Publication Date:
1991-12-13
Description:
The cDNA for human gamma-glutamyl carboxylase, which accomplishes the post-translational modification required for the activity of all of the vitamin K-dependent proteins, was cloned. The enzyme is a 758-residue integral membrane protein and appears to have three transmembrane domains near its amino terminus. The hydrophilic COOH-terminal half of the carboxylase has 19.3 percent identity with soybean seed lipoxygenase. Expression of the cloned cDNA resulted in an increase in carboxylase activity in microsomes of transfected cells compared to mock-transfected cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, S M -- Cheung, W F -- Frazier, D -- Stafford, D W -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1634-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of North Carolina, Chapel Hill 27599-3280.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749935" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Base Sequence
;
*Carbon-Carbon Ligases
;
Cattle
;
Cloning, Molecular
;
DNA/genetics
;
Humans
;
Ligases/*genetics
;
Molecular Sequence Data
;
Oligodeoxyribonucleotides/chemistry
;
Polymerase Chain Reaction
;
Recombinant Proteins
;
Sequence Alignment
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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