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Literature summary extracted from

  • Gilep, A.A.; Sushko, T.A.; Usanov, S.A.
    At the crossroads of steroid hormone biosynthesis: the role, substrate specificity and evolutionary development of CYP17 (2011), Biochim. Biophys. Acta, 1814, 200-209.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Cavia porcellus
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Mus musculus
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Rattus norvegicus
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Sus scrofa
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Felis catus
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Equus caballus
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Papio sp.
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Pan troglodytes
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17. Rat cytochrome b5 stimulates the 17,20-lyase activity of bovine CYP17A1 by a factor of 4-5 Bos taurus
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17. Rat cytochrome b5 stimulates the 17,20-lyase activity of bovine CYP17A1 by a factor of 4-5 Ovis aries
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17. Rat cytochrome b5 stimulates the 17,20-lyase activity of bovine CYP17A1 by a factor of 4-5 Capra hircus
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17. Rat cytochrome b5 stimulates the 17,20-lyase activity of bovine CYP17A1 by a factor of 4-5 Bison bison
1.14.14.32 cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17. Rat cytochrome b5 stimulates the 17,20-lyase activity of human CYP17A1 by a factor of 5. The H67A mutant of cytochrome b5 and Zn-substituted b5 are both unable to bind heme and therefore fail to stimulate the catalytic activity of CYP17 Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.32 gene CYP17A1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, expression of wild-type and mutant enzymes in COS-1 cells Homo sapiens
1.14.14.32 sequence comparisons and phylogenetic analysis Cavia porcellus
1.14.14.32 sequence comparisons and phylogenetic analysis Mus musculus
1.14.14.32 sequence comparisons and phylogenetic analysis Rattus norvegicus
1.14.14.32 sequence comparisons and phylogenetic analysis Sus scrofa
1.14.14.32 sequence comparisons and phylogenetic analysis Bos taurus
1.14.14.32 sequence comparisons and phylogenetic analysis Ovis aries
1.14.14.32 sequence comparisons and phylogenetic analysis Felis catus
1.14.14.32 sequence comparisons and phylogenetic analysis Capra hircus
1.14.14.32 sequence comparisons and phylogenetic analysis Equus caballus
1.14.14.32 sequence comparisons and phylogenetic analysis Bison bison
1.14.14.32 sequence comparisons and phylogenetic analysis Papio sp.
1.14.14.32 sequence comparisons and phylogenetic analysis Pan troglodytes

Protein Variants

EC Number Protein Variants Comment Organism
1.14.14.32 D298V mutant without heme-binding properties Homo sapiens
1.14.14.32 G111D mutant without heme-binding properties Homo sapiens
1.14.14.32 G301I mutant without heme-binding properties Homo sapiens
1.14.14.32 G90D the mutation results in loss of the 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
1.14.14.32 additional information mutations resulting in only the 17,20-lyase deficiency are located either in the putative substrate-binding region of CYP17A1 or in the region responsible for interaction with cytochrome b5 Homo sapiens
1.14.14.32 additional information several patients with 17,20-lyase deficiency carry the substitutions Q461stop and R496C. Mutant Q461stop is not active, whereas mutant R496C has low 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
1.14.14.32 P342T the mutant shows 20% of wild type activity Homo sapiens
1.14.14.32 Q461stop naturally occuring mutation, inactive mutant Homo sapiens
1.14.14.32 R347H naturally occuring mutation, results in loss of the ability of CYP17A1 to catalyze 17,20-lyase reactions, the mutant CYP17A1 loses the ability to interact with cytochrome b5 in recombinant COS-1 cells. Molecular modeling experiments indicate that substitution R347H neutralizes surface positive charges in the region responsible for redox-partner binding Homo sapiens
1.14.14.32 R347H the mutation results in loss of the ability of CYP17A1 to catalyze 17,20-lyase reactions Homo sapiens
1.14.14.32 R358Q naturally occuring mutation, results in loss of the ability of CYP17A1 to catalyze 17,20-lyase reactions, the mutant CYP17A1 loses the ability to interact with cytochrome b5 in recombinant COS-1 cells. Molecular modeling experiments indicate that substitution R358Q neutralizes surface positive charges in the region responsible for redox-partner binding Homo sapiens
1.14.14.32 R358Q the mutation results in loss of the ability of CYP17A1 to catalyze 17,20-lyase reactions Homo sapiens
