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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1996-2-1
|
| pubmed:abstractText |
Analysis of a crystal structure of alcohol dehydrogenase (Adh) from horse liver suggests that Trp54 in the homologous yeast alcohol dehydrogenase prevents the yeast enzyme from efficiently catalysing the oxidation of long-chain primary alcohols with branching at the 4 position (e.g. 4-methyl-1-pentanol, cinnamyl alcohol). This residue has been altered to Leu by site-directed mutagenesis. The alteration yields an enzyme that serves as an effective catalyst for both longer straight-chain primary alcohols and branched chain alcohols.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
0269-2139
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
8
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
457-61
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8532667-Alcohol Dehydrogenase,
pubmed-meshheading:8532667-Alcohols,
pubmed-meshheading:8532667-Binding Sites,
pubmed-meshheading:8532667-Kinetics,
pubmed-meshheading:8532667-Leucine,
pubmed-meshheading:8532667-Mutagenesis, Site-Directed,
pubmed-meshheading:8532667-Protein Engineering,
pubmed-meshheading:8532667-Saccharomyces cerevisiae,
pubmed-meshheading:8532667-Substrate Specificity,
pubmed-meshheading:8532667-Tryptophan
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Engineering yeast alcohol dehydrogenase. Replacing Trp54 by Leu broadens substrate specificity.
|
| pubmed:affiliation |
Department of Chemistry, ETH, Zurich, Switzerland.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|