EC Number   |
Protein Variants |
Reference |
|---|
    1.14.14.19 | A105L |
mutant has reduced progesterone 16alpha-hydroxylase activity. Catalyzes the 16alpha,17-epoxidation and the ordinarily minor 21-hydroxylation of 16,17-dehydroprogesterone in a 1:5 ratio of epoxide:21-hydroxylated products |
744331 |
| 1.14.14.19 | A105L |
site-directed mutagenesis, the mutant shows low 21-hydroxylation activity compared to the wild-type enzyme |
726997 |
| 1.14.14.19 | A105L |
site-directed mutagenesis, the single point mutation is sufficient to strongly reduce the 16-hydroxylase activity of the enzyme |
716051 |
| 1.14.14.19 | A105L |
the effect of the A105L mutation is to increase progesterone affinity at least 2fold but the mutant has little effect on the already lower affinity for either progesterone hydroxylation product |
734283 |
| 1.14.14.19 | A174E/K388X |
naturally occuring mutation leading to CYP17A1 deficiency and adrenal hyperplasia, phenotype, overview |
704824 |
| 1.14.14.19 | D216H |
natural genetic variant. Cells transiently expressing D216H demonstrate a selective impairment of 16alpha-hydroxyprogesterone synthesis by 2.1fold compared to wild-type CYP17A1, no effect on 17alpha-hydroxyprogesterone synthesis is observed |
745649 |
| 1.14.14.19 | E305G |
naturally occuring mutation, the active site mutant shows lack of 17,20-lyase activity and reduced 17alpha-hydroxylase activity compared to the wild-type, males homozygous show a phenotype with severe micropenis, perineal hypospadias, chordae, and bifid scrotum, while females show normal genitalia, genotyping of two families, overview |
686511 |
| 1.14.14.19 | G162R |
natural genetic variant. Mutation leads to decreased CYP17A1 protein stability with a near 70% reduction in protein levels compared to wild-type. Mutant is preferentially ubiquitinated and degraded prematurely, with an enzyme half-life of about 2.5 h, proteasome inhibitor treatment recovers G162R protein expression |
745649 |
| 1.14.14.19 | H373L |
the replacement causes complete loss of both 17alpha-hydroxylase and 17,20-lyase activities with a defect in heme binding due to a global alteration of P450c17 structure. The mutation is combined with another mutation, a deletion of codon 53 or 54 encoding Phe, TTC, in exon 1, DELTAF54, on a maternal allele. Both mutations together partially abolish both 17alpha-hydroxylase and 17,20-lyase activities. Enzyme deficiency causes clitoromegaly, phenotype, overview |
705509 |
| 1.14.14.19 | H373N |
the substitution results in markedly reduced production of 17alpha-hydroxyprogesterone at 0.2% of the wild-type P450c17 and no production of androstenedione |
705509 |
