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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1984-11-1
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pubmed:abstractText |
The NAD-dependent oxidation of ethanol, 2,3-butanediol, and other primary and secondary alcohols, catalyzed by alcohol dehydrogenases derived from Penicillium charlesii, was investigated. Alcohol dehydrogenase, ADH-I, was purified to homogeneity in a yield of 54%. The enzyme utilizes several primary alcohols as substrates, with Km values of the order of 10(-4) M. A Km value of 60 mM was obtained for R,R,-2,3-butanediol. The stereospecificity of the oxidation of 2-butanol was investigated, and S-(+)-2-butanol was found to be oxidized 2.4 times faster than was R-(-)-2-butanol. The reduction of 2-butanone was shown to produce S-(+)-2-butanol and R-(-)-butanol in a ratio of 7:3. ADH-I is the primary isozyme of alcohol dehydrogenase present in cultures utilizing glucose as the sole carbon source. The level of alcohol dehydrogenase activity increased 7.6-fold in mycelia from cultures grown with glucose and 2,3-butanediol (0.5%) as carbon sources compared with the activity in cultures grown on only glucose. Two additional forms of alcohol dehydrogenase, ADH-II and ADH-III, were present in the cultures supplemented with 2,3-butanediol. These forms of alcohol dehydrogenase catalyze the oxidation of ethanol and 2,3-butanediol. These data suggest that P. charlesii carries out an oxidation of 2,3-butanediol which may constitute the first reaction in the degradation of 2,3-butanediol as well as the last reaction in the mixed-acid fermentation. Alcohol dehydrogenase activities in P. charlesii may be encoded by multiple genes, one which is expressed constitutively and others whose expression is inducible by 2,3-butanediol.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2,3-butylene glycol,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Butylene Glycols,
http://linkedlifedata.com/resource/pubmed/chemical/Ethanol,
http://linkedlifedata.com/resource/pubmed/chemical/NAD
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
233
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
447-56
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6385855-Alcohol Dehydrogenase,
pubmed-meshheading:6385855-Alcohol Oxidoreductases,
pubmed-meshheading:6385855-Butylene Glycols,
pubmed-meshheading:6385855-Catalysis,
pubmed-meshheading:6385855-Chemical Phenomena,
pubmed-meshheading:6385855-Chemistry,
pubmed-meshheading:6385855-Ethanol,
pubmed-meshheading:6385855-Fermentation,
pubmed-meshheading:6385855-Kinetics,
pubmed-meshheading:6385855-Molecular Weight,
pubmed-meshheading:6385855-NAD,
pubmed-meshheading:6385855-Penicillium,
pubmed-meshheading:6385855-Stereoisomerism,
pubmed-meshheading:6385855-Substrate Specificity
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pubmed:year |
1984
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pubmed:articleTitle |
Occurrence of multiple forms of alcohol dehydrogenase in Penicillium supplemented with 2,3-butanediol.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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