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

BRENDA support

Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.38 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

EC Number Inhibitors Comment Organism Structure
1.1.3.38 2-Nitro-p-cresol
-
Penicillium simplicissimum
1.1.3.38 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
1.1.3.38 isoeugenol
-
Penicillium simplicissimum
1.1.3.38 p-Cresol
-
Penicillium simplicissimum

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.38 Penicillium simplicissimum
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.38 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

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.38 FAD protein-bound Penicillium simplicissimum