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Substrate specificity of catechol oxidase from Lycopus europaeus and characterization of the bioproducts of enzymic caffeic acid oxidation 1
Author(s) -
Rompel Annette,
Fischer Helmut,
Meiwes Dirk,
Büldt-Karentzopoulos Klaudia,
Magrini Annette,
Eicken Christoph,
Gerdemann Carsten,
Krebs Bernt
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00106-4
Subject(s) - catechol , caffeic acid , chemistry , catechol oxidase , tyrosinase , phenols , polyphenol oxidase , substrate (aquarium) , oxidase test , caffeic acid phenethyl ester , stereochemistry , enzyme , organic chemistry , nuclear chemistry , antioxidant , biology , peroxidase , ecology
The substrate specificity of catechol oxidase from Lycopus europaeus towards phenols is examined. The enzyme catalyzes the oxidation of o ‐diphenols to o ‐quinones without hydroxylating monophenols, the additional activity of tyrosinase. Substrates containing a ‐COOH group are inhibitors for catechol oxidase. The products of enzymic oxidation of caffeic acid were analyzed and isolated by HPLC with diode array detection. The neolignans of the 2,3‐dihydro‐1,4‐benzodioxin type (3, 6–8), 6,7‐dihydroxy‐1‐(3,4‐dihydroxyphenyl)‐2,3‐dicarboxy‐1,2‐dihydronaphthaline (1) 6,7‐dihydroxy‐1‐(3,4‐dihydroxyphenyl)‐3‐carboxynaphthaline (5) and 2,6‐bis‐(3′,4′‐dihydroxyphenyl)‐1‐carboxy‐3‐oxacyclo‐(3,0)‐pentan‐2‐on‐1‐ene (4) were formed. A reaction mechanism for the formation of (1, 4 and 5) is discussed.