1.1.99.18: cellobiose dehydrogenase (acceptor)
This is an abbreviated version!
For detailed information about cellobiose dehydrogenase (acceptor), go to the full flat file.
Word Map on EC 1.1.99.18
-
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
- 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
Reaction
Synonyms
cbdA, CBO, CBOR, Cdh, CDH IIA, CDH IIB, cdh-1, CDH1, Cdh2, CDHIIA, cellobiose (acceptor) 1-oxidoreductase, cellobiose dehydrogenase, cellobiose dehydrogenase IIA, cellobiose oxidase, cellobiose oxidoreductase, cellobiose [acceptor] 1-oxidoreductase, Cellobiose-quinone oxidoreductase, cellobiose:(acceptor) 1-oxidoreductase, cellobiose:quinone oxidoreductase, cellobiose:[acceptor] 1-oxidoreductase, DCHsr, dehydrogenase, cellobiose, EC 1.1.3.25, EC 1.1.5.1, MtCDH, oxidase, cellobiose, Thite_59724, TpCDH, TvCDH
ECTree
Advanced search results
Cofactor
Cofactor on EC 1.1.99.18 - cellobiose dehydrogenase (acceptor)
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
protoheme
-
the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme
additional information
-
limited proteolytic cleavage of the enzyme leads to an inactive heme peptide and an active FAD domain which has been termed cellobiose: quinone 1-oxidoreductase EC 1.5.1.1
-
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
crystal structure includes an alpha/beta-type FAD-binding subdomain, containing a seven-stranded beta sheet and six helices
FAD
-
the enzyme comprises two redox domains, one containing flavin adenine dinucleotide and the other protoheme
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
FAD
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
FAD
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
FAD
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
FAD
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
FAD
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
FAD
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
FAD
Thermothelomyces myriococcoides
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
FAD
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
FAD
Thermothelomyces fergusii
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
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
flavin
-
the enzyme contains a protease-sensitive linker region, can be cleaved by endogenous proteases into a catalytically active flavin fragment and an inactive haem domain. Cleavage can be prevented by using increased concentrations of peptone or certain amino acids such as Val or Leu
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
flavin
protein displays absorption maximum at 419 nm with a broad tail from about 450-480 nm, corresponding to the ferric heme and flavin groups respectively
heme
-
flavocytochrome. Binding of cellobiose to the active site inhibits electron transfer from flavin to heme
heme
-
the enzyme contains a protease-sensitive linker region, can be cleaved by endogenous proteases into a catalytically active flavin fragment and an inactive haem domain
heme
-
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
-
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
Thermothelomyces myriococcoides
-
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
-
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
[Sclerotium] coffeicola
-
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
[Sclerotium] delphinii
-
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
Thermothelomyces fergusii
-
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
protoporphyrin IX, protoheme IX, heme b, one heme per CDH molecule
heme
protein displays absorption maximum at 419 nm with a broad tail from about 450-480 nm, corresponding to the ferric heme and flavin groups respectively
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
heme b
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme b
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme b
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme b
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme b
-
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme b
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme b
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme b
Thermothelomyces myriococcoides
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors
heme b
flavocytochrome. Electrochemical methods are used to study the redox potentials of the FAD and the heme b cofactors