ArticleBiotechnology for biofuels2017
Structure of a
Article in Biotechnology for biofuels, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed.
- A binuclear copper enzyme platform for enantioconvergent radical (pseudo)halogenation.bioRxiv : the preprint server for biology · 2026Article
- Electrochemical Insight into the Copper Redox Chemistry and HACS electrochemistry · 2026Article
- Structural and biochemical basis for activity of Aspergillus nidulans α-1,3-glucanases from glycoside hydrolase family 71.Communications biology · 2025Article
- A modular enzyme with combined hemicellulose-removing and LPMO activity increases cellulose accessibility in softwood.The FEBS journal · 2025Article
- Heterologous Expression and Biochemical Characterization of a Novel Lytic Polysaccharide Monooxygenase fromMicroorganisms · 2024Article
- The Role of the Residue at Position 2 in the Catalytic Activity of AA9 Lytic Polysaccharide Monooxygenases.International journal of molecular sciences · 2023Article
- On the impact of carbohydrate-binding modules (CBMs) in lytic polysaccharide monooxygenases (LPMOs).Essays in biochemistry · 2023Review
- Molecular Mechanism of Substrate Oxidation in Lytic Polysaccharide Monooxygenases: Insight from Theoretical Investigations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Review
- Article
- Activity and substrate specificity of lytic polysaccharide monooxygenases: An ATR FTIR-based sensitive assay tested on a novel species from Pseudomonas putida.Protein science : a publication of the Protein Society · 2022Article
- Inhibition of LPMOs by Fermented Persimmon Juice.Biomolecules · 2021Article
- Oxidized Product Profiles of AA9 Lytic Polysaccharide Monooxygenases Depend on the Type of Cellulose.ACS sustainable chemistry & engineering · 2021Article
- Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species.Biotechnology for biofuels · 2021Article
- Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs).Nature communications · 2020Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- Novel Synergistic Mechanism for Lignocellulose Degradation by a Thermophilic Filamentous Fungus and a Thermophilic Actinobacterium Based on Functional Proteomics.Frontiers in microbiology · 2020Article
- Sequence and Structural Analysis of AA9 and AA10 LPMOs: An Insight into the Basis of Substrate Specificity and Regioselectivity.International journal of molecular sciences · 2019Article
- Substrate selectivity in starch polysaccharide monooxygenases.The Journal of biological chemistry · 2019Article
- Kinetic insights into the role of the reductant in HThe Journal of biological chemistry · 2019Article
- An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification.Biotechnology for biofuels · 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
No grant is acknowledged in the PubMed record.
Abstract
backgroundAuxiliary activity (AA) enzymes are produced by numerous bacterial and fungal species to assist in the degradation of biomass. These enzymes are abundant but have yet to be fully characterized. Here, we report the X-ray structure of
resultsIn TfAA10A, Trp82 and Asn83 are needed for binding, but only Trp82 affects activity. The TfAA10B domain truncation mutants reveal that CBM2 is crucial for substrate binding, but that the X1 module does not affect binding or activity. The structure of TfAA10A is similar to other bacterial lytic polysaccharide monooxygenases with mixed features showing both type I and II copper coordination.
conclusionsThe role of LPMOs and the variability of abundance in genomes are not fully explored. LPMOs likely perform initial attacks into crystalline cellulose to allow larger processive cellulases to bind and attack, but the precise nature of their synergistic behavior remains to be definitively characterized.
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.