| pubmed-article:6697988 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C1257890 | lld:lifeskim |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C0033483 | lld:lifeskim |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C0212744 | lld:lifeskim |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:6697988 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:6697988 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6697988 | pubmed:dateCreated | 1984-4-11 | lld:pubmed |
| pubmed-article:6697988 | pubmed:abstractText | 3-Oxo-3-phenylpropyne and 3-oxo-3-phenylpropene were synthesized as active-site-directed irreversible inhibitors of the bitter almond hydroxynitrile lyase (EC 4.1.2.10), an FAD-protein. The substrate and competitors (e.g. benzoate) decrease the rate of the inhibitor-mediated deactivation of the enzyme. By excess addition of either one of the two inhibitors, the deactivation process is shown to be pseudo-first order. The reaction with equimolar amounts of 3-oxo-3-phenylpropyne with the enzyme is accompanied by a shift in the ultraviolet spectrum of the inhibitor, allowing direct measurement of the enzyme-inactivation process. The spectral change has second-order kinetics. Incubation with 3-oxo-3-[p-3H]phenylpropyne or 3-oxo-3-[1-14C]phenylpropene shows a one-to-one stoichiometry for the inhibitory-enzyme reaction. Dissociation of the 3-oxo-3[p-3H]phenylpropyne-inactivated holoenzyme with acid ammonium sulfate yields a labeled apoenzyme; the inhibitor does not react with free or enzyme-bound FAD. After boranate reduction and exhaustive hydrolysis of the 3-oxo-3-[1-14C]phenylpropene-inactivated enzyme, a labeled cysteine derivative was isolated which was identified by chromatographic and mass spectroscopic comparison with synthetic references as L-2-amino-4-thia-DL-7-hydroxy-7-phenylhepatanoic acid, the reduced, linear addition product of the inhibitor to a cysteine-SH group. | lld:pubmed |
| pubmed-article:6697988 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6697988 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6697988 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6697988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6697988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6697988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6697988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6697988 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6697988 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6697988 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:6697988 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:6697988 | pubmed:author | pubmed-author:JaenickeLL | lld:pubmed |
| pubmed-article:6697988 | pubmed:author | pubmed-author:PreunJJ | lld:pubmed |
| pubmed-article:6697988 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6697988 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:6697988 | pubmed:volume | 138 | lld:pubmed |
| pubmed-article:6697988 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6697988 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6697988 | pubmed:pagination | 319-25 | lld:pubmed |
| pubmed-article:6697988 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:meshHeading | pubmed-meshheading:6697988-... | lld:pubmed |
| pubmed-article:6697988 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6697988 | pubmed:articleTitle | Chemical modification of hydroxynitrile lyase by selective reaction of an essential cysteine-SH group with alpha, beta-unsaturated propiophenones as pseudo-substrates. | lld:pubmed |
| pubmed-article:6697988 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6697988 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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