ArticleBiotechnology for biofuels2019
The GMC superfamily of oxidoreductases revisited: analysis and evolution of fungal GMC oxidoreductases.
Article in Biotechnology for biofuels, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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71 citing papers in PubMed, 163 citations in OpenAlex.
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- Structural insights into cellobiose dehydrogenases of a non-lignocellulolytic fungus and their transcriptional dynamics across different nutritional modes.Microbiology spectrum · 2026Article
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- Interaction of class III cellobiose dehydrogenase with lytic polysaccharide monooxygenase.FEBS open bio · 2025Article
- C3 Compound Metabolism in the Thermoacidophilic Methanotroph Methylacidiphilum fumariolicum SolV.Environmental microbiology reports · 2025Article
- Chromosome-Level Genome Announcement of the MonokaryoticJournal of fungi (Basel, Switzerland) · 2025Article
- Shifting the substrate scope of dimeric pyranose oxidase from monosaccharide to glycoside preference through oligomeric state modification.The FEBS journal · 2025Article
- MftG is crucial for ethanol metabolism of mycobacteria by linking mycofactocin oxidation to respiration.eLife · 2025Article
- Acidification-based mineral weathering mechanism involves a glucose/methanol/choline oxidoreductase inApplied and environmental microbiology · 2024Article
- Oestrogen Detoxification Ability of White Rot FungusJournal of fungi (Basel, Switzerland) · 2024Article
- Identification of a robust bacterial pyranose oxidase that displays an unusual pH dependence.The Journal of biological chemistry · 2024Article
- Genomic Functional Analysis of Novel Radiation-Resistant Species ofMicroorganisms · 2024Article
- Exploring class III cellobiose dehydrogenase: sequence analysis and optimized recombinant expression.Microbial cell factories · 2024Article
- Comparative secretome analysis of Striga and Cuscuta species identifies candidate virulence factors for two evolutionarily independent parasitic plant lineages.BMC plant biology · 2024Article
11 more citing papers are in PubMed but not listed here.
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5 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundThe glucose-methanol-choline (GMC) superfamily is a large and functionally diverse family of oxidoreductases that share a common structural fold. Fungal members of this superfamily that are characterised and relevant for lignocellulose degradation include aryl-alcohol oxidoreductase, alcohol oxidase, cellobiose dehydrogenase, glucose oxidase, glucose dehydrogenase, pyranose dehydrogenase, and pyranose oxidase, which together form family AA3 of the auxiliary activities in the CAZy database of carbohydrate-active enzymes. Overall, little is known about the extant sequence space of these GMC oxidoreductases and their phylogenetic relations. Although some individual forms are well characterised, it is still unclear how they compare in respect of the complete enzyme class and, therefore, also how generalizable are their characteristics.
resultsTo improve the understanding of the GMC superfamily as a whole, we used sequence similarity networks to cluster large numbers of fungal GMC sequences and annotate them according to functionality. Subsequently, different members of the GMC superfamily were analysed in detail with regard to their sequences and phylogeny. This allowed us to define the currently characterised sequence space and show that complete clades of some enzymes have not been studied in any detail to date. Finally, we interpret our results from an evolutionary perspective, where we could show, for example, that pyranose dehydrogenase evolved from aryl-alcohol oxidoreductase after a change in substrate specificity and that the cytochrome domain of cellobiose dehydrogenase was regularly lost during evolution.
conclusionsThis study offers new insights into the sequence variation and phylogenetic relationships of fungal GMC/AA3 sequences. Certain clades of these GMC enzymes identified in our phylogenetic analyses are completely uncharacterised to date, and might include enzyme activities of varying specificities and/or activities that are hitherto unstudied.
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