| pubmed-article:8461298 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8461298 | lifeskim:mentions | umls-concept:C0079870 | lld:lifeskim |
| pubmed-article:8461298 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:8461298 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:8461298 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:8461298 | lifeskim:mentions | umls-concept:C0650756 | lld:lifeskim |
| pubmed-article:8461298 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:8461298 | pubmed:dateCreated | 1993-5-5 | lld:pubmed |
| pubmed-article:8461298 | pubmed:abstractText | Amino acid sequence comparisons reveal that tyrosine-152 and lysine-156 of Drosophila alcohol dehydrogenase (ADH) are conserved in homologous dehydrogenases, suggesting that these residues are important in catalysis. To test this hypothesis, we used site-directed mutagenesis to substitute tyrosine-152 with phenylalanine, histidine, or glutamic acid or to substitute lysine-156 with isoleucine. All of these mutants are catalytically inactive. Two mutants were active: A cysteine mutation of tyrosine-152 has 0.25% of wild-type ADH activity, while an arginine substitution of lysine-156 retains 2.2% of wild-type ADH activity. Kinetic analysis shows that the cysteine mutant increases Km(ethanol) 56-fold and Km(propan-2-ol) 100-fold, while Km(NAD) values are essentially unaltered. The arginine mutant also shows the significant enlargement of Km(ethanol), but not of Km(NAD). Furthermore, the cysteine mutant and arginine mutant have different substrate specificity and behave differently on competitive inhibition than wild-type ADH. These results suggest that both tyrosine-152 and lysine-156 have essential roles in catalysis by Drosophila ADH. | lld:pubmed |
| pubmed-article:8461298 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8461298 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8461298 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8461298 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8461298 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8461298 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:8461298 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8461298 | pubmed:author | pubmed-author:LeeW RWR | lld:pubmed |
| pubmed-article:8461298 | pubmed:author | pubmed-author:ChefRR | lld:pubmed |
| pubmed-article:8461298 | pubmed:author | pubmed-author:BakerM EME | lld:pubmed |
| pubmed-article:8461298 | pubmed:author | pubmed-author:ChangS HSH | lld:pubmed |
| pubmed-article:8461298 | pubmed:author | pubmed-author:LinZ GZG | lld:pubmed |
| pubmed-article:8461298 | pubmed:author | pubmed-author:JiangJ CJC | lld:pubmed |
| pubmed-article:8461298 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8461298 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:8461298 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8461298 | pubmed:geneSymbol | nodG | lld:pubmed |
| pubmed-article:8461298 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8461298 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8461298 | pubmed:pagination | 3342-6 | lld:pubmed |
| pubmed-article:8461298 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8461298 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8461298 | pubmed:articleTitle | Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. | lld:pubmed |
| pubmed-article:8461298 | pubmed:affiliation | Department of Biochemistry, Louisiana State University, Baton Rouge 70803. | lld:pubmed |
| pubmed-article:8461298 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8461298 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:3771877 | entrezgene:pubmed | pubmed-article:8461298 | lld:entrezgene |
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