Literature summary for 1.1.3.38 extracted from

Mattevi, A.; Fraaije, M.W.; Mozzarelli, A.; Olivi, L.; Coda, A.; van Berkel, W.J.H.
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity (1997), Structure, 5, 907-920.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the enzyme in the native state and in complexes with the four inhibitors p-cresol, isoeugenol, 2-nitro-p-cresol and heptenyl-phenol	Penicillium simplicissimum

Inhibitors

Inhibitors	Comment	Organism	Structure
2-Nitro-p-cresol	-	Penicillium simplicissimum
4-(1-Heptenyl)-phenol	the crystal structure of the enzyme in complex with the inhibitor shows that the catalytic cavity is completely filled by the inhibitor	Penicillium simplicissimum
isoeugenol	-	Penicillium simplicissimum
p-Cresol	-	Penicillium simplicissimum

Organism

Organism	UniProt	Comment	Textmining
Penicillium simplicissimum	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
Vanillyl alcohol + O2 = vanillin + H2O2	the shape of the active-site cavity controls substrate specificity by providing a size exclusion mechanism. Inside the cavity the substrate aromatic ring is positioned at an angle of 18° to the flavin ring	Penicillium simplicissimum	a

Cofactor

Cofactor	Comment	Organism	Structure
FAD	protein-bound	Penicillium simplicissimum

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Release 2023.1 (January 2023)