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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1969-3-18
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pubmed:abstractText |
1. Carnitine acetyltransferase is very rapidly inhibited in the presence of bromoacetyl-(-)-carnitine plus CoA or of bromoacetyl-CoA plus (-)-carnitine. 2. Under appropriate conditions, the enzyme may be titrated with either bromoacetyl substrate analogue; in each case about 1mole of inhibitor is required to inactivate completely 1mole of enzyme of molecular weight 58000+/-3000. 3. Inhibition by bromoacetyl-CoA plus (-)-carnitine results in the formation of an inactive enzyme species, containing stoicheiometric amounts of bound adenine nucleotide and (-)-carnitine in a form that is not removed by gel filtration. This is shown to be S-carboxymethyl-CoA (-)-carnitine ester. 4. The inhibited enzyme recovers activity slowly on prolonged standing at 4 degrees . 5. Incubation with S-carboxymethyl-CoA (-)-carnitine ester causes a slow inhibition of carnitine acetyltransferase. 6. The formation of bound S-carboxymethyl-CoA (-)-carnitine ester by the enzyme is discussed. Presumably the resulting inhibition reflects binding of the ester to both the CoA- and carnitine-binding sites on the enzyme and its consequent very slow dissociation. These observations confirm that carnitine acetyltransferase can form ternary enzyme-substrate complexes; this also appears to be the case with carnitine palmitoyltransferase and choline acetyltransferase.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-13275966,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-13530702,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-13753331,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-13787531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-13915993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-14101979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-14181301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-14186683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-14285260,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-14314378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-14950213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-4158310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-4968184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-5928913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-5965258,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-5965344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-6048792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/5763788-6069132
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
111
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
225-35
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
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pubmed:year |
1969
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pubmed:articleTitle |
Conditions for the self-catalysed inactivation of carnitine acetyltransferase. A novel form of enzyme inhibition.
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pubmed:publicationType |
Journal Article
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