| pubmed-article:9211715 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9211715 | lifeskim:mentions | umls-concept:C0524829 | lld:lifeskim |
| pubmed-article:9211715 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:9211715 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9211715 | lifeskim:mentions | umls-concept:C0205225 | lld:lifeskim |
| pubmed-article:9211715 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:9211715 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:9211715 | pubmed:dateCreated | 1997-9-18 | lld:pubmed |
| pubmed-article:9211715 | pubmed:abstractText | A thermostable l-malate dehydrogenase from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus was isolated and characterized, and its gene was cloned and sequenced. The enzyme is a homodimer with a molecular mass of 70 kDa and catalyzes preferentially the reduction of oxaloacetic acid with NADH. A. fulgidus L-malate dehydrogenase was stable for 5 h at 90 degrees C, and the half-life at 101 degrees C was 80 min. Thus, A. fulgidus L-malate dehydrogenase is the most thermostable L-malate dehydrogenase characterized to date. Addition of K2HPO4 (1 M) increased the thermal stability by 40%. The primary structure shows a high similarity to L-lactate dehydrogenase from Thermotoga maritima and gram-positive bacteria, and to L-malate dehydrogenase from the archaeon Haloarcula marismortui and other L-lactate-dehydrogenase-like L-malate dehydrogenases. | lld:pubmed |
| pubmed-article:9211715 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9211715 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9211715 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9211715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9211715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9211715 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9211715 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9211715 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:9211715 | pubmed:issn | 0302-8933 | lld:pubmed |
| pubmed-article:9211715 | pubmed:author | pubmed-author:LienTT | lld:pubmed |
| pubmed-article:9211715 | pubmed:author | pubmed-author:BirkelandN... | lld:pubmed |
| pubmed-article:9211715 | pubmed:author | pubmed-author:Langelandsvik... | lld:pubmed |
| pubmed-article:9211715 | pubmed:author | pubmed-author:SteenI HIH | lld:pubmed |
| pubmed-article:9211715 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9211715 | pubmed:volume | 168 | lld:pubmed |
| pubmed-article:9211715 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9211715 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9211715 | pubmed:pagination | 59-67 | lld:pubmed |
| pubmed-article:9211715 | pubmed:dateRevised | 2000-12-18 | lld:pubmed |
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| pubmed-article:9211715 | pubmed:meshHeading | pubmed-meshheading:9211715-... | lld:pubmed |
| pubmed-article:9211715 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9211715 | pubmed:articleTitle | Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus. | lld:pubmed |
| pubmed-article:9211715 | pubmed:affiliation | Department of Microbiology, University of Bergen, Jahnebakken 5, N-5020 Bergen, Norway. | lld:pubmed |
| pubmed-article:9211715 | pubmed:publicationType | Journal Article | lld:pubmed |
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