ArticlePloS one2012
Crystal structure of Proteus mirabilis lipase, a novel lipase from the Proteus/psychrophilic subfamily of lipase family I.1.
Article in PloS one, 2012. 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, 30 citations in OpenAlex.
- Production Optimization, Partial Purification, and Biochemical Characterization of an Extracellular Lipase fromInternational journal of microbiology · 2026Article
- Prediction of lipase-specific foldase-dependence in bacterial lipase subfamilies I.1 and I.2.BMC genomics · 2025Article
- Comprehensive Insights into Microbial Lipases: Unveiling Structural Dynamics, Catalytic Mechanism, and Versatile Applications.Current microbiology · 2024Review
- An Appraisal on Prominent Industrial and Biotechnological Applications of Bacterial Lipases.Molecular biotechnology · 2023Review
- Polymer-Degrading Enzymes ofInternational journal of molecular sciences · 2023Article
- Directed evolution of a genetically encoded immobilized lipase for the efficient production of biodiesel from waste cooking oil.Biotechnology for biofuels · 2019Article
- Effects of Lid 1 Mutagenesis on Lid Displacement, Catalytic Performances and Thermostability of Cold-active Pseudomonas AMS8 Lipase in Toluene.Computational and structural biotechnology journal · 2019Article
- The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.Frontiers in bioengineering and biotechnology · 2017Review
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.Frontiers in microbiology · 2016Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial lipases from family I.1 and I.2 catalyze the hydrolysis of triacylglycerol between 25-45°C and are used extensively as biocatalysts. The lipase from Proteus mirabilis belongs to the Proteus/psychrophilic subfamily of lipase family I.1 and is a promising catalyst for biodiesel production because it can tolerate high amounts of water in the reaction. Here we present the crystal structure of the Proteus mirabilis lipase, a member of the Proteus/psychrophilic subfamily of I.1lipases. The structure of the Proteus mirabilis lipase was solved in the absence and presence of a bound phosphonate inhibitor. Unexpectedly, both the apo and inhibitor bound forms of P. mirabilis lipase were found to be in a closed conformation. The structure reveals a unique oxyanion hole and a wide active site that is solvent accessible even in the closed conformation. A distinct mechanism for Ca²⁺ coordination may explain how these lipases can fold without specific chaperones.
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