Cell
ArticleRecognition site directing vitamin K-dependent γ-carboxylation resides on the propeptide of factor IX
References (45)
- et al.
Defective propeptide processing of blood clotting Factor IX caused by mutation of arginine to glutamine at position -4
Cell
(1986) - et al.
Metal and phospholipid binding properties of partially carboxylated human prothrombin variants
J. Biol. Chem.
(1985) - et al.
Distribution of γ-carboxyglutamic acid residues in partially carboxylated human prothrombins
J. Biol. Chem.
(1986) - et al.
Prothrombin requires two sequential metal-dependent conformational transitions to bind phospholipid
J. Biol. Chem.
(1986) - et al.
Computer-generated models of blood coagulation Factor Xa, Factor IXa, and thrombin based upon structural homology with other serine proteases
J. Biol. Chem.
(1982) - et al.
Expression, purification and characterization of recombinant γ-carboxylated Factor IX synthesized in Chinese hamster ovary cells
J. Biol. Chem.
(1986) - et al.
Occurrence of β-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens
Biochem. Biophys. Res. Comm.
(1983) Lactoperoxidase-catalyzed iodination as a tool for investigation of proteins
Meth. Enzymol.
(1980)- et al.
The mode of action of vitamin K. Identification of γ-carboxyglutamic acid as a component of prothrombin
J. Biol. Chem.
(1974) - et al.
Primary structure of bovine matrix Gla protein, a new vitamin K-dependent bone protein
J. Biol. Chem.
(1985)
Metal binding properties of γ-carboxyglutamic acid
J. Biol. Chem.
Structure, function and molecular defects of Factor IX
Blood
Expression of active human clotting factor IX from recombinant DNA clones in mammalian cells
Nature
Gene structure of human antihaemophilic factor IX
EMBO J.
The structure and evolution of a 461 amino acid human protein C precursor and its messenger RNA, based upon the DNA sequence of cloned human liver cDNAs
Nucl. Acids Res.
Expression of active human factor IX in transfected cells
Nature
Isolation of the human gene for bone gla protein utilizing mouse and rat cDNA clones
EMBO J.
Isolation of Chinese hamster ovary cell mutants deficient in dihydrofolate reductase activity
Molecular cloning of the gene for human anti-haemophilic Factor IX
Nature
Primary structure of bovine vitamin K-dependent protein S
Characterization of the cDNA and gene coding for human prothrombin
Biochemistry
Active γ-carboxylated human factor IX expressed using recombinant DNA techniques
Nature
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The Molecular Basis of Blood Coagulation
2018, Comprehensive Toxicology: Third EditionFunctional Study of the Vitamin K Cycle Enzymes in Live Cells
2017, Methods in EnzymologyCitation Excerpt :However, FLEEL is a poor substrate analog for GGCX for the following reasons: (1) of the two glutamic acids, only the first glutamic acid of FLEEL is carboxylated during in vitro activity assay (Burgess, Esnouf, Rose, & Offord, 1983; Decottignies-Le Marechal, Rikong-Aide, Azerad, & Gaudry, 1979); (2) only small amounts of substrate are converted to product (Soute, Ulrich, & Vermeer, 1987); and (3) FLEEL binds poorly to GGCX, with a Km of ~ 4 mM (Suttie et al., 1979). Knowing that GGCX interacts with clotting-factor precursors, mainly through an 18-amino acid propeptide (Jorgensen et al., 1987; Pan & Price, 1985), and since propeptide significantly increases small peptide substrate carboxylation (Knobloch & Suttie, 1987), Ulrich et al. used a 28-residue peptide, based on residues − 18 to + 10 in prothrombin (proPT28), as the peptide substrate of GGCX (Ulrich, Furie, Jacobs, Vermeer, & Furie, 1988). This 28-residue peptide is efficiently carboxylated, with a Km that is three orders of magnitude lower than FLEELs.
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