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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Naturally occurring mutants of human steroid 21-hydroxylase (P450c21) pinpoint residues important for enzyme activity and stability.

Three mutants (deletion of E196, G291S, and R483P) of steroid 21-hydroxylase (P450c21) from patients with inherited congenital adrenal hyperplasia had reduced activity toward progesterone and 17-hydroxyprogesterone after transient expression in cultured mammalian cells. In addition, both the E196 deletion and the R483P mutant had shorter half-lives than the wild-type enzyme, whereas the half-life of the G291S mutant was comparable with that of the normal protein. These results directly link the clinical situation with the three mutations and suggest that G291 is important for the catalytic activity of P450c21.[1]

References

  1. Naturally occurring mutants of human steroid 21-hydroxylase (P450c21) pinpoint residues important for enzyme activity and stability. Nikoshkov, A., Lajic, S., Vlamis-Gardikas, A., Tranebjaerg, L., Holst, M., Wedell, A., Luthman, H. J. Biol. Chem. (1998) [Pubmed]
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