Source:http://linkedlifedata.com/resource/pubmed/id/11479712
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2001-7-31
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pubmed:abstractText |
The initial steps in the anaerobic oxidation of the aromatic hydrocarbon ethylbenzene by denitrifying bacteria are two sequential dehydrogenation reactions of ethylbenzene to (S)-1-phenylethanol and further to acetophenone. The enzyme catalysing the second oxidation step, (S)-1-phenylethanol dehydrogenase, was analysed in the denitrifying bacterium Azoarcus sp. strain EbN1. An NAD+-dependent 1-phenylethanol dehydrogenase for each of the enantiomers of 1-phenylethanol was identified in this bacterium; the two enzymes were induced under different growth conditions. (S)-1-phenylethanol dehydrogenase from ethylbenzene-grown cells was purified and biochemically characterised. The enzyme is a typical secondary alcohol dehydrogenase and consists of two subunits of 25.5 kDa. The enantioselective enzyme catalyses the oxidation of (S)-1-phenylethanol or the reduction of acetophenone and is inhibited by high concentrations of (R)-1-phenylethanol. The enzyme exhibits low apparent K(m) values for (S)-1-phenylethanol and acetophenone and is rather substrate-specific, using only a few chemically similar secondary alcohols, such as 1-phenylpropanol and isopropanol.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-phenylethanol dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/2-Propanol,
http://linkedlifedata.com/resource/pubmed/chemical/Benzene Derivatives,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Propanols,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/ethylbenzene
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0302-8933
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
176
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
129-35
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11479712-2-Propanol,
pubmed-meshheading:11479712-Amino Acid Sequence,
pubmed-meshheading:11479712-Anaerobiosis,
pubmed-meshheading:11479712-Azoarcus,
pubmed-meshheading:11479712-Benzene Derivatives,
pubmed-meshheading:11479712-Catalysis,
pubmed-meshheading:11479712-Isoenzymes,
pubmed-meshheading:11479712-Kinetics,
pubmed-meshheading:11479712-Molecular Sequence Data,
pubmed-meshheading:11479712-Molecular Weight,
pubmed-meshheading:11479712-Oxidoreductases,
pubmed-meshheading:11479712-Propanols,
pubmed-meshheading:11479712-Protein Subunits,
pubmed-meshheading:11479712-Sequence Alignment,
pubmed-meshheading:11479712-Substrate Specificity
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pubmed:year |
2001
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pubmed:articleTitle |
(S)-1-phenylethanol dehydrogenase of Azoarcus sp. strain EbN1, an enzyme of anaerobic ethylbenzene catabolism.
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pubmed:affiliation |
Max Planck Institute for Marine Microbiology, Celsiusstrasse 1, 28359 Bremen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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