Linked Life Data

3308517

Source:http://linkedlifedata.com/resource/pubmed/id/3308517

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-11-18
pubmed:abstractText
In the liver vitamin K epoxide, which is produced during the posttranslational carboxylation of protein-bound glutamic acid residues, is recycled by the action of one or more dithiol-dependent reductases. In vitro synthetic dithiols may serve as a cofactor for these enzymes, but the physiological reductant has not yet been found. In this paper we report that in vitro the commercially available thioredoxin/thioredoxin reductase from E. coli can replace the synthetic dithiols during the various reactions of the vitamin K cycle. Based on the assumption that in vivo thioredoxin also plays a role in the regeneration of vitamin K hydroquinone from the epoxide, an extension of the generally accepted vitamin K cycle is proposed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
222
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
353-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Vitamin K-dependent carboxylase. Possible role for thioredoxin in the reduction of vitamin K metabolites in liver.
pubmed:affiliation
Department of Biochemistry, University of Limburg, Maastricht, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't