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Information on EC 1.1.99.18 - cellobiose dehydrogenase (acceptor) and Organism(s) Phanerodontia chrysosporium and UniProt Accession Q01738
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1.1.99.18 cellobiose dehydrogenase (acceptor)IUBMB Comments
Also acts, more slowly, on cello-oligosaccharides, lactose and D-glucosyl-1,4-beta-D-mannose. The enzyme from the white rot fungus Phanerochaete chrysosporium is unusual in having two redoxin domains, one containing a flavin and the other a protoheme group. It transfers reducing equivalents from cellobiose to two types of redox acceptor: two-electron oxidants, including redox dyes, benzoquinones, and molecular oxygen, and one-electron oxidants, including semiquinone species, iron(II) complexes, and the model acceptor cytochrome c . 2,6-Dichloroindophenol can act as acceptor in vitro.
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Word Map
- 1.1.99.18
- cellulose
- phanerochaete
- chrysosporium
-
biofuels
-
basidiomycete
-
flavocytochrome
- lignocellulose
-
white-rot
- laccase
- pyranose
- corynascus
-
lpmos
-
myriococcum
-
wood-degrading
- trametes
- cellodextrins
- thermophilum
-
ligninolytic
- cello-oligosaccharides
-
cellulose-binding
-
glucose-methanol-choline
-
cellulose-degrading
-
flavodehydrogenase
- analysis
- sporotrichum
- rolfsii
- insolens
-
myrothecium
-
cellulose-grown
- biofuel production
- biotechnology
- industry
- dichlorophenol-indophenol
-
brown-rot
- pycnoporus
-
cellulose-based
- humicola
-
wood-rotting
-
bioanode
- verrucaria
- cellobiohydrolases
- diagnostics
- medicine
- synthesis
- degradation
The taxonomic range for the selected organisms is: Phanerodontia chrysosporium
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
cellobiose dehydrogenase, cdh-1, cellobiose oxidase, mtcdh, cellobiose:quinone oxidoreductase, cdh iib, cdh iia, cdhiia, cellobiose oxidoreductase, cellobiose-quinone oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cdh
-
cellobiose dehydrogenase
-
CBO
-
-
-
-
Cdh
cellobiose dehydrogenase
Cellobiose-quinone oxidoreductase
-
-
-
-
dehydrogenase, cellobiose
-
-
-
-
oxidase, cellobiose
-
-
-
-
Cdh
-
-
-
-
cellobiose dehydrogenase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor
mechanism
-
cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor
mechanism of electron transfer
-
cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor
mechanism: cellobiose rapidly reduces the flavin group, which in turn slowly reduces the cytochrome b moiety, cytochrome b may donate electrons very rapidly to either mammalian cytochrome c or bacterial cytochrome c-551. Reactions are second-order
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
-
-
-
-
oxidation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
cellobiose:acceptor 1-oxidoreductase
Also acts, more slowly, on cello-oligosaccharides, lactose and D-glucosyl-1,4-beta-D-mannose. The enzyme from the white rot fungus Phanerochaete chrysosporium is unusual in having two redoxin domains, one containing a flavin and the other a protoheme group. It transfers reducing equivalents from cellobiose to two types of redox acceptor: two-electron oxidants, including redox dyes, benzoquinones, and molecular oxygen, and one-electron oxidants, including semiquinone species, iron(II) complexes, and the model acceptor cytochrome c [9]. 2,6-Dichloroindophenol can act as acceptor in vitro.
CAS REGISTRY NUMBER
COMMENTARY
54576-85-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
cellobiose + 1,4-benzoquinone
cellobiono-1,5-lactone + reduced 1,4-benzoquinone
-
-
-
?
cellobiose + 2,6-dichloroindophenol
cellobiono-1,5-lactone + reduced 2,6-dichloroindophenol
-
-
-
?
cellobiose + 2,6-dichlorophenol indophenol
cellobiono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
-
-
?
cellobiose + 2,6-dichlorophenolindophenol
cellobiono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
cellobiose + ferricytochrome c
cellobiono-1,5-lactone + ferrocytochrome c
-
-
-
?
cellobiose + ubiquinone
cellobiono-1,5-lactone + reduced ubiquinone
-
-
-
?
D-glucose + 2,6-dichloroindophenol
D-glucono-1,5-lactone + reduced 2,6-dichloroindophenol
-
-
-
?
D-glucose + acceptor
D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
lactose + 2,6-dichloroindophenol
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced 2,6-dichloroindophenol
-
-
-
?
lactose + 2,6-dichloroindophenol
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
?
maltose + acceptor
4-O-(alpha-D-glucopyranosyl)-D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
cellobiose + 2,6-dichlorophenol-indophenol
cellobiono-1,5-lactone + reduced 2,6-dichlorophenol-indophenol
-
-
-
-
?
cellobiose + 2,6-dichlorophenolindophenol
cellobiono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
cellobiose + acceptor
cellobionolactone + reduced acceptor
-
-
-
-
?
cellobiose + benzyl viologen
cellobiono-1,5-lactone + reduced benzyl viologen
-
-
-
-
r
cellobiose + cytochrome c
cellobiono-1,5-lactone + reduced cytochrome c
-
-
-
-
?
cellobiose + Fe3+
cellobiono-1,5-lactone + reduced Fe3+
-
-
-
-
r
cellobiose + ferricyanide
cellobiono-1,5-lactone + ferrocyanide
-
-
-
-
r
cellobiose + Mn(III)-malonate
cellobiono-1,5-lactone + reduced Mn(III)-malonate
-
-
-
-
r
cellobiose + Mn3+-malonate
cellobiono-1,5-lactone + reduced Mn3+-malonate
-
-
-
-
r
cellobiose + triiodide ion
cellobiono-1,5-lactone + reduced triiodide ion
-
-
-
-
r
cellobiose + ubiquinone
cellobiono-1,5-lactone + reduced ubiquinone
-
-
-
-
?
cellopentaose + acceptor
cellopentaono-1,5-lactone + reduced acceptor
-
-
-
?
cellopentaose + ferricytochrome c
cellopentaono-1,5-lactone + ferrocytochrome c
-
-
-
-
?
cellotetraose + ferricytochrome c
cellotetraono-1,5-lactone + ferrocytochrome c
-
-
-
-
?
cellotriose + acceptor
cellotriono-1,5-lactone + reduced acceptor
-
-
-
?
cellotriose + ferricytoferricytochrome c chrome c
cellotriono-1,5-lactone + ferrocytochrome c
-
-
-
-
?
