| pubmed-article:9541402 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9541402 | lifeskim:mentions | umls-concept:C0004595 | lld:lifeskim |
| pubmed-article:9541402 | lifeskim:mentions | umls-concept:C0047519 | lld:lifeskim |
| pubmed-article:9541402 | lifeskim:mentions | umls-concept:C0442805 | lld:lifeskim |
| pubmed-article:9541402 | lifeskim:mentions | umls-concept:C0015219 | lld:lifeskim |
| pubmed-article:9541402 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:9541402 | lifeskim:mentions | umls-concept:C0031082 | lld:lifeskim |
| pubmed-article:9541402 | lifeskim:mentions | umls-concept:C1517004 | lld:lifeskim |
| pubmed-article:9541402 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:9541402 | pubmed:dateCreated | 1998-5-14 | lld:pubmed |
| pubmed-article:9541402 | pubmed:abstractText | We improved the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by an in vivo evolutionary technique using an extreme thermophile, Thermus thermophilus, as a host cell. The leuB gene encoding B. subtilis 3-isopropylmalate dehydrogenase was integrated into the chromosome of a leuB-deficient strain of T. thermophilus. The resulting transformant showed a leucine-autotrophy at 56 degrees C but not at 61 degrees C and above. Phenotypically thermostabilized strains that can grow at 61 degrees C without leucine were isolated from spontaneous mutants. Screening temperature was stepwise increased from 61 to 66 and then to 70 degrees C and mutants that showed a leucine-autotrophic growth at 70 degrees C were obtained. DNA sequence analyses of the leuB genes from the mutant strains revealed three stepwise amino acid replacements, threonine-308 to isoleucine, isoleucine-95 to leucine, and methionine-292 to isoleucine. The mutant enzymes with these amino acid replacements were more stable against heat treatment than the wild-type enzyme. Furthermore, the triple-mutant enzyme showed significantly higher specific activity than that of the wild-type enzyme. | lld:pubmed |
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| pubmed-article:9541402 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9541402 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9541402 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9541402 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9541402 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:9541402 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:9541402 | pubmed:author | pubmed-author:TanakaNN | lld:pubmed |
| pubmed-article:9541402 | pubmed:author | pubmed-author:OshimaTT | lld:pubmed |
| pubmed-article:9541402 | pubmed:author | pubmed-author:YamagishiAA | lld:pubmed |
| pubmed-article:9541402 | pubmed:author | pubmed-author:AkanumaSS | lld:pubmed |
| pubmed-article:9541402 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9541402 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:9541402 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9541402 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9541402 | pubmed:pagination | 698-705 | lld:pubmed |
| pubmed-article:9541402 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:9541402 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9541402 | pubmed:articleTitle | Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. | lld:pubmed |
| pubmed-article:9541402 | pubmed:affiliation | Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Horinouchi, Hachioji, Japan. akanuma@ls.toyaku.ac.jp | lld:pubmed |
| pubmed-article:9541402 | pubmed:publicationType | Journal Article | lld:pubmed |
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