Cloning and Characterization of a Thermostable Cellobiose Dehydrogenase fromSporotrichum thermophile

Subramaniam, Sai S.; Nagalla, Srinivasa R.; Renganathan, V.

doi:10.1006/abbi.1999.1152

Cited by 57 publications

(34 citation statements)

References 42 publications

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“…To date, all investigated CDHs have been reported to bind specifically to cellulose. For some CDHs, the cellulose-binding ability is attributed to a divergent carbohydrate-binding module (143), whereas other types of CDHs, with no cellulose-binding domain at all, bind to the cellulose surface through the FAD-binding domain (144).…”

Section: -5-␦-lactones (134)mentioning

confidence: 99%

Genomics Review of Holocellulose Deconstruction by Aspergilli

Segato

Damásio

Lucas

et al. 2014

Microbiol Mol Biol Rev

115

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SUMMARY Biomass is constructed of dense recalcitrant polymeric materials: proteins, lignin, and holocellulose, a fraction constituting fibrous cellulose wrapped in hemicellulose-pectin. Bacteria and fungi are abundant in soil and forest floors, actively recycling biomass mainly by extracting sugars from holocellulose degradation. Here we review the genome-wide contents of seven Aspergillus species and unravel hundreds of gene models encoding holocellulose-degrading enzymes. Numerous apparent gene duplications followed functional evolution, grouping similar genes into smaller coherent functional families according to specialized structural features, domain organization, biochemical activity, and genus genome distribution. Aspergilli contain about 37 cellulase gene models, clustered in two mechanistic categories: 27 hydrolyze and 10 oxidize glycosidic bonds. Within the oxidative enzymes, we found two cellobiose dehydrogenases that produce oxygen radicals utilized by eight lytic polysaccharide monooxygenases that oxidize glycosidic linkages, breaking crystalline cellulose chains and making them accessible to hydrolytic enzymes. Among the hydrolases, six cellobiohydrolases with a tunnel-like structural fold embrace single crystalline cellulose chains and cooperate at nonreducing or reducing end termini, splitting off cellobiose. Five endoglucanases group into four structural families and interact randomly and internally with cellulose through an open cleft catalytic domain, and finally, seven extracellular β-glucosidases cleave cellobiose and related oligomers into glucose. Aspergilli contain, on average, 30 hemicellulase and 7 accessory gene models, distributed among 9 distinct functional categories: the backbone-attacking enzymes xylanase, mannosidase, arabinase, and xyloglucanase, the short-side-chain-removing enzymes xylan α-1,2-glucuronidase, arabinofuranosidase, and xylosidase, and the accessory enzymes acetyl xylan and feruloyl esterases.

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Section: -5-␦-lactones (134)mentioning

confidence: 99%

Genomics Review of Holocellulose Deconstruction by Aspergilli

Segato

Damásio

Lucas

et al. 2014

Microbiol Mol Biol Rev

115

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“…Partial proteolysis of CDH was performed as previously reported (11,52). CDH was incubated with papain (Sigma) for about 2 h, and the cyt c activity was monitored.…”

Section: Vol 67 2001 Cellobiose Dehydrogenase From S Rolfsiimentioning

confidence: 99%

“…The probe used for hybridization was a 32 P-labeled 1.2-kb DNA fragment of the C-terminal domain of P. chrysosporium CDH (35) or the complete 2.8-kb DNA of Sporotrichum thermophile CDH (52).…”

Section: Vol 67 2001 Cellobiose Dehydrogenase From S Rolfsiimentioning

confidence: 99%

“…Cellobiose dehydrogenase has been isolated and characterized from a variety of white-rot fungi (2,6,21,38,43,53), soft-rot fungi (13,15,20,50,52), and one brown-rot fungus (49). Typically, CDH is a monomeric protein consisting of two domains, one containing a hexacoordinate heme b (14) and one containing a noncovalently bound flavin adenine dinucleotide (FAD) (6,43) or 6-hydroxy FAD (33).…”

mentioning

confidence: 99%

“…Typically, CDH is a monomeric protein consisting of two domains, one containing a hexacoordinate heme b (14) and one containing a noncovalently bound flavin adenine dinucleotide (FAD) (6,43) or 6-hydroxy FAD (33). These two domains are linked by a protease-sensitive region (17,35,39,52). Limited proteolytic cleavage of CDH leads to an inactive heme peptide and an active FAD domain, which has been termed cellobiose:quinone 1-oxidoreductase (CBQ; EC 1.5.1.1) (24,54).…”

mentioning

confidence: 99%

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Purification and Characterization of Cellobiose Dehydrogenase from the Plant PathogenSclerotium(Athelia)rolfsii

