phosphotriesterase substrate ethyl-paraoxon, but showed 15-fold decrease toward the lactonase substrate δ-decanolactone, resulting in a 157-fold inversion of the substrate specificity. Structural analysis of Y99L revealed that the mutation causes a ∼6.6 Å outward shift of adjacent loop 7, which may cause increased flexibility of the active site and facilitate accommodation and/or catalysis of organophosphate substrate. This study provides for the PLL family an example of how the evolutionary route from promiscuity to specificity can derive from very few mutations, which promotes alteration in the conformational adjustment of the active site loops, in turn draws the capacity of substrate binding and activity.
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