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
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1.1.99.18
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cellulose
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phanerochaete
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chrysosporium
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biofuels
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basidiomycete
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flavocytochrome
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lignocellulose
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white-rot
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laccase
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pyranose
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corynascus
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lpmos
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myriococcum
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wood-degrading
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trametes
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cellodextrins
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thermophilum
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ligninolytic
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cello-oligosaccharides
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cellulose-binding
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glucose-methanol-choline
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cellulose-degrading
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flavodehydrogenase
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analysis
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sporotrichum
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rolfsii
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insolens
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myrothecium
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cellulose-grown
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biofuel production
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biotechnology
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industry
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dichlorophenol-indophenol
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brown-rot
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pycnoporus
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cellulose-based
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humicola
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wood-rotting
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bioanode
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verrucaria
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cellobiohydrolases
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diagnostics
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medicine
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synthesis
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degradation
- 1.1.99.18
- cellulose
- phanerochaete
- chrysosporium
-
biofuels
-
basidiomycete
-
flavocytochrome
- lignocellulose
-
white-rot
- laccase
- pyranose
- corynascus
-
lpmos
-
myriococcum
-
wood-degrading
- trametes
- cellodextrins
- thermophilum
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ligninolytic
- cello-oligosaccharides
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cellulose-binding
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glucose-methanol-choline
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cellulose-degrading
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flavodehydrogenase
- analysis
- sporotrichum
- rolfsii
- insolens
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myrothecium
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cellulose-grown
- biofuel production
- biotechnology
- industry
- dichlorophenol-indophenol
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brown-rot
- pycnoporus
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cellulose-based
- humicola
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wood-rotting
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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
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Application
Application on EC 1.1.99.18 - cellobiose dehydrogenase (acceptor)
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analysis
biofuel production
biotechnology
degradation
diagnostics
industry
medicine
synthesis
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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. These concentrations of up to 80 g peptone per l are not realistic for large scale-fermentations. Yet high levels of the enzyme produced under these conditions should stimulate both basic studies on the enzyme and studies on potential technological applications, e.g. for biosensors, bioremediation, or biocatalysis
analysis
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enzyme is used in highly selective amperometric biosensors
analysis
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enzyme is used in highly selective amperometric biosensors
analysis
Coniophora puteana (Schum ex Fr) Karsten
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enzyme is used in highly selective amperometric biosensors
analysis
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cellobiose dehydrogense - electrode system for electrochemical applications
analysis
the enzyme has applications in lactose determination in food and as biosensor
analysis
the enzyme is used in lactose determination in food
application in enzymatic fuel cells is limited by their relatively low activity with this substrate
biofuel production
Thermothelomyces fergusii
application in enzymatic fuel cells is limited by their relatively low activity with this substrate
biofuel production
Thermothelomyces myriococcoides
attractive oxidoreductase for bioelectrochemical applications. Its two-domain structure allows the flavoheme enzyme to establish direct electron transfer to biosensor and biofuel cell electrodes. The application of CDH in these devices is impeded by its limited stability under turnover conditions. Screening results in one CDH variant that exhibits improved turnover stability on a biosensor electrode, which is suitable for the application in implantable continuous glucose monitoring biosensors or biofuel cells
biofuel production
the enzyme can be used for constructing biofuel cells
biofuel production
the enzyme has applications in renewable biofuel production
biofuel production
the enzyme is used in biofuel production
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the Pichia expression system is well suited for high-level production of recombinant enzyme
biotechnology
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biosensors with a cellulosic carrier containing self-assembled nanocomposites of CDH and other enzymes allow the determination of 100 nm dopamine
biotechnology
Thermothelomyces myriococcoides
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cellobiose dehydrogenase is a promising enzyme for the development of biosensors and biofuel cells
biotechnology
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class II cellobiose dehydrogenases are potential candidates for glucose biosensors and biofuel cell anodes
biotechnology
Thermothelomyces fergusii
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class II cellobiose dehydrogenases are potential candidates for glucose biosensors and biofuel cell anodes
biotechnology
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class II cellobiose dehydrogenases are potential candidates for glucose biosensors and biofuel cell anodes
biotechnology
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class II cellobiose dehydrogenases are potential candidates for glucose biosensors and biofuel cell anodes
biotechnology
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class II cellobiose dehydrogenases are potential candidates for glucose biosensors and biofuel cell anodes
biotechnology
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class II cellobiose dehydrogenases are potential candidates for glucose biosensors and biofuel cell anodes
biotechnology
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biosensors with a cellulosic carrier containing self-assembled nanocomposites of CDH and other enzymes allow the determination of 100 nm dopamine
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Thermothelomyces myriococcoides
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CDH is able to produce a sufficient amount of H2O2 to decolorize anthocyanins within 2 h
degradation
Thermothelomyces myriococcoides CBS 208.89
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CDH is able to produce a sufficient amount of H2O2 to decolorize anthocyanins within 2 h
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diagnostics
the enzyme can be used for constructing biosensors
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CDH is involved in the degradation of the two most prominent biopolymers, cellulose and lignin, CDH can produce both reagents needed for fenton chemistry, H2O2 and ferrous iron complexes, which may migrate into and disrupt the lignocellulose matrix
industry
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CDH is involved in the degradation of the two most prominent biopolymers, cellulose and lignin, CDH can produce both reagents needed for fenton chemistry, H2O2 and ferrous iron complexes, which may migrate into and disrupt the lignocellulose matrix
industry
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CDH is involved in the degradation of the two most prominent biopolymers, cellulose and lignin, CDH can produce both reagents needed for fenton chemistry, H2O2 and ferrous iron complexes, which may migrate into and disrupt the lignocellulose matrix
industry
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CDH is involved in the degradation of the two most prominent biopolymers, cellulose and lignin, CDH can produce both reagents needed for fenton chemistry, H2O2 and ferrous iron complexes, which may migrate into and disrupt the lignocellulose matrix
industry
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decolourisation of waste water in textile dyeing industry, CDH displays a synergism with laccases in the decolourisation of ABu62, an anthraquinonic dye, and an antagonism with laccases in the decolourisation of the anthraquinonic dyes ABu281 and RBu19
industry
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decolourisation of waste water in textile dyeing industry, CDH displays a synergism with laccases in the decolourisation of ABu62, an anthraquinonic dye, and an antagonism with laccases in the decolourisation of the anthraquinonic dyes ABu281 and RBu19
industry
the enzyme can be used for bleaching cotton in textile industry
industry
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decolourisation of waste water in textile dyeing industry, CDH displays a synergism with laccases in the decolourisation of ABu62, an anthraquinonic dye, and an antagonism with laccases in the decolourisation of the anthraquinonic dyes ABu281 and RBu19
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industry
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decolourisation of waste water in textile dyeing industry, CDH displays a synergism with laccases in the decolourisation of ABu62, an anthraquinonic dye, and an antagonism with laccases in the decolourisation of the anthraquinonic dyes ABu281 and RBu19
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application in biomedicine as an antimicrobial and antibiofilm agent