ISSN:
1432-072X
Schlagwort(e):
Key words Dehydrogenase
;
Eugenol
;
Purification
;
Flavocytochrome c
;
Pseudomonas fluorescens E118
;
Substrate specificity
;
4-Alkylphenol
;
4-Hydroxybenzyl alcohol
;
Electron acceptor
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
Notizen:
Abstract Pseudomonas fluorescens E118 was isolated from soil as an effective eugenol-degrading organism by a screening using eugenol as enrichment substrate. The first enzyme involved in the degradation of eugenol in this organism, eugenol dehydrogenase, was purified after induction by eugenol, and the purity of the enzyme was shown by SDS-PAGE and gel-permeation HLPC. The enzyme is a heterodimer that consists of a 10-kDa cytochrome c and a 58-kDa subunit. The larger subunit presumably contains flavin, suggesting a flavocytochrome c structure and an electron transfer via flavin and cytochrome c during dehydrogenation. The activity of the purified enzyme depended on the addition of a final electron acceptor such as phenazine methosulfate, 2,6-dichlorophenol-indophenol, cytochrome c, or potassium ferricyanide. The enzyme catalyzed the dehydrogenation of three different 4-hydroxybenzylic structures including the conversion of eugenol to coniferyl alcohol, 4-alkylphenols to 1-(4-hydroxyphenyl)alcohols, and 4-hydroxybenzylalcohols to the corresponding aldehydes. The catalytic and structural similarity between this enzyme and a Penicillium vanillyl-alcohol oxidase and 4-alkylphenol methylhydroxylases from several Pseudomonas species is discussed.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/s002030050675
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