EC Number   |
General Information |
Reference |
|---|
    1.1.99.18 | evolution |
a phylogenetic tree using basidiomycetes and ascomycetes CDH sequences shows that the CDH from Termitomyces clypeatus, which is classified as a basidiomycetes fungus, is clustered with the ascomycetes group |
762937 |
| 1.1.99.18 | malfunction |
the three CDH genes of Podospora anserina are inactivated, resulting in single and multiple CDH mutants. Almost no difference is detected in growth and fertility of the mutants on various lignocellulose sources, except on crystalline cellulose, on which a 2fold decrease in fertility of the mutants lacking Podospora anserina CDH1 (PaCDH1) and PaCDH2 is observed. A striking difference between wild-type and mutant secretomes is observed. The secretome of the mutant lacking all CDHs contains five beta-glucosidases, whereas the wild type had only one. Podospora anserina seems to compensate for the lack of CDH with secretion of beta-glucosidases |
762637 |
| 1.1.99.18 | metabolism |
the cellobiose dehydrogenase IIA (CDHI) variant is comprised of a cytochrome domain (CYT), a dehydrogenase domain (DH), and a carbohydrate-binding module (CBM) that are connected by two flexible linkers. Upon cellobiose oxidation at the DH, intramolecular electron transfer (IaET) occurs from the DH to the CYT. In vivo, CDHIIA CYT subsequently performs intermolecular electron transfer (IeET) to a lytic polysaccharide monooxygenase (LPMO) |
762761 |
| 1.1.99.18 | metabolism |
the enzyme enables Podospora anserina to consume crystalline cellulose. It seems to play a minor role on actual substrates |
762637 |
| 1.1.99.18 | metabolism |
the interaction of cellobiose dehydrogenase (CDH) and beta-GLU (beta-glucosidase) determines the conversion of cellobiose to cellobionolactone or glucose. The formation of cellobionolactone from cellobiose as a result of the action of CDH depends on the availability of quinones (for CDH), which are formed by the interaction of laccase with a phenolic compound. At low quinone concentrations, cellobiose is transformed by beta-GLU to glucose |
-, 763210 |
| 1.1.99.18 | physiological function |
cellobiose dehydrogenase enhances cellulose degradation by coupling the oxidation of cellobiose to the reductive activation of copper-dependent polysaccharide monooxygenase, EC 1.14.99.54, that catalyzes the insertion of oxygen into C-H bonds adjacent to the glycosidic linkage. In a Cdh-1 deletion strain, cellobiose dehydrogenase activity in the secretome is 800fold lower than in the wild-type secretome. Cellulase activity of the deletion strain secretome is 37-49% lower than that of wild-type |
-, 739773 |
| 1.1.99.18 | physiological function |
comparison of the binding isotherm to cellulose of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium with that of cellobiohydrolase 1 (CBH 1) from Trichoderma reesei. The binding of both enzymes decreases in the presence of ethylene glycol, increases in the presence of ammonium sulfate and is unaffected by sodium chloride |
741843 |
| 1.1.99.18 | physiological function |
lytic polysaccharide monooxygenases (LPMOs) are ubiquitous oxidoreductases, facilitating the degradation of polymeric carbohydrates in biomass. Cellobiose dehydrogenase (CDH) is a biologically relevant electron donor in this process, with the electrons resulting from cellobiose oxidation being shuttled from the CDH dehydrogenase domain to its cytochrome domain and then to the LPMO catalytic site. The main interaction surface on LPMO is located around the Cu(II) center |
-, 762733 |
| 1.1.99.18 | physiological function |
protein conformational change is essential for reductive activation of lytic polysaccharide monooxygenase by cellobiose dehydrogenase |
762531 |
| 1.1.99.18 | physiological function |
the enzyme has oxidative antimicrobial activity by producing hydrogen peroxide |
740202 |
