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Literature summary for 1.14.14.32 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

Activating Compound Comment Organism Structure
cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Cavia porcellus
cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Mus musculus
cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Rattus norvegicus
cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Sus scrofa
cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Felis catus
cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Equus caballus
cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Papio sp.
cytochrome b5 plays an important role in regulating the 17,20-lyase reaction catalyzed by CYP17 Pan troglodytes
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
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
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
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
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)

Cloned (Comment) Organism
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
sequence comparisons and phylogenetic analysis Cavia porcellus
sequence comparisons and phylogenetic analysis Mus musculus
sequence comparisons and phylogenetic analysis Rattus norvegicus
sequence comparisons and phylogenetic analysis Sus scrofa
sequence comparisons and phylogenetic analysis Bos taurus
sequence comparisons and phylogenetic analysis Ovis aries
sequence comparisons and phylogenetic analysis Felis catus
sequence comparisons and phylogenetic analysis Capra hircus
sequence comparisons and phylogenetic analysis Equus caballus
sequence comparisons and phylogenetic analysis Bison bison
sequence comparisons and phylogenetic analysis Papio sp.
sequence comparisons and phylogenetic analysis Pan troglodytes

Protein Variants

Protein Variants Comment Organism
D298V mutant without heme-binding properties Homo sapiens
G111D mutant without heme-binding properties Homo sapiens
G301I mutant without heme-binding properties Homo sapiens
G90D the mutation results in loss of the 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
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
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
P342T the mutant shows 20% of wild type activity Homo sapiens
Q461stop naturally occuring mutation, inactive mutant Homo sapiens
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
R347H the mutation results in loss of the ability of CYP17A1 to catalyze 17,20-lyase reactions Homo sapiens
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
R358Q the mutation results in loss of the ability of CYP17A1 to catalyze 17,20-lyase reactions Homo sapiens
R449A naturally occuring mutation, results in loss of the ability of CYP17A1 to catalyze 17,20-lyase reactions Homo sapiens
R449A the mutation causes loss of 17,20-lyase activity Homo sapiens
R496C naturally occuring mutation, the mutant has low 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
R96W the mutation results in loss of the 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
S106P the mutation results in loss of the 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens
T64S the mutant shows 15% of wild type activity Homo sapiens

Inhibitors

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
17alpha-hydroxypregnenolone + AH2 + O2 Cavia porcellus
-
dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2 Mus musculus
-
dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2 Rattus norvegicus
-
dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2 Felis catus
-
dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2 Bison bison
-
dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2 Papio sp.
-
dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2 Pan troglodytes
-
dehydroepiandrosterone + acetate + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2 Homo sapiens
-
7-dehydro-17alpha-hydroxy-pregnenolone + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2 Bos taurus
-
7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2 Ovis aries
-
7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2 Capra hircus
-
7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
additional information Mus musculus substrate specificity, comparison of different species, overview ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
progesterone + AH2 + O2 Cavia porcellus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Mus musculus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Rattus norvegicus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Sus scrofa
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Bos taurus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Ovis aries
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Felis catus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Capra hircus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Equus caballus
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Bison bison
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Papio sp.
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Pan troglodytes
-
17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2 Homo sapiens
-
17alpha-hydroxyprogesterone + A + H2O
-
?

Organism

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

Posttranslational Modification

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

Source Tissue

Source Tissue Comment Organism Textmining
adrenal gland
-
Homo sapiens
-
adrenal gland highest expression Homo sapiens
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Cavia porcellus
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Mus musculus
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Rattus norvegicus
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Sus scrofa
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Bos taurus
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Ovis aries
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Felis catus
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Capra hircus
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Equus caballus
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Bison bison
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Papio sp.
-
additional information the tissue-specific expression pattern of the CYP17 gene differs among species Pan troglodytes
-
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
-
ovary
-
Homo sapiens
-
testis
-
Homo sapiens
-
testis highest expression Homo sapiens
-

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
17alpha-hydroxypregnenolone + AH2 + O2
-
Cavia porcellus dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2
-
Mus musculus dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2
-
Rattus norvegicus dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2
-
Felis catus dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2
-
Bison bison dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2
-
Papio sp. dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2
-
Pan troglodytes dehydroepiandrosterone + acetate + A + H2O
-
?
17alpha-hydroxypregnenolone + AH2 + O2
-
Homo sapiens dehydroepiandrosterone + acetate + A + H2O
-
?
7,12-dimethylbenz[a]anthracene + AH2 + O2 substrate for CYP17A1 Homo sapiens ?
-
?
7-dehydro-17alpha-hydroxypregnenolone + AH2 + O2 low activity Homo sapiens 7-dehydro-dehydroepiandrosterone + acetate + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2
-
Homo sapiens 7-dehydro-17alpha-hydroxy-pregnenolone + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2
-
Bos taurus 7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2
-
Ovis aries 7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2
-
Capra hircus 7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
7-dehydro-pregnenolone + AH2 + O2
-
Homo sapiens 7-dehydro-17alpha-hydroxypregnenolone + A + H2O
-
?
aflatoxin B1 + AH2 + O2 substrate for CYP17A1 Homo sapiens aflatoxin B1epoxide + A + H2O
-
?
additional information substrate specificity, comparison of different species, overview Mus musculus ?
-
?
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. ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
additional information CYP17 has both 17alpha-hydroxylase and 17,20-lyase activities Homo sapiens ?
-
?
additional information no activity with 17alpha-hydroxyprogesterone Homo sapiens ?
-
?
pregnenolone + AH2 + O2
-
Homo sapiens 17alpha-hydroxypregnenolone + A + H2O
-
?
progesterone + AH2 + O2
-
Cavia porcellus 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Mus musculus 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Rattus norvegicus 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Sus scrofa 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Bos taurus 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Ovis aries 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Felis catus 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Capra hircus 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Equus caballus 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Bison bison 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Papio sp. 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Pan troglodytes 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + AH2 + O2
-
Homo sapiens 17alpha-hydroxyprogesterone + A + H2O
-
?
progesterone + reduced acceptor + O2
-
Homo sapiens 17alpha-hydroxyprogesterone + acceptor + H2O
-
?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
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