ReviewComputational and structural biotechnology journal2012
A structural overview of GH61 proteins - fungal cellulose degrading polysaccharide monooxygenases.
Review in Computational and structural biotechnology journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 42 citations in OpenAlex.
- Secreted Glycoside Hydrolase BcGH61 From Botrytis cinerea Induces Cell Death by the Apoplastic Location and Triggers Intracellular Immune Perception.Molecular plant pathology · 2026Article
- Insights into an unusual Auxiliary Activity 9 family member lacking the histidine brace motif of lytic polysaccharide monooxygenases.The Journal of biological chemistry · 2019Article
- An AA9-LPMO containing a CBM1 domain in Aspergillus nidulans is active on cellulose and cleaves cello-oligosaccharides.AMB Express · 2018Article
- Structural studies of the unusual metal-ion site of the GH124 endoglucanase from Ruminiclostridium thermocellum.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Lytic polysaccharide monooxygenases disrupt the cellulose fibers structure.Scientific reports · 2017Article
- Article
- Lytic polysaccharide monooxygenases: a crystallographer's view on a new class of biomass-degrading enzymes.IUCrJ · 2016Review
- Bioinformatic characterization of type-specific sequence and structural features in auxiliary activity family 9 proteins.Biotechnology for biofuels · 2016Article
- Crystal Structure and Substrate Recognition of Cellobionic Acid Phosphorylase, Which Plays a Key Role in Oxidative Cellulose Degradation by Microbes.The Journal of biological chemistry · 2015Article
- Classification of fungal and bacterial lytic polysaccharide monooxygenases.BMC genomics · 2015Article
- Fungal cellulose degradation by oxidative enzymes: from dysfunctional GH61 family to powerful lytic polysaccharide monooxygenase family.Briefings in functional genomics · 2014Review
- Metabolic engineering of yeasts by heterologous enzyme production for degradation of cellulose and hemicellulose from biomass: a perspective.Frontiers in microbiology · 2014Review
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recent years have witnessed a spurt of activities in the elucidation of the molecular function of a class of proteins with great potential in biomass degradation. GH61 proteins are of fungal origin and were originally classified in family 61 of the glycoside hydrolases. From the beginning they were strongly suspected to be involved in cellulose degradation because of their expression profiles, despite very low detectable endoglucanase activities. A major breakthrough came from structure determination of the first members, establishing the presence of a divalent metal binding site and a similarity to bacterial proteins involved in chitin degradation. A second breakthrough came from the identification of cellulase boosting activity dependent on the integrity of the metal binding site. Finally very recently GH61 proteins were demonstrated to oxidatively cleave crystalline cellulose in a Cu and reductant dependant manner. This mini-review in particular focuses on the contribution that structure elucidation has made in the understanding of GH61 molecular function and reviews the currently known structures and the challenges remaining ahead for exploiting this new class of enzymes to the full.
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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.