Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1992-7-14
pubmed:abstractText
The rat liver microsomal vitamin K-dependent carboxylase catalyzes the carboxylation of glutamyl to gamma-carboxyglutamyl residues in the presence of reduced vitamin K, O2 and CO2. The specificity of the enzyme for the vitamin substrate has been probed by the synthesis of a series of fluoro- hydroxy- and methoxy-analogs. 2-Fluoro-methyl-3-phytyl-1,4-naphthoquinone and 2-methyl-3-(1'-fluorodecyl)-1,4-naphthoquinone were synthesized but found to be unstable under enzyme assay conditions. The reduced (naphthohydroquinone) forms of 2-hydroxy-methyl-3-phytyl-1,4-naphthoquinone, 2-methoxymethyl-3-phytyl-1,4-naphthoquinone and 2-methyl-3-(1'-hydroxy-decyl)-1,4-naphthoquinone were inactive as substrates, but inhibitors of the enzyme. The two hydroxy analogs were shown to be low Ki (less than 10 microM) inhibitors of the reduced 2-methyl-3-phytyl-1,4-naphthoquinone-dependent activity of the enzyme. The oxidized forms of these compounds did not inhibit the enzyme and they had no activity as in vivo anticoagulants.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0951-6433
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
205-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Synthesis of fluoro- and hydroxy-derivatives of vitamin K as substrates or inhibitors of the liver microsomal vitamin K-dependent carboxylase.
pubmed:affiliation
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison 53706.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't