ArticleThe Journal of biological chemistry2018
Functional metagenomics identifies an exosialidase with an inverting catalytic mechanism that defines a new glycoside hydrolase family (GH156).
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed.
- Development of a Microdroplet-Based Functional Genomic Screening Pipeline by Combination of DNA Nanoflowers and PURExpress Cell-Free Expression.ACS synthetic biology · 2026Article
- Metagenomics and its impact on environmental and therapeutic microbiology.Archives of microbiology · 2025Review
- A self-immolative Kdn-glycoside substrate enables high-throughput screening for inhibitors of Kdnases.Glycobiology · 2025Article
- Plasmid Library Construction From Genomic DNA.Current protocols · 2025Article
- Carbohydrate-active enzyme (CAZyme) discovery and engineeringRSC chemical biology · 2024Review
- High-throughput nanopore DNA sequencing of large insert fosmid clones directly from bacterial colonies.Applied and environmental microbiology · 2024Article
- Genetic and functional diversity of β-N-acetylgalactosamine-targeting glycosidases expanded by deep-sea metagenome analysis.Nature communications · 2024Article
- Pangenome analysis provides insights into the genetic diversity, metabolic versatility, and evolution of the genusMicrobiology spectrum · 2023Article
- Gut Microbial Sialidases and Their Role in the Metabolism of Human Milk Sialylated Glycans.International journal of molecular sciences · 2023Review
- Mucin utilization by gut microbiota: recent advances on characterization of key enzymes.Essays in biochemistry · 2023Review
- Archaea as a Model System for Molecular Biology and Biotechnology.Biomolecules · 2023Review
- Metagenomic survey reveals global distribution and evolution of microbial sialic acid catabolism.Frontiers in microbiology · 2023Article
- Human Gut Metagenomes Encode Diverse GH156 Sialidases.Applied and environmental microbiology · 2022Article
- Characterization of a New TemperatePathogens (Basel, Switzerland) · 2022Article
- Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022Review
- Functional metagenomic screening identifies an unexpected β-glucuronidase.Nature chemical biology · 2022Article
- Metagenomic mining of Indian river confluence reveal functional microbial community with lignocelluloytic potential.3 Biotech · 2022Article
- Cloning of cellulase gene using metagenomic approach of soils collected from Wadi El Natrun, an extremophilic desert valley in Egypt.Journal, genetic engineering & biotechnology · 2022Article
- Capillary Electrophoresis-Based Functional Genomics Screening to Discover Novel Archaeal DNA Modifying Enzymes.Applied and environmental microbiology · 2022Article
- Potential Use of Microbial Community Genomes in Various Dimensions of Agriculture Productivity and Its Management: A Review.Frontiers in microbiology · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Exosialidases are glycoside hydrolases that remove a single terminal sialic acid residue from oligosaccharides. They are widely distributed in biology, having been found in prokaryotes, eukaryotes, and certain viruses. Most characterized prokaryotic sialidases are from organisms that are pathogenic or commensal with mammals. However, in this study, we used functional metagenomic screening to seek microbial sialidases encoded by environmental DNA isolated from an extreme ecological niche, a thermal spring. Using recombinant expression of potential exosialidase candidates and a fluorogenic sialidase substrate, we discovered an exosialidase having no homology to known sialidases. Phylogenetic analysis indicated that this protein is a member of a small family of bacterial proteins of previously unknown function. Proton NMR revealed that this enzyme functions via an inverting catalytic mechanism, a biochemical property that is distinct from those of known exosialidases. This unique inverting exosialidase defines a new CAZy glycoside hydrolase family we have designated GH156.
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.