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
-
1.1.3.38
-
opacification
-
simplicissimum
-
ostium
-
veratryl
-
flavinylation
-
vertebrobasilar
-
aphakia
-
p-quinone
-
logmar
-
argan
-
4-ethylphenol
-
4-alkylphenols
-
synthesis
-
analysis
- 1.1.3.38
-
opacification
- simplicissimum
-
ostium
-
veratryl
-
flavinylation
-
vertebrobasilar
- aphakia
- p-quinone
-
logmar
-
argan
- 4-ethylphenol
- 4-alkylphenols
- synthesis
- analysis
Reaction
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
Advanced search results
General Information
General Information 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.
metabolism
identification of a gated entry and exit path at the subunit interface of VAO for small phenolic ligands. The residues Met192, Met195 and Glu464 form a portal in this path. Residues His466 and Tyr503 act as concierges, obstructing the path to the active site for phenolic substrates once substrate is bound. An additional, different entry and exit path for dioxygen and hydrogen peroxide at the interface of the two domains of VAO exists. Tyr51 in this path could assist reduced flavin oxidation in VAO
metabolism
tyrosine residues Tyr-108 and Tyr-503 are positioned to facilitate deprotonation of substrate's phenol groups. The reduction of VAOA by chavicol or vanillyl alcohol occurs at two different rates: kobs1, which corresponds to its reaction with the deprotonated form of the substrate, and kobs2, which corresponds to its reaction with the protonated form of the substrate. In mutants Y108F, Y503F, and Y108F/Y503F, the relative contribution of kobs2 to the reduction is larger than in wild-type VAOA