Effect of mutations found in carbohydrate-deficient glycoprotein syndrome type IA on the activity of phosphomannomutase 2.
(1999) FEBS Letters — Vol. 452, n° 3, p. 319-322 (1999)
Files
pdfdocument.pdf
Restricted Access - Adobe PDF
- 90.64 KB
Details
- Authors
- Abstract
- Seven mutant forms of human phosphomannomutase 2 were produced in Escherichia coli and purified. These mutants had a Vmax of 0.2-50% of the wild enzyme and were unstable. The least active protein (R141H) bears a very frequent mutation, which has never been found in the homozygous state whereas the second least active protein (D188G) corresponds to a mutation associated with a particularly severe phenotype. We conclude that total lack of phosphomannomutase 2 is incompatible with life. Another conclusion is that the elevated residual phosphomannomutase activity found in fibroblasts of some patients is contributed by their mutated phosphomannomutase 2.
- Affiliations
Citations
Pirard, M., Matthijs, G., Heykants, L., Schollen, E., Grünewald, S., Jaeken, J., & Van Schaftingen, E. (1999). Effect of mutations found in carbohydrate-deficient glycoprotein syndrome type IA on the activity of phosphomannomutase 2. FEBS Letters, 452(3), 319-322. https://doi.org/10.1016/S0014-5793(99)00673-0 (Original work published 1999)