ArticleFrontiers in microbiology2019
Characterization of a Novel Moderately Thermophilic Solvent-Tolerant Esterase Isolated From a Compost Metagenome Library.
Article in Frontiers in microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 32 citations in OpenAlex.
- Precision enzyme discovery through targeted mining of metagenomic data.Natural products and bioprospecting · 2024Review
- A scalable overexpression of a thermostable recombinant poly-histidine tag carboxyl esterase under lambda promoter: purification, characterization, and protein modelling.Journal, genetic engineering & biotechnology · 2023Article
- Enhanced Activity and Stability of an Acetyl Xylan Esterase in Hydrophilic Alcohols through Site-Directed Mutagenesis.Molecules (Basel, Switzerland) · 2023Article
- Case Studies in the Assessment of Microbial Fitness: Seemingly Subtle Changes Can Have Major Effects on Phenotypic Outcomes.Journal of molecular evolution · 2023Article
- A thermostable organic solvent-tolerant lipase fromFrontiers in microbiology · 2023Article
- Molecular Cloning and Characterization of a New Family VI Esterase from an Activated Sludge Metagenome.Microorganisms · 2022Article
- Molecular study on recombinant cold-adapted, detergent- and alkali stable esterase (EstRag) from Lysinibacillus sp.: a member of family VI.World journal of microbiology & biotechnology · 2022Article
- Evaluation of a Thermophilic, Psychrostable, and Heavy Metal-Resistant Red Sea Brine Pool Esterase.Marine drugs · 2022Article
- Characterization of a novel thermostable alkaline lipase derived from a compost metagenomic library and its potential application in the detergent industry.Frontiers in microbiology · 2022Article
- Molecular Characterization of Novel Family IV and VIII Esterases from a Compost Metagenomic Library.Microorganisms · 2021Article
- Mechanism and Structural Insights Into a Novel Esterase, E53, Isolated FromFrontiers in microbiology · 2021Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel esterase, EstCS1, was isolated from a compost metagenomics library. The EstCS1 protein, which consists of 309 amino acid residues with an anticipated molecular mass of 34 kDa, showed high amino acid sequence identities to predicted esterases and alpha/beta hydrolases (59%) from some cultured bacteria and to predicted lipases/esterases from uncultured bacteria. The phylogenetic analysis suggested that the EstCS1 belongs to the hormone-sensitive lipase family of lipolytic enzyme classification and contains a catalytic triad including Ser155-Asp255-His285. The Ser155 residue of the catalytic triad in the EstCS1 was located in the consensus active-site motif, GXSXG. Besides, a conserved HGGG motif placed in an oxyanion hole of the hormone-sensitive lipase family was discovered, too. The EstCS1 demonstrated the highest activity toward
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