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Literature summary for 1.14.14.19 extracted from

  • Swart, A.C.; Storbeck, K.H.; Swart, P.
    A single amino acid residue, Ala 105, confers 16alpha-hydroxylase activity to human cytochrome P450 17alpha-hydroxylase/17,20 lyase (2010), J. Steroid Biochem. Mol. Biol., 119, 112-120.
    View publication on PubMed
Search for more literature for 1.14.14.19

Protein Variants

Protein Variants Comment Organism
A105L site-directed mutagenesis, the single point mutation is sufficient to strongly reduce the 16-hydroxylase activity of the enzyme Homo sapiens
L105A site-directed mutagenesis, the single point mutation is sufficient to confer 16-hydroxylase activity to the enzyme. It also reduced the rate of progesterone conversion Papio ursinus
L105A site-directed mutagenesis, the single point mutation is sufficient to confer 16-hydroxylase activity to the enzyme. It also reduced the rate of progesterone conversion Sus scrofa
L105A site-directed mutagenesis, the single point mutation is sufficient to confer 16-hydroxylase activity to the enzyme. It also reduced the rate of progesterone conversion Capra hircus

Organism

Organism UniProt Comment Textmining
Capra hircus A5HEW0
-
-
Capra hircus South African angora A5HEW0
-
-
Homo sapiens P05093
-
-
Papio ursinus Q9GLD2
-
-
Sus scrofa P19100
-
-

Synonyms

Synonyms Comment Organism
cytochrome P450 17alpha-hydroxylase/17,20 lyase
-
 Homo sapiens
cytochrome P450 17alpha-hydroxylase/17,20 lyase
-
 Papio ursinus
cytochrome P450 17alpha-hydroxylase/17,20 lyase
-
 Sus scrofa
cytochrome P450 17alpha-hydroxylase/17,20 lyase
-
 Capra hircus

General Information

General Information Comment Organism
additional information CYP17 also exhibits 16alpha-hydroxylase activity towards progesterone in some species, with only human and chimp CYP17 catalysing the biosynthesis of substantial amounts of 16-hydroxy-progesterone. Residue 105 is responsible for the activity, homology modelling, overview Homo sapiens
additional information CYP17 also exhibits 16alpha-hydroxylase activity towards progesterone in some species, with only human and chimp CYP17 catalysing the biosynthesis of substantial amounts of 16-hydroxy-progesterone. Residue 105 is responsible for the activity, homology modelling, overview Papio ursinus
additional information CYP17 also exhibits 16alpha-hydroxylase activity towards progesterone in some species, with only human and chimp CYP17 catalysing the biosynthesis of substantial amounts of 16-hydroxy-progesterone. Residue 105 is responsible for the activity, homology modelling, overview Sus scrofa
additional information CYP17 also exhibits 16alpha-hydroxylase activity towards progesterone in some species, with only human and chimp CYP17 catalysing the biosynthesis of substantial amounts of 16-hydroxy-progesterone. Residue 105 is responsible for the activity, homology modelling, overview Capra hircus