D-glucose + 2,6-dichlorophenolindophenol
D-glucono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
lactose + 2,6-dichlorophenol indophenol
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
lactose + 2,6-dichlorophenolindophenol
lactono-1,5-lactone + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
lactose + 3,5-di-tert-butyl-1,2-benzoquinone
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + ?
-
-
-
-
?
lactose + cytochrome c
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced cytochrome c
lactose + ferricytochrome c
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + ferrocytochrome c
-
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
the enzyme participates in lignocellulose degradation by white-rot fungi with a proposed role in the early events of wood degradation
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
acceptor: cytochrome c
-
-
?
cellobiose + cytochrome c
cellobiono-1,5-lactone + reduced cytochrome c
-
-
-
?
cellobiose + cytochrome c
cellobiono-1,5-lactone + reduced cytochrome c
-
-
-
-
?
lactose + acceptor
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
lactose + acceptor
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced acceptor
-
-
-
-
?
4-beta-glucosylmannose + O2
?
-
50% of the activity with lactose
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
Cytochrome c, 2,6-dichlorophenolindophenol, ferricyanide, 3,5-di-tert-butyl-1,2-benzoquinone, Mn3+-malonate can serve as electron acceptors. O2 is a poor acceptor in the absence of artificial acceptors and is reduced to H2O2. Molecular oxygen acts as two-electron acceptor, superoxide is produced through an iron mediated pathway
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
Cytochrome c, 2,6-dichlorophenolindophenol, ferricyanide, 3,5-di-tert-butyl-1,2-benzoquinone, Mn3+-malonate can serve as electron acceptors. O2 is a poor acceptor in the absence of artificial acceptors and is reduced to H2O2. Molecular oxygen acts as two-electron acceptor, superoxide is produced through an iron mediated pathway
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
reduction of molecular oxygen to hydrogen peroxide, and Fe3+ to Fe2+, cellulose depolymerization is studied using the model compound methyl beta-D-glucopyranoside
the formation of glucose, arabinose, gluconic acid, erythrulose and formaldehde is detected and a mechanism for the reaction is proposed
-
?
cellobiose + ferricytochrome c
cellobiono-1,5-lactone + ferrocytochrome c
-
intact CBOR fully reduced with cellobiose, CBOR partially reduced by ascorbate and isolated ascorbate-reduced heme domain, all transfer electrons at similar rates to cytochrome c. Reduction of cationic one-electron acceptors via the heme group supports an electron transfer chain model
-
-
?
cellobiose + ferricytochrome c
cellobiono-1,5-lactone + ferrocytochrome c
-
cellobiose is the preferred substrate and cytochrome c is the preferred electron acceptor
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
-
enzyme produces H2O2 in a slow process
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
-
superoxide anion as primary reduced oxygen product, H2O2 is possibly formed by dismutation of superoxide anion
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
162% of the activity with lactose
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
enzyme consumes 1 mol molecular oxygen per mol of substrate oxidized
reaction product is cellobionic acid, no H2O2 detected, but superoxide anion
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
enzyme consumes equimolar amounts of oxygen and cellobiose
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
molecular O2 as electron acceptor
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
molecular O2 as electron acceptor
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
molecular O2 as electron acceptor
product is H2O2 and the corresponding lactone
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
readily oxidized, cellobiose and cellohexaose with almost same activity
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
readily oxidized, cellobiose and cellohexaose with almost same activity
reaction product is cellobionic acid, no H2O2 detected, but superoxide anion
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
role in cellulose degradation
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
role in cellulose degradation
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
role in cellulose and probable in lignin degradation, physiologically significant electron acceptor may or may not be oxygen
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
CBO binds strongly to cellulose and the radical reducing activity may decrease repolimerization and precipitation of lignin-like polymers on the cellulose surface, thereby facilitating cellulose degradation
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
O2 as natural electron acceptor
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
O2 as natural electron acceptor
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
role in cellulose degradation, enzyme is actively influencing lignin degradation and peroxidase activity
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
enzyme action might prevent transglycosylation reactions from taking place if high cellobiose concentrations build up
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
mechanism in which reactive oxygen species generation by the flavin of the enzyme subsequently reoxidizes the cellobiose oxidoreductase haem
-
-
?
cellodextrin + O2
aldonic acid + H2O2
-
high activity towards cellodextrins
-
?
cellodextrin + O2
aldonic acid + H2O2
-
decreasing rapidity in the series from cellobiose to cellotetraose, but then with increasing size they are more rapidly oxidized
-
-
?
cellodextrin + O2
aldonic acid + H2O2
-
decreasing rapidity in the series from cellobiose to cellotetraose, but then with increasing size they are more rapidly oxidized
-
?
cellodextrin + O2
aldonic acid + H2O2
-
higher cellodextrins
-
-
?
cellotetraose + acceptor
cellotetrono-1,5-lactone + reduced acceptor
-
-
-
?
cellotetraose + acceptor
cellotetrono-1,5-lactone + reduced acceptor
-
-
-
?
cellulose + O2
?