Baminger

Subramaniam

Renganathan

et al. 2001

Appl Environ Microbiol

122

108

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Cellobiose dehydrogenase (CDH) is an extracellular hemoflavoenzyme produced by several wood-degrading fungi. In the presence of a suitable electron acceptor, e.g., 2,6-dichloro-indophenol (DCIP), cytochrome c, or metal ions, CDH oxidizes cellobiose to cellobionolactone. The phytopathogenic fungus Sclerotium rolfsii (teleomorph: Athelia rolfsii) strain CBS 191.62 produces remarkably high levels of CDH activity when grown on a cellulose-containing medium. Of the 7,500 U of extracellular enzyme activity formed per liter, less than 10% can be attributed to the proteolytic product cellobiose:quinone oxidoreductase. As with CDH from wood-rotting fungi, the intact, monomeric enzyme from S. rolfsii contains one heme b and one flavin adenine dinucleotide cofactor per molecule. It has a molecular size of 101 kDa, of which 15% is glycosylation, and a pI value of 4.2. The preferred substrates are cellobiose and cellooligosaccharides; additionally, ␤-lactose, thiocellobiose, and xylobiose are efficiently oxidized. Cytochrome c (equine) and the azino-di-(3-ethyl-benzthiazolin-6-sulfonic acid) cation radical were the best electron acceptors, while DCIP, 1,4-benzoquinone, phenothiazine dyes such as methylene blue, phenoxazine dyes such as Meldola's blue, and ferricyanide were also excellent acceptors. In addition, electrons can be transferred to oxygen. Limited in vitro proteolysis with papain resulted in the formation of several protein fragments that are active with DCIP but not with cytochrome c. Such a flavin-containing fragment, with a mass of 75 kDa and a pI of 5.1 and lacking the heme domain, was isolated and partially characterized.

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Cellobiose dehydrogenase of Chaetomium sp. INBI 2‐26(–): Structural basis of enhanced activity toward glucose at neutral pH

Vasil'chenko

Karapetyan

Yershevich

et al. 2011

Biotechnology Journal

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Cellobiose dehydrogenase (CDH) is an extracellular fungal flavocytochrome specifically oxidizing cellooligosaccharides and lactose to corresponding (-lactones by a variety of electron acceptors. In contrast to basidiomycetous CDHs, CDHs of ascomycetes also display certain activity toward glucose. The objective of this study was to establish the structural reasons of such an activity of CDH from mesophilic ascomycete Chaetomium sp. INBI 2-26 (ChCDH). The complete amino acid sequence of ChCDH displayed high levels of similarity with the amino acid sequences of CDHs from the thermophilic fungi Thielavia heterotallica and Myriococcum thermophilum. Peptide mass fingerprinting of purified ChCDH provided evidence for the oxidation of methionine residues in the FAD-domain. Comparative homology modeling of the structure of the ChCDH FAD-domain in complex with the transition state analog based on the structure of the same complex of basidiomycetous CDH (1NAA) as template indicated possible structural reasons for the enhanced activity of ascomycetous CDHs toward glucose at neutral pH, which is a prerequisite for application of CDH in a variety of biocompatible biosensors and biofuel cells.

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Cloning and Characterization of a Thermostable Cellobiose Dehydrogenase fromSporotrichum thermophile

Cited by 57 publications

References 42 publications

Genomics Review of Holocellulose Deconstruction by Aspergilli

Genomics Review of Holocellulose Deconstruction by Aspergilli

Purification and Characterization of Cellobiose Dehydrogenase from the Plant PathogenSclerotium(Athelia)rolfsii

Cellobiose dehydrogenase of Chaetomium sp. INBI 2‐26(–): Structural basis of enhanced activity toward glucose at neutral pH

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