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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

Reaction

cellobiose
+
acceptor
=
cellobiono-1,5-lactone
+
reduced acceptor

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

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.99 With unknown physiological acceptors
                1.1.99.18 cellobiose dehydrogenase (acceptor)

Engineering

Engineering on EC 1.1.99.18 - cellobiose dehydrogenase (acceptor)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C285Y
mutation causes a 5.6time decrease in KM for glucose and a decreased affinity for the other disaccharides. Overall catalytic efficiency increases 6.7times as compared to the wild type enzyme
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
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
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
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
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
-
C291Y
Thermothelomyces fergusii
mutation causes a 8.3times decrease in KM for glucose and a decreased affinity for the other disaccharides
L324C
Thermothelomyces myriococcoides
the variant loses approximately half of their activities within 52 h at 37°C
L324C/M409S
Thermothelomyces myriococcoides
lower catalytic activity as compared to wild-type enzyme. The variant loses approximately half of their activities within 52 h at 37°C
M309K
Thermothelomyces myriococcoides
retains most of its initial activity among the single variants. Mutation improve the turnover stability of the enzyme
M309K/L324C
Thermothelomyces myriococcoides
the Tm-value of the variant is 1.8°C lower than the wild-type value
M309K/M409S
Thermothelomyces myriococcoides
variant with the highest residual activity after 4 h at 41 °C under turnover conditions. Lower catalytic activity as compared to wild-type enzyme
M309V
Thermothelomyces myriococcoides
the mutant enzyme shows significant stability improvements compared to the wild-type enzyme. Higher cytochrome c/2,6-dichloroindophenol activity ratio than the wild-type enzyme
M409S
Thermothelomyces myriococcoides
mutation improve the turnover stability of the enzyme. Most stable variant with an electrode half-life of 13.5 h
N700S
Thermothelomyces myriococcoides
the kcat for oxygen turnover is increased in this mutant (4.5fold), but also substrate turnover. A 3fold increase of the kcat for cellobiose with alternative electron acceptors indicates that mutation N700S influences the oxidative- and reductive FAD half-reaction