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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1983-4-15
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pubmed:abstractText |
Methoxycarbonyl-CoA disulfide has been used as an active-site-directed inhibitor of carnitine acetyltransferase. Stoichiometric addition of methoxycarbonyl-CoA disulfide to carnitine acetyltransferase showed the modification of one sulfhydryl group with concomitant loss of about 80% enzyme activity. The rate of modification of this sulfhydryl group is an order of magnitude faster than that of the remaining sulfhydryl groups in the enzyme. Methoxycarbonyl-CoA disulfide inactivation is biphasic: k1 = 1.09 X 10(2) M-1 S-1, k2 = 1.1 X 10(1) M-1 S-1. This modification, Enz-SS-CoA is covalent; it can be reversed with either dithioerythritol or thiocholine. Acetyl-carnitine and acetyl-CoA protected the enzyme against methoxycarbonyl-CoA disulfide inactivation; however, carnitine did not. These results indicate the presence of a sulfhydryl group in carnitine acetyltransferase at the site of acetyl group transfer. Titration of carnitine acetyltransferase with nonspecific sulfhydryl reagents, DTNB, and rho-nitrophenoxycarbonyl methyl disulfide, revealed that four sulfhydryl groups were preferentially modified by these reagents. The results also show that seven other sulfhydryl groups are available for modification.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-nitrophenoxycarbonyl methyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Carnitine O-Acetyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Dithionitrobenzoic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/methoxycarbonyl-coenzyme A disulfide
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
220
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
193-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6830231-Acetyltransferases,
pubmed-meshheading:6830231-Binding Sites,
pubmed-meshheading:6830231-Carnitine O-Acetyltransferase,
pubmed-meshheading:6830231-Catalysis,
pubmed-meshheading:6830231-Chemical Phenomena,
pubmed-meshheading:6830231-Chemistry,
pubmed-meshheading:6830231-Coenzyme A,
pubmed-meshheading:6830231-Disulfides,
pubmed-meshheading:6830231-Dithionitrobenzoic Acid,
pubmed-meshheading:6830231-Sulfhydryl Compounds
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pubmed:year |
1983
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pubmed:articleTitle |
Active-site-directed inhibition of carnitine acetyltransferase.
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pubmed:publicationType |
Journal Article
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