-
cellulose as electron donor, 10times lower oxidation rate than with cellobiose
-
-
?
lactose + acceptor
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
lactose + acceptor
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
lactose + cytochrome c
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced cytochrome c
-
-
-
-
?
lactose + cytochrome c
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced cytochrome c
-
lactose binds considerably more weakly than cellobiose
-
-
?
lactose + O2
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + H2O2
-
-
-
-
?
lactose + O2
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + H2O2
-
readily oxidized
product is lactobionic acid
?
lactose + O2
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + H2O2
-
readily oxidized
product is lactobionic acid
?
maltose + O2
4-O-beta-glucosyl-glucono-1,5-lactone + H2O2
-
-
-
?
maltose + O2
4-O-beta-glucosyl-glucono-1,5-lactone + H2O2
-
22% of the activity with lactose
-
-
?
additional information
?
-
-
not as substrates: glucose, xylose, cellulose, galactobiose, gentiobiose, H2O2 not detected as product
-
-
?
additional information
?
-
-
electron acceptors: cytochrome c, ferricyanide, 3,5-di-t-butyl-o-benzoquinone and triiodide ion, 1,2,4,5-tetramethoxybenzene cation radical
-
-
?
additional information
?
-
-
enzyme reduces cytochrome c, 200 times faster than with oxygen, 2,6-dichlorophenolindophenol, phenoxy- and cation-radicals, a vatiety of quinones and Fe(III) compounds, the latter reduced 35-50 times faster than with oxygen, enzyme has a cellulose-binding domain
-
-
?
additional information
?
-
-
electron acceptors: 3,5-di-t-butyl-o-benzoquinone, 2,6-dichlorophenolindophenol, cytochrome c
-
-
?
additional information
?
-
-
electron acceptors: great number of quinones and radicals, cytochrome c, Mn(III), ferricyanide, oxygen, reduction of Fe(III) and cytochrome c more rapid than of oxygen, enzyme reduces also compounds of ligninase and manganese peroxidase in absence of their substrates
-
-
?
additional information
?
-
-
not as substrates: maltose, sophorose, glucose, xylose, cellulose
-
-
?
additional information
?
-
-
substrates: disaccharides, some insoluble polysaccharides, but no monosaccharides, oxygen as electron acceptor, artificial electron acceptors: 2,6-dichlorophenolindophenol, potassium ferricyanide, benzyl viologen, not with: FMN, FAD, riboflavin
-
-
?
additional information
?
-
-
electron acceptors are cytochrome c, benzoquinones, dichlorophenolindophenol and Mn3+. In the absence of these electron acceptors, oxygen serves as a poor electron acceptor and is reduced to H2O2
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-glucose + acceptor
D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
lactose + acceptor
4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
maltose + acceptor
4-O-(alpha-D-glucopyranosyl)-D-glucono-1,5-lactone + reduced acceptor
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
the enzyme participates in lignocellulose degradation by white-rot fungi with a proposed role in the early events of wood degradation
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
acceptor: cytochrome c
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
-
-
-
?
cellobiose + acceptor
cellobiono-1,5-lactone + reduced acceptor
-
reduction of molecular oxygen to hydrogen peroxide, and Fe3+ to Fe2+, cellulose depolymerization is studied using the model compound methyl beta-D-glucopyranoside
the formation of glucose, arabinose, gluconic acid, erythrulose and formaldehde is detected and a mechanism for the reaction is proposed
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
role in cellulose degradation
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
role in cellulose degradation
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
role in cellulose and probable in lignin degradation, physiologically significant electron acceptor may or may not be oxygen
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
CBO binds strongly to cellulose and the radical reducing activity may decrease repolimerization and precipitation of lignin-like polymers on the cellulose surface, thereby facilitating cellulose degradation
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
O2 as natural electron acceptor
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
O2 as natural electron acceptor
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
role in cellulose degradation, enzyme is actively influencing lignin degradation and peroxidase activity
-
-
?
cellobiose + O2
cellobiono-1,5-lactone + H2O2
-
enzyme action might prevent transglycosylation reactions from taking place if high cellobiose concentrations build up
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme b
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
protoheme
-
the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme
FAD
crystal structure includes an alpha/beta-type FAD-binding subdomain, containing a seven-stranded beta sheet and six helices
FAD
FAD cofactor of the enzyme recombinantly expressed in Trichoderma reesei occupancy is 70%
FAD
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
flavin
flavin cofactor within cellobiose dehydrogenase is able to reduce all electron acceptors tested. The addition of electron acceptors increases the rate of flavin reduction and the electron transfer rate between the flavin and heme. The addition of ferric iron eliminates the flavin radical present in reduced cellobiose dehydrogenase, while it increases the flavin radical ESR signal in the independent flavin domain. No radical is detected with either cellobiose dehydrogenase or the flavin domain upon the addition of methyl-1,4-benzoquinone. Oxygen behaves like a two-electron acceptor. Superoxide production is found only upon the inclusion of iron
heme
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
cytochrome b
-
one heme b and one FAD per monomer. The native ferric form of the enzyme has absorption maxima at 420, 529, and 570 nm. The ferric enzyme does not bind azide or cyanide, implying that the heme iron is probably hexacoordinate
-
FAD
-
both the reductive and the oxidative half-reactions take place on the FAD domain
FAD
-
