Linked Life Data

9198223

Source:http://linkedlifedata.com/resource/pubmed/id/9198223

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-8-8
pubmed:abstractText
Studies on the vitamin K-dependent carboxylase are still in their infancy, but the cloning and purification of the enzyme have permitted a number of advances in our understanding of both the molecular biology, and mechanism of the carboxylase. Advances in our knowledge of the molecular biology of the carboxylase include chromosomal location, characterization of messenger RNA transcript(s) and the study of patients with carboxylase mutations. Our understanding of the mechanism of the carboxylase has been enhanced by the expression of peptides in E. coli which contain multiple carboxylation sites and more closely resemble the native carboxylase substrates. These peptides have been utilized to identify elements within the substrates which are critical for carboxylation and to demonstrate that the vitamin K-dependent carboxylase is one of the first examples of a processive post-translational modification enzyme.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0340-6245
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
599-604
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Characterization of the gamma-glutamyl carboxylase.
pubmed:affiliation
Department of Biology, University of North Carolina at Chapel Hill 27599-3280, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review