pubmed-article:15487948 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:15487948 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:15487948 | lifeskim:mentions | umls-concept:C0005553 | lld:lifeskim |
pubmed-article:15487948 | lifeskim:mentions | umls-concept:C1707391 | lld:lifeskim |
pubmed-article:15487948 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:15487948 | lifeskim:mentions | umls-concept:C1707689 | lld:lifeskim |
pubmed-article:15487948 | pubmed:dateCreated | 2004-10-18 | lld:pubmed |
pubmed-article:15487948 | pubmed:abstractText | The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase. | lld:pubmed |
pubmed-article:15487948 | pubmed:language | eng | lld:pubmed |
pubmed-article:15487948 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15487948 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:15487948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15487948 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:15487948 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:15487948 | pubmed:issn | 0066-4227 | lld:pubmed |
pubmed-article:15487948 | pubmed:author | pubmed-author:VettingMatthe... | lld:pubmed |
pubmed-article:15487948 | pubmed:author | pubmed-author:EarhartCathle... | lld:pubmed |
pubmed-article:15487948 | pubmed:author | pubmed-author:OhlendorfDoug... | lld:pubmed |
pubmed-article:15487948 | pubmed:author | pubmed-author:BrownC KentCK | lld:pubmed |
pubmed-article:15487948 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:15487948 | pubmed:volume | 58 | lld:pubmed |
pubmed-article:15487948 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:15487948 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:15487948 | pubmed:pagination | 555-85 | lld:pubmed |
pubmed-article:15487948 | pubmed:meshHeading | pubmed-meshheading:15487948... | lld:pubmed |
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pubmed-article:15487948 | pubmed:year | 2004 | lld:pubmed |
pubmed-article:15487948 | pubmed:articleTitle | Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1. | lld:pubmed |
pubmed-article:15487948 | pubmed:affiliation | Center for Metals in Biocatalysis and Department of Biochemistry, Molecular Biology, and Biophysics , Minneapolis, Minnesota 55455, USA. brow0927@umn.edu | lld:pubmed |
pubmed-article:15487948 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:15487948 | pubmed:publicationType | Review | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15487948 | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15487948 | lld:pubmed |