ArticlePloS one2015
Characterization of a novel PQQ-dependent quinohemoprotein pyranose dehydrogenase from Coprinopsis cinerea classified into auxiliary activities family 12 in carbohydrate-active enzymes.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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22 citing papers in PubMed, 50 citations in OpenAlex.
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- Transcriptomic analysis and carbohydrate metabolism-related enzyme expression across different pH values inFrontiers in microbiology · 2024Article
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- Enzymatic properties of alcohol dehydrogenase PedE_M.s. derived fromFrontiers in microbiology · 2023Article
- Hyperaccumulation of Gadolinium byFrontiers in microbiology · 2022Article
- Pyrroloquinoline-Quinone Is More Than an Antioxidant: A Vitamin-like Accessory Factor Important in Health and Disease Prevention.Biomolecules · 2021Review
- Increased abundance of secreted hydrolytic enzymes and secondary metabolite gene clusters define the genomes of latent plant pathogens in the Botryosphaeriaceae.BMC genomics · 2021Article
- Amperometric Biosensors Based on Direct Electron Transfer Enzymes.Molecules (Basel, Switzerland) · 2021Review
- Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function.The Journal of biological chemistry · 2020Article
- RNA-seq Profiling Showed Divergent Carbohydrate-Active Enzymes (CAZymes) Expression Patterns inFrontiers in microbiology · 2020Article
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- Crystal Structure of the Catalytic and CytochromeApplied and environmental microbiology · 2019Article
- Comparison of three seemingly similar lytic polysaccharide monooxygenases fromThe Journal of biological chemistry · 2019Article
- Direct Electron Transfer of Enzymes Facilitated by Cytochromes.ChemElectroChem · 2019Review
- Oxidoreductases and Reactive Oxygen Species in Conversion of Lignocellulosic Biomass.Microbiology and molecular biology reviews : MMBR · 2018Review
- The Pyrroloquinoline-Quinone-Dependent Pyranose Dehydrogenase from Coprinopsis cinerea Drives Lytic Polysaccharide Monooxygenase Action.Applied and environmental microbiology · 2018Article
- Oxygen Activation by Cu LPMOs in Recalcitrant Carbohydrate Polysaccharide Conversion to Monomer Sugars.Chemical reviews · 2018Review
- Multiplicity of enzymatic functions in the CAZy AA3 family.Applied microbiology and biotechnology · 2018Review
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8 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The basidiomycete Coprinopsis cinerea contains a quinohemoprotein (CcPDH named as CcSDH in our previous paper), which is a new type of pyrroloquinoline-quinone (PQQ)-dependent pyranose dehydrogenase and is the first found among all eukaryotes. This enzyme has a three-domain structure consisting of an N-terminal heme b containing a cytochrome domain that is homologous to the cytochrome domain of cellobiose dehydrogenase (CDH; EC 1.1.99.18) from the wood-rotting basidiomycete Phanerochaete chrysosporium, a C-terminal family 1-type carbohydrate-binding module, and a novel central catalytic domain containing PQQ as a cofactor. Here, we describe the biochemical and electrochemical characterization of recombinant CcPDH. UV-vis and resonance Raman spectroscopic studies clearly reveal characteristics of a 6-coordinated low-spin heme b in both the ferric and ferrous states, as well as intramolecular electron transfer from the PQQ to heme b. Moreover, the formal potential of the heme was evaluated to be 130 mV vs. NHE by cyclic voltammetry. These results indicate that the cytochrome domain of CcPDH possesses similar biophysical properties to that in CDH. A comparison of the conformations of monosaccharides as substrates and the associated catalytic efficiency (kcat/Km) of CcPDH indicates that the enzyme prefers monosaccharides with equatorial C-2, C-3 hydroxyl groups and an axial C-4 hydroxyl group in the 1C4 chair conformation. Furthermore, a binding study shows a high binding affinity of CcPDH for cellulose, suggesting that CcPDH function is related to the enzymatic degradation of plant cell wall.
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