Cloning and expression of the cDNA for human gamma-glutamyl carboxylase.
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.
Wu
S M
SM
Department of Biology, University of North Carolina, Chapel Hill 27599-3280.
Cheung
W F
WF
Frazier
D
D
Stafford
D W
DW
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D019735:Carbon-Carbon Ligases; D002417:Cattle; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D006801:Humans; D008025:Ligases / Q000235:genetics*; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins; D016415:Sequence Alignment
D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins; D004247:DNA; D008025:Ligases; D019735:Carbon-Carbon Ligases; C020660:glutamyl carboxylase