ArticleJournal of lipid research2015
Structural insights into the substrate specificity of two esterases from the thermophilic Rhizomucor miehei.
Article in Journal of lipid research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Catalytic His-loop flexibility drives high activity in hyperthermophilic esterase EstE1 while preserving structural stability.Microbiology spectrum · 2025Article
- Nanomaterial scaffolds for enzymatic polymer degradation: a tool to advance current biodegradation assessments of polymers in liquid formulation.Bioscience nanotechnology · 2025Review
- Crystallization and preliminary X-ray crystallographic studies of AfeH from Acimetobacter sp. DL-2.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Characterization of a family IV esterase from extremely halophilic archaeon Haloarcula japonica.Extremophiles : life under extreme conditions · 2024Article
- Biochemical characterization of an esterase from Thermobifida fusca YX with acetyl xylan esterase activity.Molecular biology reports · 2024Article
- 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
- 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 characterization of an esterase from Clostridium acetobutylicum with novel GYSMG pentapeptide motif at the catalytic domain.Journal of industrial microbiology & biotechnology · 2020Article
- Comparative analysis of the human serine hydrolase OVCA2 to the model serine hydrolase homolog FSH1 from S. cerevisiae.PloS one · 2020Article
- Biochemical characterization of a novel thermostable feruloyl esterase from Geobacillus thermoglucosidasius DSM 2542Molecular biology reports · 2019Article
- Microbial esterases and ester prodrugs: An unlikely marriage for combating antibiotic resistance.Drug development research · 2019Review
- Article
- Two novel deep-sea sediment metagenome-derived esterases: residue 199 is the determinant of substrate specificity and preference.Microbial cell factories · 2018Article
- A family of archaea-like carboxylesterases preferentially expressed in the symbiotic phase of the mychorrizal fungus Tuber melanosporum.Scientific reports · 2017Article
- The first description of a hormone-sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase.MicrobiologyOpen · 2017Article
- Complete genome sequence of esterase-producing bacteriumStandards in genomic sciences · 2017Article
- Structural Basis for the Strict Substrate Selectivity of the Mycobacterial Hydrolase LipW.Biochemistry · 2016Article
- Metagenomic mining for thermostable esterolytic enzymes uncovers a new family of bacterial esterases.Scientific reports · 2016Article
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two hormone-sensitive lipase (HSL) family esterases (RmEstA and RmEstB) from the thermophilic fungus Rhizomucor miehei, exhibiting distinct substrate specificity, have been recently reported to show great potential in industrial applications. In this study, the crystal structures of RmEstA and RmEstB were determined at 2.15 Å and 2.43 Å resolutions, respectively. The structures of RmEstA and RmEstB showed two distinctive domains, a catalytic domain and a cap domain, with the classical α/β-hydrolase fold. Catalytic triads consisting of residues Ser161, Asp262, and His292 in RmEstA, and Ser164, Asp261, and His291 in RmEstB were found in the respective canonical positions. Structural comparison of RmEstA and RmEstB revealed that their distinct substrate specificity might be attributed to their different substrate-binding pockets. The aromatic amino acids Phe222 and Trp92, located in the center of the substrate-binding pocket of RmEstB, blocked this pocket, thus narrowing its catalytic range for substrates (C2-C8). Two mutants (F222A and W92F in RmEstB) showing higher catalytic activity toward long-chain substrates further confirmed the hypothesized interference. This is the first report of HSL family esterase structures from filamentous fungi. The information on structure-function relationships could open important avenues of exploration for further industrial applications of esterases.
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