Regulation of vitamin K-dependent carboxylation.
نویسندگان
چکیده
منابع مشابه
Vitamin K-dependent carboxylation of the carboxylase.
Vitamin K-dependent (VKD) proteins require modification by the VKD-gamma-glutamyl carboxylase, an enzyme that converts clusters of glus to glas in a reaction that requires vitamin K hydroquinone, for their activity. We have discovered that the carboxylase also carboxylates itself in a reaction dependent on vitamin K. When pure human recombinant carboxylase was incubated in vitro with 14CO2 and ...
متن کاملVitamin K-dependent carboxylation of pulmonary surfactant-associated proteins.
Rat type II pneumocytes expressed vitamin K-dependent carboxylase activity that incorporated 14CO2 into microsomal protein precursors of molecular weights similar to those of surfactant-associated proteins (SAP). Compared to carboxylated precursor proteins present in the liver, these molecules appeared to be unique to the lung. Antibodies raised against purified rat surfactant reacted with SAP ...
متن کاملMolecular Basis of Vitamin K - Dependent y - Carboxylation
H E VITAMIN K-dependent blood clotting and regulaT tory proteins, including prothrombin, factor TX, factor X, factor VII, protein C, and protein S, require a number of posttranslational modifications to yield the biologically active forms of these proteins that circulate in the blood. In addition to the typical processing characteristic of secreted proteins, including signal peptide cleavage, p...
متن کاملSoluble enzyme system for vitamin K-dependent carboxylation.
The vitamin K-dependent carboxylating system has been solubilized by Lubrol PX or Triton X-100 treatment of vitamin K-deficient rat liver microsomes. As obtained from vitamin K-deficient rat liver, this soluble preparation is dependent upon the in vitro addition of vitamin K1 for carboxylating activity. The enzyme system is complex and is dependent upon NADH and dithiothreitol for maximum activ...
متن کاملEvidence for the vitamin K-dependent y-carboxylation of the first glutamic acid residue
The peptide substrate commonly used in vitamin K-dependent carboxylation, Phe-Leu-Glu-Glu-Val, has been shown, by the use of high-voltage paper electrophoresis, to be degraded from the N-terminus by a microsomal leucine aminopeptidase. The replacement of phenylalanine with a N-t-butoxycarbonyl group resulted in a tetrapeptide substrate with a blocked N-terminus resistant to enzymic degradation....
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)86176-8