Linked Life Data

10075640

Source:http://linkedlifedata.com/resource/pubmed/id/10075640

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1999-3-9
pubmed:abstractText
We isolated a eugenol-degrading bacterium, Pseudomonas fluorescens E118. This strain produced a novel enzyme, eugenol dehydrogenase, which catalyzes the conversion of eugenol into coniferyl alcohol. The enzyme was purified from the eugenol-induced cells of P. fluorescens E118. The purified enzyme appeared to be homogeneous, judging from the analysis of polyacrylamide gel electrophoresis. The enzyme was a 68-kDa protein composed of two different subunits (alpha subunit, 10 kDa; and beta subunit, 58 kDa). The enzyme exhibited a cytochrome c-like absorption spectrum. The alpha subunit corresponded to cytochrome c. The enzyme catalyzed the dehydrogenation of 4-alkylphenol into the corresponding alkyl 1-(4-hydroxyphenyl)-alcohol derivatives. The reaction products were isolated and identified physicochemically. The enzyme catalyzed the enantioselective hydroxylation of p-alkylphenols. p-Ethylphenol and p-propylphenol were converted to S-(-)-p-(1-hydroxyphenyl)ethanol and S-(-)-p(1-hydroxyphenyl)propanol, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
864
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
81-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Novel double bond-transferring hydroxylation reaction involved in microbial metabolism of eugenol.
pubmed:affiliation
Department of Biomolecular Science, Gifu University, Japan.
pubmed:publicationType
Journal Article