ArticleMicrobial cell factories2018
Two novel deep-sea sediment metagenome-derived esterases: residue 199 is the determinant of substrate specificity and preference.
Article in Microbial cell factories, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed.
- Enzymatic Characterization of a Novel HSL Family IV Esterase EstD04 fromMolecules (Basel, Switzerland) · 2023Article
- Molecular Cloning and Characterization of a New Family VI Esterase from an Activated Sludge Metagenome.Microorganisms · 2022Article
- Isolation, identification, and biochemical characterization of a novel bifunctional phosphomannomutase/phosphoglucomutase from the metagenome of the brown algaFrontiers in microbiology · 2022Article
- Molecular Characterization of Novel Family IV and VIII Esterases from a Compost Metagenomic Library.Microorganisms · 2021Article
- Marine Bacterial Esterases: Emerging Biocatalysts for Industrial Applications.Applied biochemistry and biotechnology · 2021Review
- Characterization of a novel family VIII esterase EstM2 from soil metagenome capable of hydrolyzing estrogenic phthalates.Microbial cell factories · 2020Article
- Biochemical characterization of an esterase from Clostridium acetobutylicum with novel GYSMG pentapeptide motif at the catalytic domain.Journal of industrial microbiology & biotechnology · 2020Article
- Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases.Biotechnology for biofuels · 2020Article
- Current Status and Potential Applications of Underexplored Prokaryotes.Microorganisms · 2019Review
- One-Step Process for Environment-Friendly Preparation of Agar Oligosaccharides FromFrontiers in microbiology · 2019Article
- Characterization of a Novel Moderately Thermophilic Solvent-Tolerant Esterase Isolated From a Compost Metagenome Library.Frontiers in microbiology · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
backgroundThe deep-sea environment harbors a vast pool of novel enzymes. Owing to the limitations of cultivation, cultivation-independent has become an effective method for mining novel enzymes from the environment. Based on a deep-sea sediment metagenomics library, lipolytic-positive clones were obtained by activity-based screening methods.
resultsTwo novel esterases, DMWf18-543 and DMWf18-558, were obtained from a deep-sea metagenomic library through activity-based screening and high-throughput sequencing methods. These esterases shared 80.7% amino acid identity with each other and were determined to be new members of bacterial lipolytic enzyme family IV. The two enzymes showed the highest activities toward p-nitrophenyl (p-NP) butyrate at pH 7.0 and 35-40 °C and were found to be resistant to some metal ions (Ba
conclusionsThis study characterized two novel homologous esterases obtained from a deep-sea sediment metagenomic library. The structural modeling and mutagenesis analysis provided insight into the determinants of their substrate specificity and preference. The characterization and mechanistic analyses of these two novel enzymes should provide a basis for further exploration of their potential biotechnological applications.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.