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evolution
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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
evolution
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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
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
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
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
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
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
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
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
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
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
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
evolution
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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
malfunction
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natural mutations causing CYP17A1 deficiency, i.e. 17OHD, a rare form of congenital adrenal hyperplasia
malfunction
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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
malfunction
deficiency of CYP17A1 causes hypertension
metabolism
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CYP17 catalyzes the last step in androgen biosynthesis
metabolism
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Cyp17 is important in the metabolism of androgens, overview
metabolism
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CYP17 is the key enzyme for the biosynthesis of androgens
metabolism
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CYP17 is the key enzyme in androgen biosynthesis pathway
metabolism
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the enzyme is important in adrogene biosynthesis
metabolism
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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
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
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CYP17-dependent alternative steroids biosynthesis, overview
metabolism
cytochrome b5 plays an important role in the intracellular regulation of biosynthesis of androgens at the level of CYP17. Cytochrome b5 mainly stimulates 17,20-lyase activity of CYP17, but has no effect on the 17alpha-hydroxylation reaction
metabolism
cytochrome P450 CYP17A1 catalyzes a series of reactions that lie at the intersection of corticoid and androgen biosynthesis and thus occupies an essential role in steroid hormone metabolism
metabolism
the bifunctional enzyme is responsible for pregnenolone C17 hydroxylation, followed by a 17,20-lyase reaction to produce dehydroepiandrosterone, the key intermediate in human synthesis of androgen and estrogen sex steroids
physiological function
cytochromeP450 17alpha-hydroxylase/c17-20 lyase is one of the key enzymes involved in the steroidogenic shift that occurs prior to oocyte maturation in teleosts
physiological function
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the enzyme catalyzes two sequential and necessary reactions in the production of androgens
physiological function
17alpha-hydroxylase/17,20-lyase is a critical enzyme in the production of androgens and estrogens in vertebrates
physiological function
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17alpha-hydroxylase/C17,20-lyase, CYP17, a P450 enzyme, is responsible for catalyzing the final step in androgen biosynthesis
physiological function
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CYP17 is involved in endometrial cancinogenesis through apoptosis and invasion pathways. CYP17 affects endometrial carcinoma KLE cell apoptosis by regulating expression of several apoptosis related genes, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
-
CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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CYP17A1 catalyzes the 17alpha-hydroxylase and 17,20-lyase reactions using various C21-steroids as substrates, overview
physiological function
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the cytochrome P450 17alpha-hydroxylase/C(17,20)-lyase plays a pivotal role in the synthesis of dehydroepiandrosterone from pregnenolone and progesterone
physiological function
CYP17A1 plays an essential role in the production of steroid androgens by mediating two subsequent steps in the steroidogenic pathway
physiological function
cytochrome CYP17 is a key enzyme of steroid hormone biosynthesis. Bifunctional CYP17 catalyzes two independent reactions in the same active center, the 17alpha-hydroxylase and 17,20-lyase reactions
physiological function
cytochrome P450c17 is a steroidogenic enzyme that catalyzes the steroid 17alpha-hydroxylation needed for glucocorticoid synthesis
physiological function
human steroidogenic cytochrome P450 CYP17A1 is required for the biosynthesis of androgens, glucocorticoids, and mineralocorticoids
physiological function
P450c17, a key steroidogenic enzyme, plays important roles in the production of sex steroid and cortisol. In teleost, there are two types of P450c17, P450c17-I possessing 17alpha-hydroxylase and 17,20-lyase activities, and P450c17-II only possessing 17alpha-hydroxylase activity. Only P450c17-II is involved in the production of cortisol in barfin flounder
physiological function
P450c17, a key steroidogenic enzyme, plays important roles in the production of sex steroid and cortisol. In teleost, there are two types of P450c17, P450c17-I possessing 17alpha-hydroxylase and 17,20-lyase activities, and P450c17-II only possessing 17alpha-hydroxylase activity. P450c17-I is not involved in the production of cortisol in barfin flounder
physiological function
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the enzyme plays a critical role in the production of androgens and estrogens in vertebrates, important role of P450c17-I during shift in steroidogenesis
physiological function
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the enzyme produces dehydroepiandrosterone, which is the most abundant circulating endogenous sex steroid precursor. Dehydroepiandrosterone plays a key role in e.g. sexual functioning and development
physiological function
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the enzyme produces dehydroepiandrosterone, which is the most abundant circulating endogenous sex steroid precursor. Dehydroepiandrosterone plays a key role in e.g. sexual functioning and development
physiological function
close interactions within living cells between cytochrome P450c17 and cytochrome b5. Residues E48 and E49 residues in cytochrome b5 are essential for activity. The wild type cytochrome b5, but not a mutated, E48G/E49G cyt b5, alters the kinetics of electron transfer between the electrode and the P450c17 during quartz crystal microbalance studies
physiological function
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the cytochrome P450 17alpha-hydroxylase/C(17,20)-lyase plays a pivotal role in the synthesis of dehydroepiandrosterone from pregnenolone and progesterone
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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
additional information
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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
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
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
additional information
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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
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
additional information
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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
additional information
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in the case of CYP17 the attack of Fe(III)-O-O(-) on the target carbon is promoted by cytochrome b5, which acts as a conformational regulator of CYP17. It is this regulation of CYP17 that provides a safety mechanism which ensures that during corticoid biosynthesis, which involves 17alpha-hydroxylation by CYP17, androgen formation is avoided
additional information
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knockdown of CYP17 by siRNA affects cellular proliferation
additional information
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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
additional information
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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
additional information
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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
additional information
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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
additional information
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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
additional information
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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
additional information
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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
additional information
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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
additional information
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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
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
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
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
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
additional information
modeling of tertiary structure of CYP17, overview. Direct molecular interactions, with electrostatic interactions playing a crucial role, between steroidogenic enzymes CYP17 and CYP21 that are localized in endoplasmic reticulum membranes of adrenal cortex and involved in biosynthesis of corticosteroid hormones, overview
additional information
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optimization and standardization of the porcine adrenal cortex microsome assay, overview
additional information
substrate-modulated interactions of cytochrome P450 17A1 and cytochrome b5, by reversible binding, involving enzyme anionic residues Glu48 or Glu49 and corresponding cationic CYP17A1 residues Arg347, Arg358, and Arg449, NMR analysis, overview. The CYP17A1/b5 interaction is stronger when the hydroxylase substrate pregnenolone is present in the CYP17A1 active site than when the lyase substrate 17alpha-hydroxypregnenolone is in the active site
additional information
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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
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