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Literature summary extracted from

  • Furster, C.; Bergman, T.; Wikvall, K.
    Biochemical characterization of a truncated form of CYP27A purified from rabbit liver mitochondria (1999), Biochem. Biophys. Res. Commun., 263, 663-666.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.15.15 additional information the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine Oryctolagus cuniculus
1.14.15.18 additional information the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.15.15 additional information the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine Oryctolagus cuniculus
1.14.15.18 additional information the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.15.15 mitochondrion
-
 Oryctolagus cuniculus 5739
-
1.14.15.18 mitochondrion
-
 Oryctolagus cuniculus 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.15.15 51000
-
 x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE Oryctolagus cuniculus
1.14.15.15 52000
-
 x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE Oryctolagus cuniculus
1.14.15.18 51000
-
 x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE Oryctolagus cuniculus
1.14.15.18 52000
-
 x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.15.15 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 Oryctolagus cuniculus
-
 (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.18 25-hydroxyvitamin D + NADPH + O2 Oryctolagus cuniculus
-
 1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.15.15 Oryctolagus cuniculus
-
 full-length and truncated enzyme forms
-
1.14.15.18 Oryctolagus cuniculus
-
 full-length and truncated enzyme forms
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.14.15.15 proteolytic modification the naturally occuring truncated enzyme form is formed by via proteolytic processing of CYP27A by endogenous protease Oryctolagus cuniculus
1.14.15.18 proteolytic modification the naturally occuring truncated enzyme form is formed by via proteolytic processing of CYP27A by endogenous protease Oryctolagus cuniculus

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.15.15 full-length and truncated enzyme forms from liver mitochondria Oryctolagus cuniculus
1.14.15.18 full-length and truncated enzyme forms from liver mitochondria Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.15.15 kidney truncated enzyme form Oryctolagus cuniculus
-
1.14.15.15 liver truncated enzyme form Oryctolagus cuniculus
-
1.14.15.15 additional information no truncated enzyme form in lung, testis, heart, or brain mitochondria Oryctolagus cuniculus
-
1.14.15.15 small intestine truncated enzyme form Oryctolagus cuniculus
-
1.14.15.15 spleen truncated enzyme form Oryctolagus cuniculus
-
1.14.15.18 kidney truncated enzyme form Oryctolagus cuniculus
-
1.14.15.18 liver truncated enzyme form Oryctolagus cuniculus
-
1.14.15.18 additional information no truncated enzyme form in lung, testis, heart, or brain mitochondria Oryctolagus cuniculus
-
1.14.15.18 small intestine truncated enzyme form Oryctolagus cuniculus
-
1.14.15.18 spleen truncated enzyme form Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.15.15 additional information
-
 27-hydroxylation activity of the full-length enzyme form is about 4fold higher than the activity of the truncated enzyme form Oryctolagus cuniculus
1.14.15.18 additional information
-
 1alpha-hydroxylation activity of the full-length enzyme form is 10fold higher than the activity of the truncated enzyme form Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.15 5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + reduced adrenodoxin + O2 oxidation to the corresponding C27-acid Oryctolagus cuniculus 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestane-27-oic acid + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2
-
 Oryctolagus cuniculus (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 cholesterol + reduced adrenodoxin + O2
-
 Oryctolagus cuniculus 24-hydroxycholesterol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 cholesterol + reduced adrenodoxin + O2
-
 Oryctolagus cuniculus 27-hydroxycholesterol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 cholesterol + reduced adrenodoxin + O2
-
 Oryctolagus cuniculus 25-hydroxycholesterol + oxidized adrenodoxin + H2O
-
 ?
1.14.15.15 additional information a multifunctional enzyme catalyzing also the reaction of 25-hydroxyvitamin D3 1alpha-hydroxylase, EC 1.14.13.13, as well as the 24- and 25-hydroxylation of cholesterol, the truncated enzyme form is less efficient than the full-length CYP27A in the 27-hydroxylation of C27-sterols, and much less efficient in the 25-hydroxylation of 1alpha-hydroxyvitamin D3 Oryctolagus cuniculus ?
-
 ?
1.14.15.18 25-hydroxyvitamin D + NADPH + O2
-
 Oryctolagus cuniculus 1alpha,25-dihydroxyvitamin D + NADP+ + H2O
-
 ?
1.14.15.18 additional information a multifunctional enzyme catalyzing also the reaction of cholestanetriol 26-monooxygenase, EC 1.14.13.15, as well as oxidation of 5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol into the corresponding C27-acid, and the 24- and 25-hydroxylation of cholesterol, the truncated enzyme form is less efficient than the full-length CYP27A in the 27-hydroxylation of C27-sterols, and much less efficient in the 25-hydroxylation of 1alpha-hydroxyvitamin D3 Oryctolagus cuniculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.15.15 ? x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE Oryctolagus cuniculus
1.14.15.15 More amino acid sequence comparison of full-length and truncated enzyme forms Oryctolagus cuniculus
1.14.15.18 ? x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE Oryctolagus cuniculus
1.14.15.18 More amino acid sequence comparison of full-length and truncated enzyme forms Oryctolagus cuniculus

Synonyms

EC Number Synonyms Comment Organism
1.14.15.15 CYP27A
-
 Oryctolagus cuniculus
1.14.15.15 cytochrome P450c27
-
 Oryctolagus cuniculus
1.14.15.15 More cf. EC 1.14.13.13 Oryctolagus cuniculus
1.14.15.15 sterol 27-hydroxylase
-
 Oryctolagus cuniculus
1.14.15.18 CYP27A
-
 Oryctolagus cuniculus
1.14.15.18 More cf. EC 1.14.13.15 Oryctolagus cuniculus
1.14.15.18 vitamin D3 25-hydroxylase
-
 Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.15.15 7.4
-
 assay at Oryctolagus cuniculus
1.14.15.18 7.4
-
 assay at Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.15 adrenodoxin
-
 Oryctolagus cuniculus
1.14.15.15 NADPH
-
 Oryctolagus cuniculus
1.14.15.18 NADPH
-
 Oryctolagus cuniculus