Cited by 47Steroid Chemistry and BiochemistryAdrenal Hormones and DisordersCholesterol and Lipid Metabolism

Substrate specificity of adrenocortical cytochrome P-450scc–I. Effect of structural modification of cholesterol side-chain on pregnenolone production

Masuo, Morisaki, Carmenza, Duque, Nobuo, Ikekawa, Mikio, Shikita·1980·Journal of Steroid Biochemistry

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Crossref · 10.1016/0022-4731(80)90211-3

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29 of 29 references verified0 citation errors · 0 not checkable

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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.”
  • 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.”
  • 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].”
  • 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].”
  • 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].”

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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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