FAD domain has all properties of cellobiose:quinone oxidoreductase, and could be formed by proteolytic cleavage of CBO into 55 kDa FAD and 35 kDd heme domain by papain, cellulose-binding site is located on the FAD domain
FAD
-
the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme
flavin
-
flavohemoprotein, one flavin per enzyme molecule
flavin
-
1 mol cellobiose reduces 1 mol enzyme-bound flavin in the fast kinetic process
flavin
-
flavin component probably is the sugar dehydrogenating unit in the enzyme
flavin
-
falvocytochrome. Binding of cellobiose to the active site inhibits electron transfer from flavin to haem
flavin
-
recombinant enzyme contains 0.96 mol of flavin per mol of enzyme, wild-type enzyme contains 0.97 mol of flavin per mol of enzyme
heme
-
flavocytochrome. Binding of cellobiose to the active site inhibits electron transfer from flavin to heme
heme b
-
heme group: cytochrome b type, inactivated at higher pH levels, caused by conformational changes of protein, heme is necessary for reduction of cytochrome c, it acts as a single electron reductant, 35 kDa heme-containing domain
heme b
-
heme component serves for the storage of electrons to be incorporated into molecular oxygen for direct reduction to water
heme b
-
heme domain increases the rate of electron transfer to one-electron acceptors
heme b
-
cleavage of heme containing fragment by papain or V8 proteinase can convert CBO to cellobiose:quinone dehydrogenase, cytochrome b-type heme group used for storage and delivery of electrons from a two-electron donor, e.g. cellobiose, via FADH2 to one-electron acceptors, e.g. radicals, cytochrome c, ferricyanide and oxygen
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
the enzyme shows an increase in catalytic current for a factor of 2.4 at up to 100 mM Ca2+. There is a positive effect of metal cations, particularly Ca2+, on the electron transfer between the dehydrogenase domain and the cytochrome domain
Iron
-
the ferric enzyme does not bind azide or cyanide, implying that the heme iron is probably hexacoordinate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cellobiose
-
strong substrate inhibition at concentrations higher than 0.015 mM
cellobiose
-
two binding sites for the substrate: the active site and the inhibition site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0064
2,6-dichlorophenol indophenol
pH 4.5, reaction with cellobiose, wild-type enzyme
0.0074
2,6-dichlorophenol indophenol
pH 4.5, reaction with cellobiose, mutant enzyme M65H
0.018
cellobiose
pH 4.5, electron acceptor: cytochrome c, wild-type enzyme
0.035
cellobiose
pH 4.5, electron acceptor: 2,6-dichlorophenol indophenol, mutant enzyme M65H
0.04
cellobiose
pH 4.5, electron acceptor: 2,6-dichlorophenol indophenol, wild-type enzyme
0.06
cellobiose
purified wild type enzyme, pH and temperature not specified in the publication
0.08
cellobiose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
0.0008
cytochrome c
pH 4.5, reaction with cellobiose, wild-type enzyme
0.0179
cytochrome c
mutant F166Y, cellobiose oxidation with electron acceptors
0.0286
cytochrome c
wild type, cellobiose oxidation with electron acceptors
2109
D-glucose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
1.16
lactose
purified wild type enzyme, pH and temperature not specified in the publication
1.42
lactose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
0.056
ubiquinone
mutant F166Y, cellobiose oxidation with electron acceptors
0.0579
ubiquinone
wild type, cellobiose oxidation with electron acceptors
0.021
cellobiose
-
pH 4.5, 23°C, mutant enzyme H689Q or mutant enzyme H689A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.8
D-glucose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
74
FAD
-
reduction rate increases with increasing concententrations of the electron acceptors methyl-1,4-benzoquinone or Fe3+
25
2,6-dichlorophenol indophenol
pH 4.5, reaction with cellobiose, mutant enzyme M65H
27
2,6-dichlorophenol indophenol
pH 4.5, reaction with cellobiose, wild-type enzyme
0.1
cellobiose
pH 4.5, electron acceptor: cytochrome c, mutant enzyme M65H
10.5
cellobiose
pH 4.5, electron acceptor: cytochrome c, wild-type enzyme
25.7
cellobiose
pH 4.5, electron acceptor: 2,6-dichlorophenol indophenol, wild-type enzyme
26
cellobiose
pH 4.5, electron acceptor: 2,6-dichlorophenol indophenol, mutant enzyme M65H
27.8
cellobiose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
0.1
cytochrome c
pH 4.5, reaction with cellobiose, mutant enzyme M65H
10.8
cytochrome c
pH 4.5, reaction with cellobiose, wild-type enzyme
32.3
lactose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
0.004
cellobiose
-
pH 4.5, 23°C, mutant enzyme H689N or mutant H689Q
0.003
lactose
-
pH 4.5, 23°C, mutant enzyme H689Q or mutant H689A
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
D-glucose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
340
cellobiose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
22.7
lactose
pH 4.5, 30°C, acceptor: 2,6-dichlorophenolindophenol
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.51
cytochrome c
wild type, cellobiose oxidation with electron acceptors
3.54
cytochrome c
mutant F166Y, cellobiose oxidation with electron acceptors
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.3
purified mutant enzyme E279N, pH and temperature not specified in the publication
1.9
purified wild type enzyme, pH and temperature not specified in the publication
10.3
additional information
additional information
-
6.8 micromol/min*l, enzyme activity in extracelluar solution after growth for 4 d
additional information
-
1.7 micromol/min*l, cellulose bound enzyme after growth for 4 d
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
3
-
cellobiose + cytochrome c, highest activity at pH 3, decreasing as the pH increases, recombinant wild-type enzyme, mutant enzymes N732H, N732Q and N732A
3 - 5
-
cellobiose + 2,6-dichlorophenol-indophenol, wild-type enzyme
4
-
enzyme treatment of methyl beta-D-glucopyranoside, monosaccharides and cellulose
6.5 - 7
-
cellobiose + 2,6-dichlorophenol-indophenol, mutant enzyme N732E and N732D
4
activity with cytochrome c or 1,4-benzoquinone as acceptor
4.5
activity with 2,6-dichlorophenolindophenol as acceptor
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5 - 5
3 - 6
