| pubmed-article:11286887 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11286887 | lifeskim:mentions | umls-concept:C0003732 | lld:lifeskim |
| pubmed-article:11286887 | lifeskim:mentions | umls-concept:C0017713 | lld:lifeskim |
| pubmed-article:11286887 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11286887 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11286887 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11286887 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:11286887 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11286887 | pubmed:dateCreated | 2001-7-11 | lld:pubmed |
| pubmed-article:11286887 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11286887 | pubmed:abstractText | ATP is the most common phosphoryl group donor for kinases. However, certain hyperthermophilic archaea such as Thermococcus litoralis and Pyrococcus furiosus utilize unusual ADP-dependent glucokinases and phosphofructokinases in their glycolytic pathways. These ADP-dependent kinases are homologous to each other but show no sequence similarity to any of the hitherto known ATP-dependent enzymes. | lld:pubmed |
| pubmed-article:11286887 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11286887 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11286887 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11286887 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11286887 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11286887 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:11286887 | pubmed:author | pubmed-author:ItoSS | lld:pubmed |
| pubmed-article:11286887 | pubmed:author | pubmed-author:KogaSS | lld:pubmed |
| pubmed-article:11286887 | pubmed:author | pubmed-author:MatsuzawaHH | lld:pubmed |
| pubmed-article:11286887 | pubmed:author | pubmed-author:YoshiokaII | lld:pubmed |
| pubmed-article:11286887 | pubmed:author | pubmed-author:WakagiTT | lld:pubmed |
| pubmed-article:11286887 | pubmed:author | pubmed-author:FushinobuSS | lld:pubmed |
| pubmed-article:11286887 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11286887 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:11286887 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:11286887 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11286887 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11286887 | pubmed:pagination | 205-14 | lld:pubmed |
| pubmed-article:11286887 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11286887 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11286887 | pubmed:articleTitle | Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon. | lld:pubmed |
| pubmed-article:11286887 | pubmed:affiliation | Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-Ku, Tokyo 113-8657, Japan. | lld:pubmed |
| pubmed-article:11286887 | pubmed:publicationType | Journal Article | lld:pubmed |
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