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, cellobiose (acceptor) 1-oxidoreductase, cellobiose dehydrogenase, 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, 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
N700S
-
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
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
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
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