1.14.14.32 R449A naturally occuring mutation, results in loss of the ability of CYP17A1 to catalyze 17,20-lyase reactions Homo sapiens
1.14.14.32 R449A the mutation causes loss of 17,20-lyase activity Homo sapiens
1.14.14.32 R496C naturally occuring mutation, the mutant has low 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
1.14.14.32 R96W the mutation results in loss of the 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
1.14.14.32 S106P the mutation results in loss of the 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
1.14.14.32 T64S the mutant shows 15% of wild type activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.32 abiraterone acetate
-
Homo sapiens
1.14.14.32 bitertanol
-
Homo sapiens
1.14.14.32 fluconazole
-
Homo sapiens
1.14.14.32 flusilazole
-
Homo sapiens
1.14.14.32 ketoconazole
-
Homo sapiens
1.14.14.32 additional information itraconazole has no effect on human CYP17A1 Homo sapiens
1.14.14.32 Propiconazole
-
Homo sapiens
1.14.14.32 tebuconazole highest affinity for human CYP17A1 Homo sapiens
1.14.14.32 triadimenol
-
Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.14.32 endoplasmic reticulum membrane
-
Cavia porcellus 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Mus musculus 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Rattus norvegicus 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Sus scrofa 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Bos taurus 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Ovis aries 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Felis catus 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Capra hircus 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Equus caballus 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Bison bison 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Papio sp. 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Pan troglodytes 5789
-
1.14.14.32 endoplasmic reticulum membrane
-
Homo sapiens 5789
-
1.14.14.32 microsome
-
Cavia porcellus
-
-
1.14.14.32 microsome
-
Mus musculus
-
-
1.14.14.32 microsome
-
Rattus norvegicus
-
-
1.14.14.32 microsome
-
Sus scrofa
-
-
1.14.14.32 microsome
-
Bos taurus
-
-
1.14.14.32 microsome
-
Ovis aries
-
-
1.14.14.32 microsome
-
Felis catus
-
-
1.14.14.32 microsome
-
Capra hircus
-
-
1.14.14.32 microsome
-
Equus caballus
-
-
1.14.14.32 microsome
-
Bison bison
-
-
1.14.14.32 microsome
-
Papio sp.
-
-
1.14.14.32 microsome
-
Pan troglodytes
-
-
1.14.14.32 microsome
-
Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2 Cavia porcellus
-
dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2 Mus musculus
-
dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2 Rattus norvegicus
-
dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2 Felis catus
-
dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2 Bison bison
-
dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2 Papio sp.
-
dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2 Pan troglodytes
-
dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2 Homo sapiens
-
7-dehydro-17alpha-hydroxy-pregnenolone + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2 Bos taurus
-
7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2 Ovis aries
-
7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2 Capra hircus
-
7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
1.14.14.32 additional information Mus musculus substrate specificity, comparison of different species, overview ?
-
?
1.14.14.32 additional information Papio sp. the baboon enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview ?
-
?
1.14.14.32 additional information Bison bison the bison enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview ?
-
?
1.14.14.32 additional information Bos taurus the bovine enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview ?
-
?
1.14.14.32 additional information Felis catus the cat enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview ?
-
?
1.14.14.32 additional information Pan troglodytes the chimp enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview ?
-
?
1.14.14.32 additional information Capra hircus the goat enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview ?
-
?
1.14.14.32 additional information Cavia porcellus the guinea pig enzyme belongs to the DELTA4-type CYP17, which has no, or very low, 17,20-lyase activity with 17alpha-hydroxy-pregnenolone with the formation of dehydroepiandrosterone, substrate specificity, comparison of different species, overview ?
-
?
1.14.14.32 additional information Equus caballus the horse enzyme belongs to the DELTA4,5-type of CYP17, which catalyses the 17alpha-hydroxylation of progesterone and pregnenolone and the 17,20-lyase reaction of 17alpha-hydroxy-progesterone and 17alpha-hydroxy-pregnenolone, substrate specificity, comparison of different species, overview ?
