ReviewBiochemical Society transactions2021
Lytic polysaccharide monooxygenases and other histidine-brace copper proteins: structure, oxygen activation and biotechnological applications.
Review in Biochemical Society transactions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 60 citations in OpenAlex.
- Experimental estimation of copper-site geometry reproducibility in biologically relevant redox and saccharide-bound states of a model lytic polysaccharide monooxygenase.Acta crystallographica. Section D, Structural biology · 2026Article
- Review
- Computer-Aided Virtual Saturation Mutagenesis Improves the Lignocellulose-Degrading Performance of anFoods (Basel, Switzerland) · 2026Article
- Ammonia monooxygenase: a work in progress.Chemical science · 2026Review
- Requirement of group I lytic polysaccharide monooxygenase for turnover of chitinous cuticle during moulting in two forest pest beetles, Monochamus alternatus and Psacothea hilaris.Insect molecular biology · 2026Article
- Electrochemical Insight into the Copper Redox Chemistry and HACS electrochemistry · 2026Article
- Anions and citrate inhibit LsAA9A, a lytic polysaccharide monooxygenase (LPMO).The FEBS journal · 2025Article
- Structure-Function Analysis of an Understudied Type of LPMO with Unique Redox Properties and Substrate Specificity.ACS catalysis · 2025Article
- Capturing the Binuclear Copper State of Peptidylglycine Monooxygenase Using a Peptidyl-Homocysteine Lure.Journal of the American Chemical Society · 2024Article
- Direct Methane Oxidation by Copper- and Iron-Dependent Methane Monooxygenases.Chemical reviews · 2024Review
- Calcium-binding site in AA10 LPMO fromQRB discovery · 2024Article
- Comparison of simultaneous saccharification and fermentation with LPMO-supported hybrid hydrolysis and fermentation.Frontiers in bioengineering and biotechnology · 2024Article
- A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases.Nature communications · 2023Article
- Fenton-like Chemistry by a Copper(I) Complex and HJournal of the American Chemical Society · 2023Article
- Revisiting the role of electron donors in lytic polysaccharide monooxygenase biochemistry.Essays in biochemistry · 2023Review
- New structures reveal flexible dynamics between the subdomains of peptidylglycine monooxygenase. Implications for an open to closed mechanism.Protein science : a publication of the Protein Society · 2023Article
- Molecular Mechanism of Substrate Oxidation in Lytic Polysaccharide Monooxygenases: Insight from Theoretical Investigations.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Review
- A fast, sensitive and fluorescent LPMO activity assay.Frontiers in microbiology · 2023Article
- Sequence-Activity Relationship of ATCUN Peptides in the Context of Alzheimer's Disease.Molecules (Basel, Switzerland) · 2022Article
- Knowing friend from foe.eLife · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lytic polysaccharide monooxygenases (LPMOs) are mononuclear copper enzymes that catalyse the oxidative cleavage of glycosidic bonds. They are characterised by two histidine residues that coordinate copper in a configuration termed the Cu-histidine brace. Although first identified in bacteria and fungi, LPMOs have since been found in all biological kingdoms. LPMOs are now included in commercial enzyme cocktails used in industrial biorefineries. This has led to increased process yield due to the synergistic action of LPMOs with glycoside hydrolases. However, the introduction of LPMOs makes control of the enzymatic step in industrial stirred-tank reactors more challenging, and the operational stability of the enzymes is reduced. It is clear that much is still to be learned about the interaction between LPMOs and their complex natural and industrial environments, and fundamental scientific studies are required towards this end. Several atomic-resolution structures have been solved providing detailed information on the Cu-coordination sphere and the interaction with the polysaccharide substrate. However, the molecular mechanisms of LPMOs are still the subject of intense investigation; the key question being how the proteinaceous environment controls the copper cofactor towards the activation of the O-O bond in O2 and cleavage of the glycosidic bonds in polysaccharides. The need for biochemical characterisation of each putative LPMO is discussed based on recent reports showing that not all proteins with a Cu-histidine brace are enzymes.
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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.