Cellobiose dehydrogenase formation by filamentous fungus Chaetomium sp. INBI 2-26(−)

Vasil'chenko, L. G.; Khromonygina, V. V.; Karapetyan, K.N.; Vasilenko, O. V.; Rabinovich, M. A.

doi:10.1016/j.jbiotec.2005.03.023

Cited by 16 publications

(21 citation statements)

References 51 publications

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“…Thus, during the reductive halfreaction, there will be a flow of electrons from the catalytic centre to the haem domain. Such a flow is observed for class-I CDHs only below pH 6, but for some class-II CDHs also under neutral or slightly alkaline conditions [37,40,73]. The experimentally determined redox potential [56] of F ox /F red of the isolated flavin domain decreases with the increase in pH from 106 mV (pH 3.0) to -132 mV (pH 7.0).…”

Section: Interdomain Electron Transfermentioning

confidence: 88%

“…The fact that monosaccharides are poor or no substrates for CDH is attributed to the presence of various modes of non-productive binding in the two binding sites. However, in this case one should expect strong inhibition of CDH by monosaccharides, which is not confirmed [40,50,66].…”

Section: Catalytic Mechanism Of the Reductive Half-reactionmentioning

confidence: 90%

“…Two different forms of this thermostable CDH detected under various growth conditions are probably due to posttranslational modifications of a single transcript. CDH was purified and characterised also from the asporogenic filamentous fungus INBI 2-26(-) [40] belonging to the genus of Chaetomium. This enzyme with a molecular weight of 95 kDa possessed a rather high pH optimum between 5.5 -7.0, and a characteristic absorption spectrum.…”

Section: Production Of Cdh In Ascomycetesmentioning

confidence: 99%

“…At [40,66] any given pH, the FAD of P. chrysosporium CDH is more reductive than the haem. Thus, during the reductive halfreaction, there will be a flow of electrons from the catalytic centre to the haem domain.…”

Section: Interdomain Electron Transfermentioning

confidence: 99%

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Cellobiose Dehydrogenase – A Flavocytochrome from Wood-Degrading, Phytopathogenic and Saprotropic Fungi

Zámocký¹,

Ludwig

Peterbauer

et al. 2006

CPPS

221

230

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Cellobiose dehydrogenase, the only currently known extracellular flavocytochrome, is formed not only by a number of wood-degrading but also by various phytopathogenic fungi. This inducible enzyme participates in early events of lignocellulose degradation, as investigated in several basidiomycete fungi at the transcriptional and translational level. However, its role in the ascomycete fungi is not yet obvious. Comprehensive sequence analysis of CDH-encoding genes and their translational products reveals significant sequence similarities along the entire sequences and also a common domain architecture. All known cellobiose dehydrogenases fall into two related subgroups. Class-I members are represented by sequences from basidiomycetes whereas class-II comprises longer, more complex sequences from ascomycete fungi. Cellobiose dehydrogenase is typically a monomeric protein consisting of two domains joined by a protease-sensitive linker region. Each larger (dehydrogenase) domain is flavin-associated while the smaller (cytochrome) domains are haem-binding. The latter shorter domains are unique sequence motifs for all currently known flavocytochromes. Each cytochrome domain of CDH can bind a single haem b as prosthetic group. The larger dehydrogenase domain belongs to the glucose-methanol-choline (GMC) oxidoreductase superfamily - a widespread flavoprotein evolutionary line. The larger domains can be further divided into a flavin-binding subdomain and a substrate-binding subdomain. In addition, the class-II (but not class-I) proteins can possess a short cellulose-binding module of type 1 at their C-termini. All the cellobiose dehydrogenases oxidise cellobiose, cellodextrins, and lactose to the corresponding lactones using a wide spectrum of different electron acceptors. Their flexible specificity serves as a base for the development of possible biotechnological applications.

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Section: Interdomain Electron Transfermentioning

confidence: 88%

Section: Catalytic Mechanism Of the Reductive Half-reactionmentioning

confidence: 90%

Section: Production Of Cdh In Ascomycetesmentioning

confidence: 99%

Section: Interdomain Electron Transfermentioning

confidence: 99%

See 2 more Smart Citations

Cellobiose Dehydrogenase – A Flavocytochrome from Wood-Degrading, Phytopathogenic and Saprotropic Fungi