more than 50% activity in the pH range between pH 3.0-6.0, acceptor: 1,4-benzoquinone
3.2 - 6.2
pH 3.2: about 30% of maximal activity, pH 6.2: about 45% of maximal activity, activity with 2,6-dichlorophenolindophenol as acceptor, Phanerochaete chrysosporium enzyme recombinantly expressed in Trichoderma reesei
3.5 - 6
pH 3.5: about 35% of maximal activity, pH 6.0: about 40% of maximal activity, activity with 2,6-dichlorophenolindophenol as acceptor, enzyme from Phanerochaete chrysosporium
3 - 5.5
-
highest activity at pH 3, decreases to 10-20% of the activity when the pH increases to pH 5.5, cellobiose + cytochrome c recombinant wild-type enzyme, mutant enzymes N732H, N732Q and N732A
3 - 7
-
highest activity at pH 3, decreases when the pH increases to pH 7.0, cellobiose + 2,6-dichlorophenol-indophenol, to about 10% with recombinant wild-type enzyme, to about 25% with mutant enzymes N732Q, to about 40% with mutant enzyme N732A and to about 50% with mutant enzyme N732H
4 - 6
-
pH 5.0: about 35% of maximal activity, pH 7.0: about 20% of maximal activity, cellobiose + cytochrome c, mutant enzyme N732E
4 - 6.5
-
the relative activity of purified enzyme is decreased when pH is over 4.5 and it is below 80% at 6.5
4.1 - 5.7
-
pH 4.1: less than 50% of maximum activity, pH 5.7: less than 50% of maximum activity
5 - 7
-
pH 5.0: about 40% of maximal activity, pH 7.0: about 20% of maximal activity, cellobiose + cytochrome c, mutant enzyme N732D
5.5 - 7.5
-
pH 5.0: about 45% of maximal activity, pH 7.0: about 65% of maximal activity, cellobiose + 2,6-dichlorophenol-indophenol, mutant enzyme N732E
5.5 - 8
-
pH 5.5: about 50% of maximal activity, pH 8.0: about 60% of maximal activity, cellobiose + 2,6-dichlorophenol-indophenol, mutant enzyme N732D
2.5 - 5
pH 2.5: about 15% of maximal activity, pH 5.0: about 40% of maximal activity, activity with cytochrome c as acceptor, Phanerochaete chrysosporium enzyme recombinantly expressed in Trichoderma reesei
2.5 - 5
pH 2.5: about 45% of maximal activity, pH 5.0: about 55% of maximal activity, activity with cytochrome c as acceptor, enzyme from Phanerochaete chrysosporium
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
30
-
enzyme treatment of methyl beta-D-glucopyranoside, monosaccharides and cellulose
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CDH_PHACH
773
0
82007
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
90000
93000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
glycoprotein
high mannose-type N-glycans in the enzyme from Phanerochaete chrysosporium. Only single N-acetyl-D-glucosamine additions at the six potential N-glycosylation sites in the enzyme recombinantly expressed in Trichoderma reesei
glycoprotein
-
MW after deglycosylation is 92000 for the recombinant enzyme and 90000 for wild-type enzyme
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure with a bound inhibitor,cellobiono-1,5-lactone, at 1.8 A resolution
hanging-drop vapour diffusion method, crystal structure determined at 1.5 A resolution
hanging-drop vapour diffusion method, crystal structure of M65H cytochrome domain determined at 1.9 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E279A
the mutation has no effect on the expression of the protein in Pichia pastoris but completely abolishes its enzymatic activity
E279D
the mutation has no effect on the expression of the protein in Pichia pastoris but completely abolishes its enzymatic activity
E279N
the mutation has no effect on the expression of the protein in Pichia pastoris but completely abolishes its enzymatic activity. The mutant retains most of its activity with cellobiose but was completely inactive with lactose
F166Y
the redox potential of heme in the mutant is lower than that of the wild type enzyme
M65F
mutant with increased activity and stability in the presence of peroxide. 70% of residual activity after 6 h of incubation in 0.3 M hydrogen peroxide, compared to wild-type CDH that retained 40% of original activity
M65H
the variant retains the flavin catalytic reactivity, the ability of the mutant to reduce external one-electron acceptors such as cytochrome c is impaired, decrease in the redox midpoint potential of the heme by 210 mV. IN contrast to the wild-type enzyme, the ferric state of the protoheme displays a mixed low spin/high spin state at room temperature and low spion character at 90 K
M685Y
mutant with increased activity and stability in the presence of peroxide. 90% of residual activity after 6 h of incubation in 0.3 M hydrogen peroxide, compared to wild-type CDH that retained 40% of original activity. 2.5 times increased kcat for lactose compared to wild-type enzyme. The mutant enzyme is a good candidate for applications in biofuel cells and biocatalysis for lactobionic acid production
M738S
mutant with increased activity and stability in the presence of peroxide. 80% of residual activity after 6 h of incubation in 0.3 M hydrogen peroxide, compared to wild-type CDH that retained 40% of original activity
H689A
-
more than 1000fold lower turnover value, Km-value for cellobiose and lactose is similar to that of the wild-type enzyme
H689E
-
more than 1000fold lower turnover value, Km-value for cellobiose and lactose is similar to that of the wild-type enzyme
H689N
-
more than 1000fold lower turnover value, Km-value for cellobiose and lactose is similar to that of the wild-type enzyme
H689Q
-
more than 1000fold lower turnover value, Km-value for cellobiose and lactose is similar to that of the wild-type enzyme
H689V
-
more than 1000fold lower turnover value, Km-value for cellobiose and lactose is similar to that of the wild-type enzyme
N732A
-
the turnover-number for cellobiose is 38.8fold lower than the turnover-number of the wild-type enzyme, the Km-value for cellobiose is 1.1fold higher than the KM-value of the wild-type enzyme, the turnover-number for lactose is 20.4fold lower than the turnover-number of the wild-type enzyme, the Km-value for lactose is 4.4fold higher than the KM-value of the wild-type enzyme
N732D
-
