ArticleThe Journal of biological chemistry2015
Interdomain hydrophobic interactions modulate the thermostability of microbial esterases from the hormone-sensitive lipase family.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 citing papers in PubMed, 72 citations in OpenAlex.
- Dynamic and Catalytic Multiphase Coacervates.Biomacromolecules · 2026Article
- Ayu: a machine intelligence tool for identification of extracellular proteins in the marine secretome.Nature communications · 2025Article
- Abridgement of Microbial Esterases and Their Eminent Industrial Endeavors.Molecular biotechnology · 2025Review
- Characterization of a family IV esterase from extremely halophilic archaeon Haloarcula japonica.Extremophiles : life under extreme conditions · 2024Article
- C-Terminal β8-α9 Interaction Modulates Thermal Stability and Enzymatic Activity Differently in Hyperthermophilic Esterase EstE1 and Mesophilic Esterase rPPE.Applied and environmental microbiology · 2023Article
- Sequence and Structural Motifs Controlling the Broad Substrate Specificity of the Mycobacterial Hormone-Sensitive Lipase LipN.ACS omega · 2023Article
- Crystal structure and biochemical analysis of acetylesterase (LgEstI) from Lactococcus garvieae.PloS one · 2023Article
- Evaluation of a Thermophilic, Psychrostable, and Heavy Metal-Resistant Red Sea Brine Pool Esterase.Marine drugs · 2022Article
- Identification and characterization of a novel carboxylesterase EstQ7 from a soil metagenomic library.Archives of microbiology · 2021Article
- Molecular Characterization of Novel Family IV and VIII Esterases from a Compost Metagenomic Library.Microorganisms · 2021Article
- Article
- Structural and Biochemical Characterization of a Cold-Active PMGL3 Esterase with Unusual Oligomeric Structure.Biomolecules · 2021Article
- Mechanism and Structural Insights Into a Novel Esterase, E53, Isolated FromFrontiers in microbiology · 2021Article
- Biochemical and Structural Characterization of a novel thermophilic esterase EstD11 provide catalytic insights for the HSL family.Computational and structural biotechnology journal · 2021Article
- Sequence-Based Prediction of Promiscuous Acyltransferase Activity in Hydrolases.Angewandte Chemie (International ed. in English) · 2020Article
- Characterization of Novel Salt-Tolerant Esterase Isolated from the Marine BacteriumJournal of microbiology and biotechnology · 2020Article
- Comparative analysis of the human serine hydrolase OVCA2 to the model serine hydrolase homolog FSH1 from S. cerevisiae.PloS one · 2020Article
- Crystal structure of PMGL2 esterase from the hormone-sensitive lipase family with GCSAG motif around the catalytic serine.PloS one · 2020Article
- Thermal Inactivation of a Cold-Active Esterase PMGL3 Isolated from the Permafrost Metagenomic Library.Biomolecules · 2019Article
- Rational Design of Alginate Lyase fromMarine drugs · 2019Article
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12 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Microbial hormone-sensitive lipases (HSLs) contain a CAP domain and a catalytic domain. However, it remains unclear how the CAP domain interacts with the catalytic domain to maintain the stability of microbial HSLs. Here, we isolated an HSL esterase, E40, from a marine sedimental metagenomic library. E40 exhibited the maximal activity at 45 °C and was quite thermolabile, with a half-life of only 2 min at 40 °C, which may be an adaptation of E40 to the permanently cold sediment environment. The structure of E40 was solved to study its thermolability. Structural analysis showed that E40 lacks the interdomain hydrophobic interactions between loop 1 of the CAP domain and α7 of the catalytic domain compared with its thermostable homologs. Mutational analysis showed that the introduction of hydrophobic residues Trp(202) and Phe(203) in α7 significantly improved E40 stability and that a further introduction of hydrophobic residues in loop 1 made E40 more thermostable because of the formation of interdomain hydrophobic interactions. Altogether, the results indicate that the absence of interdomain hydrophobic interactions between loop 1 and α7 leads to the thermolability of E40. In addition, a comparative analysis of the structures of E40 and other thermolabile and thermostable HSLs suggests that the interdomain hydrophobic interactions between loop 1 and α7 are a key element for the thermostability of microbial HSLs. Therefore, this study not only illustrates the structural element leading to the thermolability of E40 but also reveals a structural determinant for HSL thermostability.
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