Substrate specificity of adrenocortical cytochrome P-450scc–I. Effect of structural modification of cholesterol side-chain on pregnenolone production
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Purified CYP11A1 also converts desmosterol and plant sterols including campesterol and β-sitosterol to pregnenolone.
“The purified enzyme, also converts desmosterol and plant sterols including campesterol and β-sitosterol, to pregnenolone.”
From Novel activities of CYP11A1 and their potential physiological significance (2015) · cites this paper as [19]
Purified CYP11A1 and/or steroidogenic mitochondria can act on a range of steroids or secosteroids other than cholesterol.
“Studies carried out over a number of years reveal that purified CYP11A1 and/or steroidogenic mitochondria that contain CYP11A1, can act on a range of steroids or secosteroids, other than cholesterol.”
From Novel activities of CYP11A1 and their potential physiological significance (2015) · cites this paper as [19]
Purified bovine and human CYP11A1 and steroidogenic mitochondria cleave the side chains of 24-hydroxycholesterol, 25-hydroxycholesterol, and 27-hydroxycholesterol.
“These include cleaving the side chains of 24-hydroxycholesterol, 25-hydroxycholesterol, and 27-hydroxycholesterol (discussed above) [16,17,19,48].”
From Novel activities of CYP11A1 and their potential physiological significance (2015) · cites this paper as [19]
Desmosterol is converted to pregnenolone by bovine, rat, and human CYP11A1 with similar catalytic efficiency to cholesterol.
“Desmosterol (5,24-cholestadien-3β-ol, see Fig. 1), which has recently come to prominence, is also converted to pregnenolone by bovine, rat, and human CYP11A1 [16,17,19], with similar catalytic efficiency to that seen for cholesterol [48].”
From Novel activities of CYP11A1 and their potential physiological significance (2015) · cites this paper as [19]
Human and bovine CYP11A1 cleave the side chain of plant sterols campesterol and β-sitosterol producing pregnenolone, with catalytic efficiencies comparable to cholesterol for campesterol and 5-10 fold less for β-sitosterol.
“Human and bovine CYP11A1 can also cleave the side chain of the plant sterols, campesterol (24α-methylcholesterol), and β-sitosterol (24β-ethylcholesterol) producing pregnenolone [19], with catalytic efficiencies comparable to cholesterol for campesterol and 5–10 fold less for β-sitosterol [48].”
From Novel activities of CYP11A1 and their potential physiological significance (2015) · cites this paper as [19]
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- Authors
- Masuo, M., Carmenza, D., Nobuo, I., & Mikio, S.
- Affiliations
- Tokyo Institute of Technology (JP)
- Venue
- Journal of Steroid Biochemistry
- Publisher
- Elsevier BV
- Published
- 1980-05
- Volume
- 13
- Issue
- 5
- Pages
- 545-550
- ISSN
- 0022-4731 (ISSN-L)
- OpenAlex
- W2056394711
- Cited by
- 47
- References
- 29
- Citations by year
- 2024: 1 · 2023: 2 · 2021: 2 · 2019: 1 · 2015: 2 · 2014: 1 · 2013: 1
- FWCI
- 1.10
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Steroid Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Steroid Chemistry and Biochemistry
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adrenal Hormones and Disorders
- Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
- Keywords
- cholesterol side-chain cleavage, substrate specificity, cholesterol analogues, steroidogenesis
- MeSH terms
- Adrenal Cortex, Animals, Cattle, Chemistry, Cholesterol, Cytochrome P-450 Enzyme System, Dehydrocholesterols, Hydroxycholesterols, Pregnenolone, Substrate Specificity, Chemical Phenomena
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