the turnover-number for cellobiose is 3875fold lower than the turnover-number of the wild-type enzyme, the Km-value for cellobiose is 10.6fold higher than the KM-value of the wild-type enzyme, the turnover-number for lactose is 2860fold lower than the turnover-number of the wild-type enzyme, the Km-value for lactose is 42.2fold higher than the KM-value of the wild-type enzyme. The pH optimum is shifted from pH 3-5 for the wild-type enzyme in the reaction with cellobiose and 2,6-dichlorophenol-indophenol to pH 6.5-7.0. The pH optimum is shifted from pH 3 for the wild-type enzyme in the reaction with cellobiose and cytochrome c to pH 6
N732E
-
the turnover-number for cellobiose is 73.8fold lower than the turnover-number of the wild-type enzyme, the Km-value for cellobiose is 14.4fold higher than the KM-value of the wild-type enzyme, the turnover-number for lactose is 47.7fold lower than the turnover-number of the wild-type enzyme, the Km-value for lactose is 61.5fold higher than the KM-value of the wild-type enzyme. The pH optimum is shifted from pH 3-5 for the wild-type enzyme in the reaction with cellobiose and 2,6-dichlorophenol-indophenol to pH 6.5-7.0.The pH optimum is shifted from pH 3 for the wild-type enzyme in the reaction with cellobiose and cytochrome c to pH 5
N732H
-
the turnover-number for cellobiose is 5.7fold lower than the turnover-number of the wild-type enzyme, the Km-value for cellobiose is 2.4fold higher than the KM-value of the wild-type enzyme, the turnover-number for lactose is 8.4fold lower than the turnover-number of the wild-type enzyme, the Km-value for lactose is 8.5fold higher than the KM-value of the wild-type enzyme
N732Q
-
the turnover-number for cellobiose is 15.5fold lower than the turnover-number of the wild-type enzyme, the Km-value for cellobiose is 2.6fold higher than the KM-value of the wild-type enzyme, the turnover-number for lactose is 11.9fold lower than the turnover-number of the wild-type enzyme, the Km-value for lactose is 14.8fold higher than the KM-value of the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 11
-
pH 2: below large loss of activity, pH 11: above large loss of activity
389751
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 60
-
the enzyme is highly stable at 30-60°C, with maximum activity at 30°C when incubated for 5 min. Below 30°C and above 60°C, the enzyme activity decreases, respectively
40 - 60
-
20% activity lost after 12 h at 50°C and pH 6.1, 80% activity lost after 1 h at 60°C and pH 6.1, all activity lost after 10 min at 70°C and pH 6.1
60
-
25 min half-life at 60°C, instantaneousley inactivated at 70°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM sodium acetate buffer, pH 5, 1 week, less than 10% loss of activity
-
0°C, 50 mM sodium acetate buffer, pH 5, 1 week, less than 10% loss of activity
-
4°C, 50 mM potassium phosphate buffer, pH 6, several months, stable, slowly loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and Resource Q column chromatography
enzyme from Phanerochaete chrysosporium and enzyme recombinantly expressed in Trichoderma reesei
ammonium sulfate, DEAE-Sephadex, Phenyl-Sepharose, Sephacryl S-200, Mono Q
-
using a Q-Sepharose anion exchange column, a Phenyl Sepharose hydrophobic interaction column, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Pichia pastoris strain GS115 and Trichoderma reesei strain QM9414
expression in Trichoderma reesei. Heterologous production of the enzyme (PcCDH) is faster and the yield higher than secretion by Phanerochaete chrysosporium. It does not need a cellulose-based medium that impedes efficient production and purification of the enzyme (PcCDH) by binding to the polysaccharide. The obtained high uniformity of Phanerochaete chrysosporium CDHTr glycoforms is very useful to investigate electron transfer characteristics in biosensors and biofuel cells, which are depending on the spatial restrictions inflicted by high-mannose N-glycan trees. The determined catalytic and electrochemical properties of PcCDHTr are very similar to those of PcCDH and the FAD cofactor occupancy is good, which advocates Trichoderma reesei as expression host for engineered PcCDH for biosensors and biofuel cells
wild type and mutant cellobiose dehydrogenase genes are cloned for heterologously expression in yeast Pichia pastoris
expression in Pichia pastoris, enzyme retains catalytic and cellulose-binding properties of the wild-type enzyme
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
diagnostics
industry
the enzyme can be used for bleaching cotton in textile industry
medicine
application in biomedicine as an antimicrobial and antibiofilm agent
analysis
biotechnology
-
the Pichia expression system is well suited for high-level production of recombinant enzyme
biofuel production
the enzyme can be used for constructing biofuel cells
diagnostics
the enzyme can be used for constructing biosensors
analysis
-
enzyme is used in highly selective amperometric biosensors
analysis
-
cellobiose dehydrogense - electrode system for electrochemical applications
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bao, W.; Usha, S.N.; Renganathan, V.
Purification and characterization of cellobiose dehydrogenase, a novel extracellular hemoflavoenzyme from the white-rot fungus Phanerochoaete chrysosporium
Arch. Biochem. Biophys.
300
705-713
1993
Phanerodontia chrysosporium, Phanerodontia chrysosporium OGC 101
Costa-Ferreira, M.; Ander, P.; Duarte, J.
On the relationship between cellobiose dehydrogenase and cellobiose:quinone oxidoreductase under conditions where [14C]DHP is mineralized by whole cultures of Phanerochoaete chrysosporium
Enzyme Microb. Technol.
16
771-776
1994
Phanerodontia chrysosporium, Phanerodontia chrysosporium ME-446
-
Subramaniam, S.S.; Nagalla, S.R.; Renganathan, V.
Cloning and characterization of a thermostable cellobiose dehydrogenase from Sporotrichum thermophile
Arch. Biochem. Biophys.
365
223-230
1999
Phanerodontia chrysosporium, Thermothelomyces heterothallicus
Cameron, M.D.; Aust, S.D.
Kinetics and reactivity of the flavin and heme cofactors of cellobiose dehydrogenase from Phanerochaete chrysosporium
Biochemistry
39
13595-13601
2000
Phanerodontia chrysosporium
Henriksson, G.; Johansson, G.; Pettersson, G.
A critical review of cellobiose dehydrogenase
J. Biotechnol.
10
93-113
2000
Phanerodontia chrysosporium, Thermothelomyces heterothallicus, Coniophora puteana (Schum ex Fr) Karsten, Athelia rolfsii, Humicola insolens, Monilia sitophila, Schizophyllum commune
Ayers, A.R.; Eriksson, K.E.
