| pubmed-article:5461620 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:5461620 | lifeskim:mentions | umls-concept:C0002074 | lld:lifeskim |
| pubmed-article:5461620 | lifeskim:mentions | umls-concept:C0007259 | lld:lifeskim |
| pubmed-article:5461620 | lifeskim:mentions | umls-concept:C0019602 | lld:lifeskim |
| pubmed-article:5461620 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:5461620 | lifeskim:mentions | umls-concept:C1709915 | lld:lifeskim |
| pubmed-article:5461620 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:5461620 | pubmed:dateCreated | 1970-5-4 | lld:pubmed |
| pubmed-article:5461620 | pubmed:abstractText | Incubation of carnitine acetyltransferase with low concentrations of bromoacetyl-l-carnitine causes a rapid and irreversible loss of enzyme activity; one mol of inhibitor can inactivate one mol of enzyme. Bromoacetyl-d-carnitine, iodoacetate or iodoacetamide are ineffective. l-Carnitine protects the transferase from bromoacetyl-l-carnitine. Investigation shows that the enzyme first reversibly binds bromoacetyl-l-carnitine with an affinity similar to that shown for the normal substrate acetyl-l-carnitine; this binding is followed by an alkylation reaction, forming the carnitine ester of a monocarboxymethyl-protein, which is catalytically inactive. The carnitine is released at an appreciable rate by spontaneous hydrolysis, and the resulting carboxymethyl-enzyme is also inactive. Total acid hydrolysis of enzyme after treatment with 2-[(14)C]bromoacetyl-l-carnitine yields N-3-carboxy[(14)C]methylhistidine as the only labelled amino acid. These findings, taken in conjunction with previous work, suggest that the single active centre of carnitine acetyltransferase contains a histidine residue. | lld:pubmed |
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| pubmed-article:5461620 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:5461620 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:5461620 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:5461620 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:5461620 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:5461620 | pubmed:author | pubmed-author:TubbsP KPK | lld:pubmed |
| pubmed-article:5461620 | pubmed:author | pubmed-author:ChaseJ FJF | lld:pubmed |
| pubmed-article:5461620 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:5461620 | pubmed:volume | 116 | lld:pubmed |
| pubmed-article:5461620 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:5461620 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:5461620 | pubmed:pagination | 713-20 | lld:pubmed |
| pubmed-article:5461620 | pubmed:dateRevised | 2010-9-10 | lld:pubmed |
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| pubmed-article:5461620 | pubmed:year | 1970 | lld:pubmed |
| pubmed-article:5461620 | pubmed:articleTitle | Specific alkylation of a histidine residue in carnitine acetyltransferase by bromoacetyl-L-carnitine. | lld:pubmed |
| pubmed-article:5461620 | pubmed:publicationType | Journal Article | lld:pubmed |
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