Change search
ReferencesLink to record
Permanent link

Direct link
Cellobiose dehydrogenase - A flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi
Show others and affiliations
2006 (English)In: Current protein and peptide science, ISSN 1389-2037, Vol. 7, no 3, 255-280 p.Article, review/survey (Refereed) Published
Abstract [en]

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 basidiomycetcs 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 I 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.

Place, publisher, year, edition, pages
2006. Vol. 7, no 3, 255-280 p.
Keyword [en]
cellobiose dehydrogenase, flavocytochrome, wood degrading fungi, GMC flavoenzyme superfamily, basidiomycete phanerochaete-chrysosporium, white-rot fungi, electron-transfer, quinone oxidoreductase, trametes-versicolor, sporotrichum-pulverulentum, coniophora-puteana, humicola-insolens, crystal-structure, glucose-oxidase
URN: urn:nbn:se:kth:diva-15742ISI: 000238251100007ScopusID: 2-s2.0-33745090845OAI: diva2:333784
QC 20100525Available from: 2010-08-05 Created: 2010-08-05Bibliographically approved

Open Access in DiVA

No full text


Search in DiVA

By author/editor
Divne, Christina
By organisation
In the same journal
Current protein and peptide science

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Total: 106 hits
ReferencesLink to record
Permanent link

Direct link