Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of <i>Phanerochaete chrysosporium</i>

Habu, Naoto; Samejima, Masahiro; Dean, Jeffrey F. D.; Eriksson, Karl–Erik L.

doi:10.1016/0014-5793(93)80162-n

Cited by 55 publications

(34 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…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). CBQ carries the catalytic site and reduces cellobiose efficiently.…”

mentioning

confidence: 99%

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

Baminger

Subramaniam

Renganathan

et al. 2001

Appl Environ Microbiol

121

108

View full text Add to dashboard Cite

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.

show abstract

mentioning

confidence: 99%

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

Baminger

Subramaniam

Renganathan

et al. 2001

Appl Environ Microbiol

121

108

View full text Add to dashboard Cite

show abstract

“…It was formerly known as cellobiose oxidase (CBO, EC 1.1.3.25), but Fe(III)-containing compounds and quinones were found to have much higher affinity for this enzyme than does molecular oxygen (6, 7) so CBO was recently renamed CDH (8). Recent investigations have also demonstrated that another cellobiose-oxidizing flavoprotein, cellobiose:quinone oxidoreductase (CBQ, EC 1.1.5.1) (9,10), is the flavincontaining domain of CDH produced by proteolytic activity (11)(12)(13). In addition to their catalytic function, both CDH and CBQ can bind to cellulose as well as many cellulases (11,14).…”

mentioning

confidence: 99%

Cellobiose Dehydrogenase from the Fungi Phanerochaete chrysosporium and Humicola insolens

Igarashi¹,

Verhagen²,

Samejima³

et al. 1999

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Cellobiose dehydrogenases (CDH) were purified from cellulose-grown cultures of the fungi Phanerochaete chrysosporium and Humicola insolens. The pH optimum of the cellobiose-cytochrome c oxidoreductase activity of P. chrysosporium CDH was acidic, whereas that of H. insolens CDH was neutral. The absorption spectra of the two CDHs showed them to be typical hemoproteins, but there was a small difference in the visible region. Limited proteolysis between the heme and flavin domains was performed to investigate the cofactors. There was no difference in absorption spectrum between the heme domains of P. chrysosporium and H. insolens CDHs. The midpoint potentials of heme at pH 7.0 were almost identical, and no difference in pH dependence was observed over the range of pH 3-9. The pH dependence of cellobiose oxidation by the flavin domains was similar to that of the native CDHs, indicating that the difference in the pH dependence of the catalytic activity between the two CDHs is because of the flavin domains. The absorption spectrum of the flavin domain from H. insolens CDH has absorbance maxima at 343 and 426 and a broad absorption peak at 660 nm, whereas that of P. chrysosporium CDH showed a normal flavoprotein spectrum. Flavin cofactors were extracted from the flavin domains and analyzed by high-performance liquid chromatography. The flavin cofactor from H. insolens was found to be a mixture of 60% 6-hydroxy-FAD and 40% FAD, whereas that from P. chrysosporium CDH was normal FAD. After reconstitution of the deflavo-proteins it was found that flavin domains containing 6-hydroxy-FAD were clearly active but their cellobiose oxidation rates were lower than those of flavin domains containing normal FAD. Reconstitution of flavin cofactor had no effect on the optimum pH. From these results, it is concluded that the pH dependence is not because of the flavin cofactor but is because of the protein molecule.

show abstract

“…Sorbitol dehydrogenase and other dehydrogenase detected in present study may be associated with the oxidative degradation of cellulose as proposed [36] in P. chrysosporium. The production of proteases during lignocellulose degradation has been widely reported and their expression has been correlated with the activation of cellulase activity in Sporotrichum pulverulentum [47] and CDH functional domain cleavage in P. chrysosporium [48].…”

Section: Accepted Manuscriptmentioning

confidence: 99%

Differential production of lignocellulolytic enzymes by a white rot fungus Termitomyces sp. OE147 on cellulose and lactose

Bashir

Gangwar

Mishra

2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

View full text Add to dashboard Cite

Release of the FAD domain from cellobiose oxidase by proteases from cellulolytic cultures of Phanerochaete chrysosporium

Cited by 55 publications

References 14 publications

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

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

Cellobiose Dehydrogenase from the Fungi Phanerochaete chrysosporium and Humicola insolens

Differential production of lignocellulolytic enzymes by a white rot fungus Termitomyces sp. OE147 on cellulose and lactose

Contact Info

Product

Resources

About