EC 1.1.3.B5: eugenol oxidase
This is an abbreviated version!
For detailed information about eugenol oxidase, go to the full flat file.

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Synonyms
EUGO, RHA1_ro03282
ECTree
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Engineering
Engineering on EC 1.1.3.B5 - eugenol oxidase
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I427A
mutant is significantly more efficient with 2,6-dimethoxy-4-allylphenol than wild-type
L438C
variant displays lowered activity towards all substrates as compared to wild-type
Q425T
display similar activity to the wild-type enzyme with vanillyl alcohol, but no measurable activity towards any other substrate
V436I
variant displays lowered activity towards vanillyl alcohol and eugenol
additional information
exchange of a loop at the dimer-dimer interface in octameric vanillin oxidase that is not present in dimeric EUGO. A vanillin oxidase variant where the loop was deleted, loopless VAO, exclusively forms dimers. Introduction of the loop into EUGO is not sufficient to induce its octamerization. Neither variant displays major changes in its catalytic properties as compared to the wild-type enzyme

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