ArticleScientific reports2017
Structural insight into a CE15 esterase from the marine bacterial metagenome.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed.
- Structural, Biochemical, and Phylogenetic Analysis of Bacterial and Fungal Carbohydrate Esterase Family 15 Glucuronoyl Esterases in the Rumen.The protein journal · 2024Article
- Exploration of three Dyadobacter fermentans enzymes uncovers molecular activity determinants in CE15.Applied microbiology and biotechnology · 2024Article
- New insights to diversity and enzyme-substrate interactions of fungal glucuronoyl esterases.Applied microbiology and biotechnology · 2023Review
- Structural and functional investigation of a fungal member of carbohydrate esterase family 15 with potential specificity for rare xylans.Acta crystallographica. Section D, Structural biology · 2023Article
- Glucuronoyl esterases - enzymes to decouple lignin and carbohydrates and enable better utilization of renewable plant biomass.Essays in biochemistry · 2023Review
- Mechanism and biomass association of glucuronoyl esterase: an α/β hydrolase with potential in biomass conversion.Nature communications · 2022Article
- Structural and Functional Analysis of a Multimodular Hyperthermostable Xylanase-Glucuronoyl Esterase fromBiochemistry · 2021Article
- The coordinated action of glucuronoyl esterase and α-glucuronidase promotes the disassembly of lignin-carbohydrate complexes.FEBS letters · 2021Article
- The structural basis of fungal glucuronoyl esterase activity on natural substrates.Nature communications · 2020Article
- Investigation of a thermostable multi-domain xylanase-glucuronoyl esterase enzyme fromBiotechnology for biofuels · 2020Article
- Structural and biochemical studies of the glucuronoyl esteraseThe Journal of biological chemistry · 2019Article
- Structure-function analyses reveal that a glucuronoyl esterase fromThe Journal of biological chemistry · 2019Article
- Biochemical and structural features of diverse bacterial glucuronoyl esterases facilitating recalcitrant biomass conversion.Biotechnology for biofuels · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-characterized fungal homologs, and resolves three large loop regions that are unique to this bacterial sub-clade. The catalytic triad of the bacterial CE15, which includes Asp 332 as its third member, closely resembles that of family 1 carbohydrate esterases (CE1), despite the overall lower structural similarity with members of this family. Two of the three loop regions form a subdomain that deepens the active site pocket and includes several basic residues that contribute to the high positive charge surrounding the active site. Docking simulations predict specific interactions with the sugar moiety of glucuronic-acid substrates, and with aromatically-substituted derivatives that serve as model compounds for the lignin-carbohydrate complex of plant cell walls. Molecular dynamics simulations indicate considerable flexibility of the sub-domain in the substrate-bound form, suggesting plasticity to accommodate different substrates is possible. The findings from this first reported structure of a bacterial member of the CE15 family provide insight into the basis of its broader substrate specificity.
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.