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Molecular basis of hemophilia B: a defective enzyme due to an unprocessed propeptide is caused by a point mutation in the factor IX precursor.
- Source :
- Proceedings of the National Academy of Sciences of the United States of America; August 1986, Vol. 83 Issue: 16 p5803-5807, 5p
- Publication Year :
- 1986
-
Abstract
- A mutant factor IX, designated factor IXCambridge, was isolated from a patient with hemophilia B. This protein includes an 18-residue propeptide attached to the NH2 terminus of factor IX. A point mutation at residue -1, from an arginine to a serine, precludes cleavage of the propeptide by a processing protease and interferes with gamma-carboxylation of the factor IX, indicating the importance of the leader sequence in substrate recognition by the vitamin K-dependent carboxylase. This represents an example of an enzyme defect due to the presence of a point mutation in a precursor protein (preproenzyme) that is the cause of a human hereditary disease. This defect will serve as a prototype for understanding the molecular basis of some forms of hemophilia and other hereditary enzyme deficiencies.
Details
- Language :
- English
- ISSN :
- 00278424 and 10916490
- Volume :
- 83
- Issue :
- 16
- Database :
- Supplemental Index
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Periodical
- Accession number :
- ejs60458998
- Full Text :
- https://doi.org/10.1073/pnas.83.16.5803