| pubmed-article:17127057 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17127057 | lifeskim:mentions | umls-concept:C0007028 | lld:lifeskim |
| pubmed-article:17127057 | lifeskim:mentions | umls-concept:C0022173 | lld:lifeskim |
| pubmed-article:17127057 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:17127057 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:17127057 | lifeskim:mentions | umls-concept:C0182324 | lld:lifeskim |
| pubmed-article:17127057 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:17127057 | pubmed:dateCreated | 2007-1-22 | lld:pubmed |
| pubmed-article:17127057 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17127057 | pubmed:abstractText | The activation of the metalloenzyme carbonic anhydrase (CA, EC 4.2.1.1) with L-adrenaline and histamine has been investigated by kinetic and X-ray crystallographic studies. L-Adrenaline behaves as a potent activator of isozyme CA I (activation constant of 90 nM), being a much weaker activator of isozyme CA II (activation constant of 96 microM). Isoforms CA IV, VA, VII, and XIV were activated by L-adrenaline with K(A)s in the range of 36-63 microM. The X-ray crystal structure of the CA II-L-adrenaline adduct revealed that the activator plugs the entrance of the active site cavity, obstructing it almost completely. | lld:pubmed |
| pubmed-article:17127057 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17127057 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17127057 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17127057 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17127057 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17127057 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17127057 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17127057 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17127057 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17127057 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17127057 | pubmed:issn | 0960-894X | lld:pubmed |
| pubmed-article:17127057 | pubmed:author | pubmed-author:ScozzafavaAnd... | lld:pubmed |
| pubmed-article:17127057 | pubmed:author | pubmed-author:SupuranClaudi... | lld:pubmed |
| pubmed-article:17127057 | pubmed:author | pubmed-author:TemperiniClau... | lld:pubmed |
| pubmed-article:17127057 | pubmed:author | pubmed-author:Mastrolorenzo... | lld:pubmed |
| pubmed-article:17127057 | pubmed:author | pubmed-author:InnocentiAles... | lld:pubmed |
| pubmed-article:17127057 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17127057 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:17127057 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:17127057 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17127057 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17127057 | pubmed:pagination | 628-35 | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:meshHeading | pubmed-meshheading:17127057... | lld:pubmed |
| pubmed-article:17127057 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17127057 | pubmed:articleTitle | Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV. | lld:pubmed |
| pubmed-article:17127057 | pubmed:affiliation | Università degli Studi di Firenze, Laboratorio di Chimica Bioinorganica, Rm. 188, Via della Lastruccia 3, I-50019 Sesto Fiorentino (Firenze), Italy. | lld:pubmed |
| pubmed-article:17127057 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17127057 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:17127057 | lld:chembl |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17127057 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17127057 | lld:pubmed |
