Factor IX: Difference between revisions

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The post-translational modification of the glutamic acid residues of the FIX polypeptide is carried out by vitamin K-dependent ''γ''-glutamyl carboxylase <ref>PMID:902786</ref>. Vitamin K-dependent carboxylase is a membrane associated protein in the endoplasmic reticulum. It converts a multiple of glutamic acid residues which are located within 40 residues of a propeptide-containing sequence into ''γ''-carboxyglutamate <ref>PMID:8530480</ref>.

The association ~~ofvitamin~~ K-dependent carboxylase and its substrates is dependent on the 18-amino acid propeptide sequence (<ref>PMID:3875856</ref><ref>PMID:2890628</ref>. The propeptide anchors the substrate to the carboxylase for a carboxylation reaction to occur. This binding of the propeptide to carboxylase stimulates the incorporation of carbon dioxide into the glutamate residues with the use of a reduced vitamin K and oxygen <ref>PMID:2890628</ref><ref>PMID:2802629</ref>. The residues 495-513 of the carboxylase function as an internal propeptide that is homologous to the the propeptide sequence.

The association of vitamin K-dependent carboxylase and its substrates is dependent on the 18-amino acid propeptide sequence <ref>PMID:3875856</ref><ref>PMID:2890628</ref>. The propeptide anchors the substrate to the carboxylase for a carboxylation reaction to occur. This binding of the propeptide to carboxylase stimulates the incorporation of carbon dioxide into the glutamate residues with the use of a reduced vitamin K and oxygen <ref>PMID:2890628</ref><ref>PMID:2802629</ref>. The residues 495-513 of the carboxylase function as an internal propeptide that is homologous to the the propeptide sequence.

To identify the internal propetide region of the Vitamin K-dependent carboxylase, five mutant carboxylase molecules (F496A, V502A, Q503R, Q503N, and P504Q) were generated identify the residues responsible for homologous substrate propeptide binding.

Factor IX: Difference between revisions

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 The post-translational modification of the glutamic acid residues of the FIX polypeptide is carried out by vitamin K-dependent  ''&gamma;''-glutamyl carboxylase <ref>PMID:902786</ref>. Vitamin K-dependent carboxylase is a membrane associated protein in the endoplasmic reticulum. It converts a multiple of glutamic acid residues which are located within 40 residues of a propeptide-containing sequence into ''&gamma;''-carboxyglutamate <ref>PMID:8530480</ref>.
-The association ofvitamin K-dependent carboxylase and its substrates is dependent on the 18-amino acid propeptide sequence (<ref>PMID:3875856</ref><ref>PMID:2890628</ref>. The propeptide anchors the substrate to the carboxylase for a carboxylation reaction to occur. This binding of the propeptide to carboxylase stimulates the incorporation of carbon dioxide into the glutamate residues with the use of a reduced vitamin K and oxygen <ref>PMID:2890628</ref><ref>PMID:2802629</ref>. The residues 495-513 of the carboxylase function as an internal propeptide that is homologous to the the propeptide sequence.
+The association of vitamin K-dependent carboxylase and its substrates is dependent on the 18-amino acid propeptide sequence <ref>PMID:3875856</ref><ref>PMID:2890628</ref>. The propeptide anchors the substrate to the carboxylase for a carboxylation reaction to occur. This binding of the propeptide to carboxylase stimulates the incorporation of carbon dioxide into the glutamate residues with the use of a reduced vitamin K and oxygen <ref>PMID:2890628</ref><ref>PMID:2802629</ref>. The residues 495-513 of the carboxylase function as an internal propeptide that is homologous to the the propeptide sequence.
 To identify the internal propetide region of the Vitamin K-dependent carboxylase, five mutant carboxylase molecules (F496A, V502A, Q503R, Q503N, and P504Q) were generated identify the residues responsible for homologous substrate propeptide binding.