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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1997-1-6
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pubmed:abstractText |
Vitamin K belongs to a class of compounds commonly known as prenylquinones. Three other prenylquinones which are abundantly found in food are plastoquinone-9, ubiquinone-9 and ubiquinone-10. Using in vitro assay systems, it was recently found that synthetic derivatives of prenylquinones inhibit the vitamin K-dependent enzyme gamma-glutamylcarboxylase and, to a lesser extent, the vitamin K-epoxide reductase. In this paper we describe how natural prenylquinones affect the vitamin K-dependent enzymes in vitro. All three prenylquinones were found to inhibit both the vitamin K-dependent carboxylase and the K-epoxide reductase in a rat as well as in a cow liver system; 50% inhibition was obtained at concentrations in the micromolar range. On the basis of their respective standard redox potentials, a possible mechanism for the inhibitory effect of prenylquinones on the carboxylase enzyme is put forward. It is concluded that natural prenylquinones are potential antagonists of vitamin K and may interfere with vitamin K-dependent reactions in vivo.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Carbon Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroquinones,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Plastoquinone,
http://linkedlifedata.com/resource/pubmed/chemical/Quinones,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquinone,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin K,
http://linkedlifedata.com/resource/pubmed/chemical/Vitamin K 1,
http://linkedlifedata.com/resource/pubmed/chemical/glutamyl carboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/vitamin K epoxidase,
http://linkedlifedata.com/resource/pubmed/chemical/vitamin K1 oxide
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
1298
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
87-94
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8948492-Animals,
pubmed-meshheading:8948492-Carbon-Carbon Ligases,
pubmed-meshheading:8948492-Cattle,
pubmed-meshheading:8948492-Electrochemistry,
pubmed-meshheading:8948492-Enzyme Inhibitors,
pubmed-meshheading:8948492-Hydroquinones,
pubmed-meshheading:8948492-Ligases,
pubmed-meshheading:8948492-Microsomes, Liver,
pubmed-meshheading:8948492-Mixed Function Oxygenases,
pubmed-meshheading:8948492-Molecular Structure,
pubmed-meshheading:8948492-Oxidation-Reduction,
pubmed-meshheading:8948492-Plants,
pubmed-meshheading:8948492-Plastoquinone,
pubmed-meshheading:8948492-Quinones,
pubmed-meshheading:8948492-Rats,
pubmed-meshheading:8948492-Rats, Inbred Lew,
pubmed-meshheading:8948492-Ubiquinone,
pubmed-meshheading:8948492-Vitamin K,
pubmed-meshheading:8948492-Vitamin K 1
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pubmed:year |
1996
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pubmed:articleTitle |
Natural prenylquinones inhibit the enzymes of the vitamin K cycle in vitro.
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pubmed:affiliation |
Department of Biochemistry, University of Limburg, Maastricht, The Netherlands.
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pubmed:publicationType |
Journal Article
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