-
?
1.14.14.32 additional information Homo sapiens the human enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview ?
-
?
1.14.14.32 additional information Sus scrofa the pig enzyme belongs to the DELTA4,5-type of CYP17, which catalyses the 17alpha-hydroxylation of progesterone and pregnenolone and the 17,20-lyase reaction of 17alpha-hydroxy-progesterone and 17alpha-hydroxy-pregnenolone, substrate specificity, comparison of different species, overview ?
-
?
1.14.14.32 additional information Rattus norvegicus the rat enzyme belongs to the DELTA4,5-type of CYP17, which catalyses the 17alpha-hydroxylation of progesterone and pregnenolone and the 17,20-lyase reaction of 17alpha-hydroxy-progesterone and 17alpha-hydroxy-pregnenolone, substrate specificity, comparison of different species, overview ?
-
?
1.14.14.32 additional information Ovis aries the sheep enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview ?
-
?
1.14.14.32 progesterone + AH2 + O2 Cavia porcellus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Mus musculus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Rattus norvegicus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Sus scrofa
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Bos taurus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Ovis aries
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Felis catus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Capra hircus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Equus caballus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Bison bison
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Papio sp.
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Pan troglodytes
-
17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2 Homo sapiens
-
17alpha-hydroxyprogesterone + A + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.32 Bison bison
-
-
-
1.14.14.32 Bos taurus
-
-
-
1.14.14.32 Capra hircus
-
-
-
1.14.14.32 Cavia porcellus
-
-
-
1.14.14.32 Equus caballus
-
-
-
1.14.14.32 Felis catus
-
-
-
1.14.14.32 Homo sapiens P05093
-
-
1.14.14.32 Homo sapiens P05093 CYP17A1; CYP17A1
-
1.14.14.32 Mus musculus
-
-
-
1.14.14.32 Ovis aries
-
-
-
1.14.14.32 Pan troglodytes
-
-
-
1.14.14.32 Papio sp.
-
-
-
1.14.14.32 Rattus norvegicus
-
-
-
1.14.14.32 Sus scrofa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.14.14.32 phosphoprotein phosphorylation of the CYP17 protein affects its stability and activity Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.14.32 adrenal gland
-
Homo sapiens
-
1.14.14.32 adrenal gland highest expression Homo sapiens
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Cavia porcellus
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Mus musculus
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Rattus norvegicus
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Sus scrofa
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Bos taurus
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Ovis aries
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Felis catus
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Capra hircus
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Equus caballus
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Bison bison
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Papio sp.
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species Pan troglodytes
-
1.14.14.32 additional information the tissue-specific expression pattern of the CYP17 gene differs among species. The human mRNA appears to be ubiquitously expressed in all tissues,with the highest levels detected in testis and adrenals, and also in various human fetal tissues. The enzyme occurs in steroidogenic cells Homo sapiens
-
1.14.14.32 ovary
-
Homo sapiens
-
1.14.14.32 testis
-
Homo sapiens
-
1.14.14.32 testis highest expression Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Cavia porcellus
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Mus musculus
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Rattus norvegicus
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Sus scrofa
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Bos taurus
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Ovis aries
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Felis catus
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Capra hircus
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Equus caballus
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Bison bison
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Papio sp.
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Pan troglodytes
1.14.14.32 additional information
-
17alpha-hydroxylase and 17,20-lyase activities of purified enzyme, comparisons of different species, overview Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2
-
Cavia porcellus dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2
-
Mus musculus dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2
-
Rattus norvegicus dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2
-
Felis catus dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2
-
Bison bison dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2
-
Papio sp. dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2
-
Pan troglodytes dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 17alpha-hydroxypregnenolone + AH2 + O2
-
Homo sapiens dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 7,12-dimethylbenz[a]anthracene + AH2 + O2 substrate for CYP17A1 Homo sapiens ?
-
?
