| http://purl.uniprot.org/citations/9211715 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9211715 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9211715 | http://www.w3.org/2000/01/rdf-schema#comment | "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."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.org/dc/terms/identifier | "doi:10.1007/s002030050470"xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.org/dc/terms/identifier | "doi:10.1007/s002030050470"xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/author | "Birkeland N.K."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/author | "Birkeland N.K."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/author | "Lien T."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/author | "Lien T."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/author | "Steen I.H."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/author | "Steen I.H."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/author | "Langelandsvik A.S."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/author | "Langelandsvik A.S."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/name | "Arch. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/name | "Arch. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/pages | "59-67"xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/pages | "59-67"xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/title | "Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/title | "Properties and primary structure of a thermostable L-malate dehydrogenase from Archaeoglobus fulgidus."xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/volume | "168"xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://purl.uniprot.org/core/volume | "168"xsd:string |
| http://purl.uniprot.org/citations/9211715 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9211715 |
| http://purl.uniprot.org/citations/9211715 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9211715 |