| pubmed-article:15063312 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15063312 | lifeskim:mentions | umls-concept:C1056478 | lld:lifeskim |
| pubmed-article:15063312 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:15063312 | lifeskim:mentions | umls-concept:C0003995 | lld:lifeskim |
| pubmed-article:15063312 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:15063312 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:15063312 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:15063312 | lifeskim:mentions | umls-concept:C0062094 | lld:lifeskim |
| pubmed-article:15063312 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:15063312 | pubmed:dateCreated | 2004-4-5 | lld:pubmed |
| pubmed-article:15063312 | pubmed:abstractText | Fluoroacetate dehalogenase from Moraxella sp. B (FAc-DEX) catalyzes cleavage of the carbon-fluorine bond of fluoroacetate, whose dissociation energy is among the highest found in natural products. Asp105 functions as the catalytic nucleophile that attacks the alpha-carbon atom of the substrate to displace the fluorine atom. In spite of the essential role of Asp105, we found that site-directed mutagenesis to replace Asp105 by Asn does not result in total inactivation of the enzyme. The activity of the mutant enzyme increased in a time- and temperature-dependent manner. We analyzed the enzyme by ion-spray mass spectrometry and found that the reactivation was caused by the hydrolytic deamidation of Asn105 to generate the wild-type enzyme. Unlike Asn10 of the l-2-haloacid dehalogenase (L-DEX YL) D10N mutant, Asn105 of the fluoroacetate dehalogenase D105N mutant did not function as a nucleophile to catalyze the dehalogenation. | lld:pubmed |
| pubmed-article:15063312 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15063312 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15063312 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15063312 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15063312 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15063312 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15063312 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15063312 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15063312 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15063312 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15063312 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:15063312 | pubmed:author | pubmed-author:EsakiNobuyosh... | lld:pubmed |
| pubmed-article:15063312 | pubmed:author | pubmed-author:KuriharaTatsu... | lld:pubmed |
| pubmed-article:15063312 | pubmed:author | pubmed-author:KawasakiHaruh... | lld:pubmed |
| pubmed-article:15063312 | pubmed:author | pubmed-author:IchiyamaSusum... | lld:pubmed |
| pubmed-article:15063312 | pubmed:author | pubmed-author:TsunasawaSusu... | lld:pubmed |
| pubmed-article:15063312 | pubmed:author | pubmed-author:KogureYoshifu... | lld:pubmed |
| pubmed-article:15063312 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15063312 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:15063312 | pubmed:volume | 1698 | lld:pubmed |
| pubmed-article:15063312 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15063312 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15063312 | pubmed:pagination | 27-36 | lld:pubmed |
| pubmed-article:15063312 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15063312 | pubmed:meshHeading | pubmed-meshheading:15063312... | lld:pubmed |
| pubmed-article:15063312 | pubmed:meshHeading | pubmed-meshheading:15063312... | lld:pubmed |
| pubmed-article:15063312 | pubmed:meshHeading | pubmed-meshheading:15063312... | lld:pubmed |
| pubmed-article:15063312 | pubmed:meshHeading | pubmed-meshheading:15063312... | lld:pubmed |
| pubmed-article:15063312 | pubmed:meshHeading | pubmed-meshheading:15063312... | lld:pubmed |
| pubmed-article:15063312 | pubmed:meshHeading | pubmed-meshheading:15063312... | lld:pubmed |
| pubmed-article:15063312 | pubmed:meshHeading | pubmed-meshheading:15063312... | lld:pubmed |
| pubmed-article:15063312 | pubmed:meshHeading | pubmed-meshheading:15063312... | lld:pubmed |
| pubmed-article:15063312 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15063312 | pubmed:articleTitle | Reactivity of asparagine residue at the active site of the D105N mutant of fluoroacetate dehalogenase from Moraxella sp. B. | lld:pubmed |
| pubmed-article:15063312 | pubmed:affiliation | Laboratory of Microbial Biochemistry, Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan. | lld:pubmed |
| pubmed-article:15063312 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15063312 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15063312 | lld:pubmed |
