| http://purl.uniprot.org/citations/9325430 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9325430 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/9325430 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/9325430 | http://www.w3.org/2000/01/rdf-schema#comment | "A thermostable homodimeric isocitrate dehydrogenase from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus was purified and characterized. The mol. mass of the isocitrate dehydrogenase subunit was 42 kDa as determined by SDS-PAGE. Following separation by SDS-PAGE, A. fulgidus isocitrate dehydrogenase could be renatured and detected in situ by activity staining. The enzyme showed dual coenzyme specificity with a high preference for NADP+. Optimal temperature for activity was 90 degrees C or above, and a half-life of 22 min was found for the enzyme when incubated at 90 degrees C in a 50 mM Tricine-KOH buffer (pH 8.0). Based on the N-terminal amino acid sequence, the gene encoding the isocitrate dehydrogenase was cloned. DNA sequencing identified the icd gene as an open reading frame encoding a protein of 412 amino acids with a molecular mass corresponding to that determined for the purified enzyme. The deduced amino acid sequence closely resembled that of the isocitrate dehydrogenase from the archaeon Caldococcus noboribetus (59% identity) and bacterial isocitrate dehydrogenases, with 57% identity with isocitrate dehydrogenase from Escherichia coli. All the amino acid residues directly contacting substrate and coenzyme (except Ile-320) in E. coli isocitrate dehydrogenase are conserved in the enzyme from A. fulgidus. The primary structure of A. fulgidus isocitrate dehydrogenase confirmes the presence of Bacteria-type isocitrate dehydrogenases among Archaea. Multiple alignment of all the available amino acid sequences of di- and multimeric isocitrate dehydrogenases from the three domains of life shows that they can be divided into three distinct phylogenetic groups."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/name | "Arch. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/name | "Arch. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.org/dc/terms/identifier | "doi:10.1007/s002030050516"xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.org/dc/terms/identifier | "doi:10.1007/s002030050516"xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9325430 |
| http://purl.uniprot.org/citations/9325430 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9325430 |
| http://purl.uniprot.org/citations/9325430 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/9325430 |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/author | "Birkeland N.-K."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/author | "Birkeland N.-K."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/author | "Lien T."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/author | "Lien T."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/author | "Steen I.H."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/author | "Steen I.H."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/date | "1997"xsd:gYear |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/pages | "412-420"xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/pages | "412-420"xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/title | "Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/title | "Biochemical and phylogenetic characterization of isocitrate dehydrogenase from a hyperthermophilic archaeon, Archaeoglobus fulgidus."xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/volume | "168"xsd:string |
| http://purl.uniprot.org/citations/9325430 | http://purl.uniprot.org/core/volume | "168"xsd:string |