Zámocký¹,

Ludwig

Peterbauer

et al. 2006

CPPS

221

230

View full text Add to dashboard Cite

show abstract

“…CDH activity was reported in cultures of the ascomycetes Thielavia heterothallica (synonyms, Myceliophthora thermophila and Sporotrichum thermophile) (3,4), Chaetomium sp. INBI 2-26(Ϫ) (38), Chaetomium cellulolyticum (10), Neurospora crassa (11), Humicola insolens (32), and Myriococcum thermophilum (14). While some of these enzymes were characterized biochemically to various extents, only the cdh genes from Sporotrichum thermophile (34), H. insolens (40), and Myriococcum thermophilum (44) were cloned.…”

mentioning

confidence: 99%

Catalytic Properties and Classification of Cellobiose Dehydrogenases from Ascomycetes

Harreither

Sygmund

Augustin

et al. 2011

Appl Environ Microbiol

131

102

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Putative cellobiose dehydrogenase (CDH) genes are frequently discovered in various fungi by genome sequencing projects. The expression of CDH, an extracellular flavocytochrome, is well studied in white rot basidiomycetes and is attributed to extracellular lignocellulose degradation. CDH has also been reported for plant-pathogenic or saprotrophic ascomycetes, but the molecular and catalytic properties of these enzymes are currently less investigated. This study links various ascomycetous cdh genes with the molecular and catalytic characteristics of the mature proteins and suggests a differentiation of ascomycete class II CDHs into two subclasses, namely, class IIA and class IIB, in addition to the recently introduced class III of hypothetical ascomycete CDHs. This new classification is based on sequence and biochemical data obtained from sequenced fungal genomes and a screening of 40 ascomycetes. Thirteen strains showed CDH activity when they were grown on cellulose-based media, and Chaetomium atrobrunneum, Corynascus thermophilus, Dichomera saubinetii, Hypoxylon haematostroma, Neurospora crassa, and Stachybotrys bisbyi were selected for detailed studies. In these strains, one or two cdh-encoding genes were found that stem either from class IIA and contain a C-terminal carbohydrate-binding module or from class IIB without such a module. In several strains, both genes were found. Regarding substrate specificity, class IIB CDHs show a less pronounced substrate specificity for cellobiose than class IIA enzymes. A pH-dependent pattern of the intramolecular electron transfer was also observed, and the CDHs were classified into three groups featuring acidic, intermediate, or alkaline pH optima. The pH optimum, however, does not correlate with the CDH subclasses and is most likely a species-dependent adaptation to different habitats.

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Application of cellulose‐based self‐assembled tri‐enzyme system in a pseudo‐reagent‐less biosensor for biogenic catecholamine detection

Rabinovich

Vasil'chenko

Karapetyan

et al. 2007

Biotechnology Journal

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Amorphous cellulose was used as a specific carrier for the deposition of self-assembled multienzyme complexes capable of catalyzing coupled reactions. Naturally glycosylated fungal cellobiohydrolases (CBHs) of glycosyl hydrolase families 6 and 7 were specifically deposited onto the cellulose surface through their family I cellulose-binding modules (CBM). Naturally glycosylated fungal laccase was then deposited onto the preformed glycoprotein layer pretreated by ConA, through the interaction of mannosyl moieties of fungal glycoproteins with the multivalent lectin. The formation of a cellulase-ConA-laccase composite was proven by direct and indirect determination of activity of immobilized laccase. In the absence of cellulases and ConA, no laccase deposition onto the cellulose surface was observed. Finally, basidiomycetous cellobiose dehydrogenase (CDH) was deposited onto the cellulose surface through the specific interaction of its FAD domain with cellulose. The obtained paste was applied onto the surface of a Clark-type oxygen electrode and covered with a dialysis membrane. In the presence of traces of catechol or dopamine as mediators, the obtained immobilized multienzyme composite was capable of the coupled oxidation of cellulose by dissolved oxygen, thus providing the basis for a sensitive assay of the mediator. Swollen amorphous cellulose plays three different roles in the obtained biosensor as: (i) a gelforming matrix that captures the analyte and its oxidized intermediate, (ii) a specific carrier for protein self-assembly, and (iii) a source of excess substrate for a pseudo-reagent-less assay with signal amplification. The detection limit of such a tri-enzyme biosensor is 50-100 nM dopamine.

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Cellobiose dehydrogenase formation by filamentous fungus Chaetomium sp. INBI 2-26(−)

Cited by 16 publications

References 51 publications

Cellobiose Dehydrogenase – A Flavocytochrome from Wood-Degrading, Phytopathogenic and Saprotropic Fungi

Cellobiose Dehydrogenase – A Flavocytochrome from Wood-Degrading, Phytopathogenic and Saprotropic Fungi

Catalytic Properties and Classification of Cellobiose Dehydrogenases from Ascomycetes

Application of cellulose‐based self‐assembled tri‐enzyme system in a pseudo‐reagent‐less biosensor for biogenic catecholamine detection

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