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| pubmed-article:11704672 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:11704672 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:11704672 | lifeskim:mentions | umls-concept:C0768183 | lld:lifeskim |
| pubmed-article:11704672 | lifeskim:mentions | umls-concept:C0053241 | lld:lifeskim |
| pubmed-article:11704672 | lifeskim:mentions | umls-concept:C0039894 | lld:lifeskim |
| pubmed-article:11704672 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11704672 | pubmed:dateCreated | 2002-1-21 | lld:pubmed |
| pubmed-article:11704672 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11704672 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11704672 | pubmed:abstractText | The crystal structure of a quinohemoprotein amine dehydrogenase from Pseudomonas putida has been determined at 1.9-A resolution. The enzyme comprises three non-identical subunits: a four-domain alpha-subunit that harbors a di-heme cytochrome c, a seven-bladed beta-propeller beta-subunit that provides part of the active site, and a small gamma-subunit that contains a novel cross-linked, proteinous quinone cofactor, cysteine tryptophylquinone. More surprisingly, the catalytic gamma-subunit contains three additional chemical cross-links that encage the cysteine tryptophylquinone cofactor, involving a cysteine side chain bridged to either an Asp or Glu residue all in a hitherto unknown thioether bonding with a methylene carbon atom of acidic amino acid side chains. Thus, the structure of the 79-residue gamma-subunit is quite unusual, containing four internal cross-links in such a short polypeptide chain that would otherwise be difficult to fold into a globular structure. | lld:pubmed |
| pubmed-article:11704672 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11704672 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11704672 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11704672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11704672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11704672 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11704672 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11704672 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:MiyaharaIkuko... | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:HirotsuKenK | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:SatohAtsukoA | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:KimJong-KeunJ... | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:DevreeseBartB | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:VandenbergheI... | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:Hacisalihoglu... | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:OkajimaToshih... | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:KurodaShun'ic... | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:AdachiOsaoO | lld:pubmed |
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| pubmed-article:11704672 | pubmed:author | pubmed-author:Van... | lld:pubmed |
| pubmed-article:11704672 | pubmed:author | pubmed-author:TanizawaKatsu... | lld:pubmed |
| pubmed-article:11704672 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11704672 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:11704672 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11704672 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11704672 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11704672 | pubmed:pagination | 2830-4 | lld:pubmed |
| pubmed-article:11704672 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:11704672 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11704672 | pubmed:articleTitle | Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas putida. Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges. | lld:pubmed |
| pubmed-article:11704672 | pubmed:affiliation | Department of Chemistry, Graduate School of Science, Osaka City University, Osaka 558-8585, Japan. | lld:pubmed |
| pubmed-article:11704672 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11704672 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| family:PF08992.6 | family:pubmed | pubmed-article:11704672 | lld:pfam |
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