1.14.14.32 7-dehydro-17alpha-hydroxypregnenolone + AH2 + O2 low activity Homo sapiens 7-dehydro-dehydroepiandrosterone + acetate + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2
-
Homo sapiens 7-dehydro-17alpha-hydroxy-pregnenolone + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2
-
Bos taurus 7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2
-
Ovis aries 7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2
-
Capra hircus 7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
1.14.14.32 7-dehydro-pregnenolone + AH2 + O2
-
Homo sapiens 7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
1.14.14.32 aflatoxin B1 + AH2 + O2 substrate for CYP17A1 Homo sapiens aflatoxin B1epoxide + A + H2O
-
?
1.14.14.32 additional information substrate specificity, comparison of different species, overview Mus musculus ?
-
?
1.14.14.32 additional information the baboon enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview Papio sp. ?
-
?
1.14.14.32 additional information the bison enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview Bison bison ?
-
?
1.14.14.32 additional information the bovine enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview Bos taurus ?
-
?
1.14.14.32 additional information the cat enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview Felis catus ?
-
?
1.14.14.32 additional information the chimp enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview Pan troglodytes ?
-
?
1.14.14.32 additional information the goat enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview Capra hircus ?
-
?
1.14.14.32 additional information the guinea pig enzyme belongs to the DELTA4-type CYP17, which has no, or very low, 17,20-lyase activity with 17alpha-hydroxy-pregnenolone with the formation of dehydroepiandrosterone, substrate specificity, comparison of different species, overview Cavia porcellus ?
-
?
1.14.14.32 additional information the horse enzyme belongs to the DELTA4,5-type of CYP17, which catalyses the 17alpha-hydroxylation of progesterone and pregnenolone and the 17,20-lyase reaction of 17alpha-hydroxy-progesterone and 17alpha-hydroxy-pregnenolone, substrate specificity, comparison of different species, overview Equus caballus ?
-
?
1.14.14.32 additional information the human enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview Homo sapiens ?
-
?
1.14.14.32 additional information the pig enzyme belongs to the DELTA4,5-type of CYP17, which catalyses the 17alpha-hydroxylation of progesterone and pregnenolone and the 17,20-lyase reaction of 17alpha-hydroxy-progesterone and 17alpha-hydroxy-pregnenolone, substrate specificity, comparison of different species, overview Sus scrofa ?
-
?
1.14.14.32 additional information the rat enzyme belongs to the DELTA4,5-type of CYP17, which catalyses the 17alpha-hydroxylation of progesterone and pregnenolone and the 17,20-lyase reaction of 17alpha-hydroxy-progesterone and 17alpha-hydroxy-pregnenolone, substrate specificity, comparison of different species, overview Rattus norvegicus ?
-
?
1.14.14.32 additional information the sheep enzyme belongs to the DELTA5-type CYP17, which has no, or very low, 17,20-lyase activity with 17-OH-progesterone with the formation of androstendione, substrate specificity, comparison of different species, none of the primate enzymes has 17,20-lyase activity towards DELTA4-steroids, overview Ovis aries ?
-
?
1.14.14.32 additional information CYP17 has both 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens ?
-
?
1.14.14.32 additional information no activity with 17alpha-hydroxyprogesterone Homo sapiens ?
-
?
1.14.14.32 pregnenolone + AH2 + O2
-
Homo sapiens 17alpha-hydroxypregnenolone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Cavia porcellus 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Mus musculus 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Rattus norvegicus 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Sus scrofa 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Bos taurus 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Ovis aries 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Felis catus 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Capra hircus 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Equus caballus 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Bison bison 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Papio sp. 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Pan troglodytes 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + AH2 + O2
-
Homo sapiens 17alpha-hydroxyprogesterone + A + H2O
-
?
1.14.14.32 progesterone + reduced acceptor + O2
-
Homo sapiens 17alpha-hydroxyprogesterone + acceptor + H2O
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.14.32 CYP17
-
Cavia porcellus
1.14.14.32 CYP17
-
Mus musculus
1.14.14.32 CYP17
-
Rattus norvegicus
1.14.14.32 CYP17
-
Sus scrofa
1.14.14.32 CYP17
-
Bos taurus
1.14.14.32 CYP17
-
Ovis aries
1.14.14.32 CYP17
-
Felis catus
1.14.14.32 CYP17
-
Capra hircus
1.14.14.32 CYP17
-
Equus caballus
1.14.14.32 CYP17
-
Bison bison
1.14.14.32 CYP17
-
Papio sp.
