Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.1.3.38: vanillyl-alcohol oxidase

This is an abbreviated version!
For detailed information about vanillyl-alcohol oxidase, go to the full flat file.

Word Map on EC 1.1.3.38

Reaction

Vanillyl alcohol
+
O2
=
Vanillin
 +
H2O2

Synonyms

4-allylphenol oxidase, 4-hydroxy-2-methoxybenzyl alcohol oxidase, Aryl-alcohol oxidase, EUGO, HMFO, Oxidase, vanillyl alcohol, RHA1_ro03282, vanillyl-alcohol oxidase, VAO, VAOA

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.38 vanillyl-alcohol oxidase

Engineering

Engineering on EC 1.1.3.38 - vanillyl-alcohol oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C470L
mutant displays similar activity to the wild-type enzyme with the substrates vanillyl alcohol, chavicol aund eugenol, but no activity with linear 4-alkylphenols
D170A
D170A/T457E
-
produces (S)-1-(4'-hydroxyphenyl)ethanol from 4-ethylphenol. The wild-type enzyme produces (R)-1-(4'-hydroxyphenyl)ethanol
D170E
D170N
D170S
D170S/T457E
-
produces (S)-1-(4'-hydroxyphenyl)ethanol from 4-ethylphenol. The wild-type enzyme produces (R)-1-(4'-hydroxyphenyl)ethanol
E502G
the octamer/dimer ratio is 1:10. The catalytic efficiency of the mutant is significantly increased for ortho-substituted 4-methylphenols
F424G
mutant does not contain any flavin after purification
F454Y
as for wild-type enzyme the octamer/dimer ratio of the mutant enzyme is 1.5:1. The catalytic efficiency of the mutant is significantly increased for ortho-substituted 4-methylphenols
H422A
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Mutant enzyme is still able to form a stable binary complex of reduced enzyme and a quinone methide product intermediate, a crucial step during vanillyl-alcohol oxidase-mediated catalysis. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD
H422C
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD
H422T
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD
I238T
the octamer/dimer ratio is 4:1. The catalytic efficiency of the mutant is significantly increased for ortho-substituted 4-methylphenols
I468V
mutant displays similar activity to the wild-type enzyme with the substrates vanillyl alcohol, chavicol aund eugenol, but no activity with linear 4-alkylphenols
L316M
mutant displays substrate specificity profile similar to wild-type
T457Q
mutant shows about 3fold increased activity towards vanillyl alcohol, but decrease in activity with all other substrates
T459I
mutant displays substrate specificity profile similar to wild-type
T505S
as for wild-type enzyme the octamer/dimer ratio of the mutant enzyme is 1.5:1
Y108F
deprotonation of the substrate's phenol group is impaired
Y108F/Y503F
deprotonation of the substrate's phenol group is impaired
Y503F
deprotonation of the substrate's phenol group is impaired
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