Cellobiose oxidase from Sporotrichum pulverulentum
Methods Enzymol.
89
129-135
1982
Phanerodontia chrysosporium
Morpeth, F.F.
Some properties of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum
Biochem. J.
228
557-564
1985
Phanerodontia chrysosporium
Jones, G.D.; Wilson, M.T.
Rapid kinetic studies of the reduction of cellobiose oxidase from the white-rot fungus Sporotrichum pulverulentum by cellobiose
Biochem. J.
256
713-718
1988
Phanerodontia chrysosporium, Phanerodontia chrysosporium CMI 172727
Ayers, A.R.; Ayers, S.B.; Eriksson, K.E.
Cellobiose oxidase, purification and partial characterization of a hemoprotein from Sporotrichum pulverulentum
Eur. J. Biochem.
90
171-181
1978
Phanerodontia chrysosporium
Eriksson, K.E.
Enzyme mechanisms involved in cellulose hydrolysis by the rot fungus Sporotrichum pulverulentum
Biotechnol. Bioeng.
20
317-332
1978
Phanerodontia chrysosporium
-
Henriksson, G.; Johansson, G.; Pettersson, G.
Is cellobiose oxidase from Phanerochaete chrysosporium a one-electron reductase?
Biochim. Biophys. Acta
1144
184-190
1993
Phanerodontia chrysosporium, Phanerodontia chrysosporium K 3
Eriksson, K.E.; Habu, N.; Samejima, M.
Recent advances in fungal cellobiose oxidoreductases
Enzyme Microb. Technol.
15
1002-1008
1993
Phanerodontia chrysosporium, Phanerodontia chrysosporium K 3
-
Ander, P.; Sena-Martins, G.; Duarte, J.C.
Influence of cellobiose oxidase on peroxidases from Phanerochaete chrysosporium
Biochem. J.
293
431-435
1993
Coniophora puteana, Phanerodontia chrysosporium, Phanerodontia chrysosporium K 3
Ander, P.
The cellobiose-oxidizing enzymes CBQ and CbO as related to lignin and cellulose degradation, a review
FEMS Microbiol. Rev.
13
297-312
1994
Phanerodontia chrysosporium, Coniophora puteana
-
Igarashi, K.; Momohara, I.; Nishino, T.; Samejima, M.
Kinetics of interdomain electron transfer in flavocytochrome cellobiose dehydrogenase from white-rot fungus Phanerochaete chrysosporium
Biochem. J.
265
521-526
2002
Phanerodontia chrysosporium
Rotsaert, F.A.J.; Renganathan, V.; Gold, M.H.
Role of the flavin domain residues, His689 and Asn732, in the catalytic mechanism of cellobiose dehydrogenase from Phanerochaete chrysosporium
Biochemistry
42
4049-4056
2003
Phanerodontia chrysosporium
Mason, M.G.; Nicholls, P.; Divne, C.; Hallberg, B.M.; Henriksson, G.; Wilson, M.T.
The heme domain of cellobiose oxidoreductase: a one-electron reducing system
Biochim. Biophys. Acta
1604
47-54
2003
Phanerodontia chrysosporium
Yoshida, M.; Ohira, T.; Igarashi, K.; Nagasawa, H.; Aida, K.; Hallberg, B.M.; Divne, C.; Nishino, T.; samejima, M.
Production and characterization of recombinant Phanerochaete chrysosporium cellobiose dehydrogenase in the methylotrophic yeast Pichia pastoris
Biosci. Biotechnol. Biochem.
65
2050-2057
2001
Phanerodontia chrysosporium
Mason, M.G.; Wilson, M.T.; Ball, A.; Nicholls, P.
Oxygen reduction by cellobiose oxidoreductase: the role of the heme group
FEBS Lett.
518
29-32
2002
Phanerodontia chrysosporium
Rotsaert, F.A.J.; Hallberg, B.M.; de Vrise, S.; Moenne-Loccoz, P.; Divne, C.; Renganathan, V.; Gold, M.H.
Biophysical and structural analysis of a novel heme b iron ligation in the flavocytochrome cellobiose dehydrogenase
J. Biol. Chem.
278
33224-33231
2003
Phanerodontia chrysosporium (Q01738)
Hallberg, B.M.; Henriksson, G.; Pettersson, G.; Vasella, A.; Divne, C.
Mechanism of the reductive half-reaction in cellobiose dehydrogenase
J. Biol. Chem.
278
7160-7166
2003
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium
Hallberg, M.B.; Henriksson, G.; Pettersson, G.; Divne, C.
Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
J. Mol. Biol.
315
421-434
2002
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium, Phanerodontia chrysosporium K3 (Q01738)
Rogers, M.S.; Jones, G.D.; Antonini, G.; Wilson, M.T.; Brunori, M.
Electron transfer from Phanerochaete chrysosporium cellobiose oxidase to equine cytochrome c and Pseudomonas aeruginosa cytochrome c-551
Biochem. J.
298
329-334
1994
Phanerodontia chrysosporium
-
Feng, J.; Himmel, M.E.; Decker, S.R.
Electrochemical oxidation of water by a cellobiose dehydrogenase from Phanerochaete chrysosporium
Biotechnol. Lett.
27
555-560
2005
Phanerodontia chrysosporium
Zamocky, M.; Ludwig, R.; Peterbauer, C.; Hallberg, B.M.; Divne, C.; Nicholls, P.; Haltrich, D.
Cellobiose dehydrogenase--a flavocytochrome from wood-degrading, phytopathogenic and saprotropic fungi
Curr. Protein Pept. Sci.