1.14.14.32 CYP17
-
Pan troglodytes
1.14.14.32 CYP17
-
Homo sapiens
1.14.14.32 CYP17A1
-
Homo sapiens
1.14.14.32 CYP17A1 isoform Homo sapiens
1.14.14.32 steroid 17alphahydroxylase/17,20-lyase
-
Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.14.32 cytochrome b5 without effect on steroid 17alpha-hydroxylation, cytochrome b5 causes a 5-10fold stimulation of the 17,20-lyase reaction mediated by CYP17 Homo sapiens

Expression

EC Number Organism Comment Expression
1.14.14.19 Homo sapiens the expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries. At least three factors, NF1, SF1 and SF3, control the expression level of human CYP17A1 in adrenals. Regions of the CYP17A1 gene responsible for binding transcriptional factors are: nt -107 to -85 and nt -178 to -152 for NF1-1C, nt -227 to -184 for SF1 and SF3 additional information

General Information

EC Number General Information Comment Organism
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Cavia porcellus
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Mus musculus
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Rattus norvegicus
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Sus scrofa
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Bos taurus
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Ovis aries
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Felis catus
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Capra hircus
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Equus caballus
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Bison bison
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Papio sp.
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Pan troglodytes
1.14.14.19 evolution the CYP17 enzymes from various species have 46-98% sequence homology, depending on the evolutionary distance between the organisms. Enzymes from different mammalian species show relatively high homology of amino acid sequences, but have different types of activity and different requirements for cytochrome b5 Homo sapiens
1.14.14.19 malfunction mutations resulting in only the 17,20-lyase deficiency are located either in the putative substrate-binding region of CYP17A1 or in the region responsible for interaction with cytochrome b5 Homo sapiens
1.14.14.19 metabolism CYP17 catalyzes the 17alpha-hydroxylation reaction of delta4-C21 steroids (progesterone derivatives) and delta5-C21 steroids (pregnenolone derivatives) aswell as the 17,20-lyase reaction producing C19-steroids, a key branch point in steroid hormone biosynthesis. Depending on CYP17 activity, the steroid hormone biosynthesis pathway is directed to either the formation of mineralocorticoids and glucocorticoids or sex hormones Homo sapiens
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Cavia porcellus
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Mus musculus
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Rattus norvegicus
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Sus scrofa
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Bos taurus
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Ovis aries
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Felis catus
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Capra hircus
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Equus caballus
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Bison bison
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Papio sp.
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Pan troglodytes
1.14.14.19 metabolism CYP17-dependent alternative steroids biosynthesis, overview Homo sapiens
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Cavia porcellus
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Mus musculus
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Rattus norvegicus
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Sus scrofa
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Bos taurus
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Ovis aries
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Felis catus
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Capra hircus
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Equus caballus
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Bison bison
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Papio sp.
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Pan troglodytes
1.14.14.19 additional information the following factors contribute to the regulation of CYP17 activities: 1. the ratio of NADPH-cytochrome P450 reductase to CYP17, i.e. the rate of delivery of reducing equivalents to the P450, 2. the presence of cytochrome b5 either as an allosteric effector or as an electron donor, 3. phosphorylation of the CYP17 protein, which affects its stability and activity, and 4. retention of the intermediate, 17-OHP5 or 17-OHP4, in the active site of CYP17, which facilitates the 17,20-lyase reaction. Expression level of CYP17A1 in adrenals is regulated by ACTH and by gonadotropic hormone in the testis and ovaries Homo sapiens
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Cavia porcellus
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Mus musculus
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Rattus norvegicus
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Sus scrofa
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Bos taurus
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Ovis aries
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Felis catus
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Capra hircus
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Equus caballus
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Bison bison
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Papio sp.
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Pan troglodytes
1.14.14.19 physiological function CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview Homo sapiens