| pubmed-article:13129355 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:13129355 | lifeskim:mentions | umls-concept:C1999216 | lld:lifeskim |
| pubmed-article:13129355 | lifeskim:mentions | umls-concept:C0068813 | lld:lifeskim |
| pubmed-article:13129355 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:13129355 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:13129355 | lifeskim:mentions | umls-concept:C1313069 | lld:lifeskim |
| pubmed-article:13129355 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:13129355 | pubmed:dateCreated | 2003-9-17 | lld:pubmed |
| pubmed-article:13129355 | pubmed:abstractText | Nitrile hydratase (NHase) is a non-heme iron or non-corrin cobalt enzyme having two post-translationally modified ligand residues, cysteine-sulfinic acid (alphaCys112-SO(2)H) and -sulfenic acid (alphaCys114-SOH). We studied the interaction between Fe-type NHase and isobutyronitrile (iso-BN) which had been reported as a competitive inhibitor with a K(i) value of 5 microM. From detailed kinetic studies of the inhibitory effect of iso-BN on Fe-type NHase, we found that authentic iso-BN was hydrated normally and that the impurity present in commercially available iso-BN inhibited NHase activity strongly. The inhibitory compound induced significant changes in the UV-vis absorption spectrum of NHase, suggesting its interaction with the iron center. This compound was purified by using reversed-phase HPLC and identified as 2-cyano-2-propyl hydroperoxide (Cpx) by (1)H and PFG-HMBC NMR spectroscopy. Upon addition of a stoichiometric amount of Cpx, NHase was irreversibly inactivated, probably by the oxidation of alphaCys114-SOH to Cys-SO(2)H. This result suggests that the -SOH structure of alphaCys114 is essential for the catalytic activity. The oxygen atom in Cys-SO(2)H is confirmed to come from the solvent H(2)O. The oxidized NHase was found to induce the UV-vis absorption spectral changes by addition of Cpx, suggesting that Cpx strongly interacted with iron(III) in the oxidized NHase to form a stable complex. Thus, Cpx functions as a novel irreversible inhibitor for NHase. | lld:pubmed |
| pubmed-article:13129355 | pubmed:language | eng | lld:pubmed |
| pubmed-article:13129355 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:13129355 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:13129355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:13129355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:13129355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:13129355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:13129355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:13129355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:13129355 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:13129355 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:13129355 | pubmed:issn | 0002-7863 | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:HoshinoMikioM | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:KoshinoHiroyu... | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:NakayamaHiros... | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:TakioKojiK | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:DohmaeNaoshiN | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:EndoIsaoI | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:YoshidaShigeo... | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:AsamiTadaoT | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:MaedaMizuoM | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:OdakaMasafumi... | lld:pubmed |
| pubmed-article:13129355 | pubmed:author | pubmed-author:TsujimuraMasa... | lld:pubmed |
| pubmed-article:13129355 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:13129355 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:13129355 | pubmed:volume | 125 | lld:pubmed |
| pubmed-article:13129355 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:13129355 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:13129355 | pubmed:pagination | 11532-8 | lld:pubmed |
| pubmed-article:13129355 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:13129355 | pubmed:meshHeading | pubmed-meshheading:13129355... | lld:pubmed |
| pubmed-article:13129355 | pubmed:meshHeading | pubmed-meshheading:13129355... | lld:pubmed |
| pubmed-article:13129355 | pubmed:meshHeading | pubmed-meshheading:13129355... | lld:pubmed |
| pubmed-article:13129355 | pubmed:meshHeading | pubmed-meshheading:13129355... | lld:pubmed |
| pubmed-article:13129355 | pubmed:meshHeading | pubmed-meshheading:13129355... | lld:pubmed |
| pubmed-article:13129355 | pubmed:meshHeading | pubmed-meshheading:13129355... | lld:pubmed |
| pubmed-article:13129355 | pubmed:meshHeading | pubmed-meshheading:13129355... | lld:pubmed |
| pubmed-article:13129355 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:13129355 | pubmed:articleTitle | A novel inhibitor for Fe-type nitrile hydratase: 2-cyano-2-propyl hydroperoxide. | lld:pubmed |
| pubmed-article:13129355 | pubmed:affiliation | Biomolecular Characterization Division, RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. | lld:pubmed |
| pubmed-article:13129355 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:13129355 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:13129355 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:13129355 | lld:pubmed |