7
255-280
2006
Aspergillus fumigatus (Q4WZA6), Aspergillus nidulans, Athelia rolfsii (Q7Z975), Chaetomium sp., Coniophora puteana (Q6BDD5), Flammulina velutipes, Fusarium graminearum, Ganoderma gibbosum, Grifola frondosa (Q8J2T4), Hericium erinaceus, Heterobasidion annosum, Humicola insolens (Q9P8H5), Irpex lacteus (Q6AW20), Monilia sp., Neurospora crassa, Phanerodontia chrysosporium (Q01738), Pyricularia grisea, Saccharomyces cerevisiae, Schizophyllum commune, Shewanella frigidimarina, Thermothelomyces fergusii, Thermothelomyces myriococcoides, Trametes cinnabarina (O74253), Trametes pubescens, Trametes versicolor (O42729), Trametes villosa, [Sclerotium] coffeicola, [Sclerotium] delphinii
Igarashi, K.; Yoshida, M.; Matsumura, H.; Nakamura, N.; Ohno, H.; Samejima, M.; Nishino, T.
Electron transfer chain reaction of the extracellular flavocytochrome cellobiose dehydrogenase from the basidiomycete Phanerochaete chrysosporium
FEBS J.
272
2869-2877
2005
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium
Krusa, M.; Henriksson, G.; Johansson, G.; Reitberger, T.; Lennholm, H.
Oxidative cellulose degradation by cellobiose dehydrogenase from Phanerochaete chrysosporium: A model compound study
Holzforschung
59
263-268
2005
Phanerodontia chrysosporium
-
Stoica, L.; Ruzgas, T.; Ludwig, R.; Haltrich, D.; Gorton, L.
Direct electron transfer--a favorite electron route for cellobiose dehydrogenase (CDH) from Trametes villosa. Comparison with CDH from Phanerochaete chrysosporium
Langmuir
22
10801-10806
2006
Trametes villosa, Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium
Stoica, L.; Ruzgas, T.; Gorton, L.
Electrochemical evidence of self-substrate inhibition as functions regulation for cellobiose dehydrogenase from Phanerochaete chrysosporium
Bioelectrochemistry
76
42-52
2009
Phanerodontia chrysosporium
Tasca, F.; Gorton, L.; Harreither, W.; Haltrich, D.; Ludwig, R.; Nll, G.
Direct electron transfer at cellobiose dehydrogenase modified anodes for biofuel cells
J. Phys. Chem. C Nanomater. Interfaces
112
9956-9961
2008
Phanerodontia chrysosporium, Athelia rolfsii, Thermothelomyces myriococcoides, Phanerochaete sordida, Trametes villosa, Trametes villosa CBS 334.49, Phanerochaete sordida MB 66, Athelia rolfsii CBS 191.62, Thermothelomyces myriococcoides CBS 208.89, Phanerodontia chrysosporium K3
-
Desriani, S.; Ferri, S.; Sode, K.
Amino acid substitution at the substrate-binding subsite alters the specificity of the Phanerochaete chrysosporium cellobiose dehydrogenase
Biochem. Biophys. Res. Commun.
391
1246-1250
2010
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium, Phanerodontia chrysosporium RP78 (Q01738)
Desriani, ; Ferri, S.; Sode, K.
Functional expression of Phanerochaete chrysosporium cellobiose dehydrogenase flavin domain in Escherichia coli
Biotechnol. Lett.
32
855-859
2010
Phanerodontia chrysosporium
Schulz, C.; Ludwig, R.; Micheelsen, P.; Silow, M.; Toscano, M.; Gorton, L.
Enhancement of enzymatic activity and catalytic current of cellobiose dehydrogenase by calcium ions
Electrochem. Commun.
17
71-74
2012
Phanerodontia chrysosporium, Humicola insolens, Thermothelomyces myriococcoides
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Wang, M.; Lu, X.
Exploring the synergy between cellobiose dehydrogenase from Phanerochaete chrysosporium and cellulase from Trichoderma reesei
Front. Microbiol.
7
620
2016
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium
Choi, H.; Kim, D.; Thapa, L.; Lee, S.; Kim, S.; Cho, J.; Park, C.; Kim, S.
Production and characterization of cellobiose dehydrogenase from Phanerochaete chrysosporium KCCM 60256 and its application for an enzymatic fuel cell
Korean J. Chem. Engin.
33
3434-3441
2016
Phanerodontia chrysosporium, Phanerodontia chrysosporium KCCM 60256
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Bao, W.; Usha, S.N.; Renganathan, V.
Purification and characterization of cellobiose dehydrogenase, a novel extracellular hemoflavoenzyme from the white-rot fungus Phanerochaete chrysosporium
Arch. Biochem. Biophys.
300
705-713
1993
Phanerodontia chrysosporium
Henriksson, G.; Salumets, A.; Divne, C.; Petersson, G.
Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1
Biochem. J.
324
833-838
1997
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium
Cameron, M.D.; Aust, S.D.
Kinetics and reactivity of the flavin and heme cofactors of cellobiose dehydrogenase from Phanerochaete chrysosporium
Biochemistry
39
13595-13601
2000
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium
Scheiblbrandner, S.; Ludwig, R.
Cellobiose dehydrogenase Bioelectrochemical insights and applications
Bioelectrochemistry
131
107345
2020
Trametes hirsuta, Athelia rolfsii, Albifimbria verrucaria, Phanerochaete sordida, Trametes villosa, Thermothelomyces myriococcoides (A9XK88), Thermothelomyces fergusii (E7D6B9), Dichomera saubinetii (E7D6C1), Phanerodontia chrysosporium (Q01738), Humicola insolens (Q9P8H5)
Wohlschlager, L.; Csarman, F.; Chang, H.; Fitz, E.; Seiboth, B.; Ludwig, R.
Heterologous expression of Phanerochaete chrysosporium cellobiose dehydrogenase in Trichoderma reesei
Microb. Cell Fact.
20
2
2021
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium
Balaz, A.M.; Stevanovic, J.; Ostafe, R.; Blazic, M.; Ilic Durdic, K.; Fischer, R.; Prodanovic, R.
Semi-rational design of cellobiose dehydrogenase for increased stability in the presence of peroxide
Mol. Divers.
24
593-601
2020
Phanerodontia chrysosporium (Q01738), Phanerodontia chrysosporium
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