Substrate specificity of catechol oxidase from Lycopus europaeus and characterization of the bioproducts of enzymic caffeic acid oxidation 1

FEBS Letters

Magrini, Annette¹  Meiwes, Dirk²  Krebs, Bernt¹  Büldt-Karentzopoulos, Klaudia¹  Fischer, Helmut²  Rompel, Annette¹  Eicken, Christoph¹  Gerdemann, Carsten¹ 

[1] Anorganisch-Chemisches Institut der Universität Münster, Wilhelm-Klemm-Str. 8, 48149 Münster, Germany;Institut für Biochemie der Universität Münster, 48149 Münster, Germany

关键词: Type 3 copper center;    Caffeic acid;    Enzyme kinetic;    Polyphenol oxidase;    Lignan;   

DOI  :  10.1016/S0014-5793(99)00106-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown