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Literature summary for 1.14.15.15 extracted from
- Biochemical characterization of a truncated form of CYP27A purified from rabbit liver mitochondria (1999), Biochem. Biophys. Res. Commun., 263, 663-666.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine | Oryctolagus cuniculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine | Oryctolagus cuniculus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Oryctolagus cuniculus | 5739 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 51000 | - |
x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE | Oryctolagus cuniculus |
| 52000 | - |
x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE | Oryctolagus cuniculus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 | Oryctolagus cuniculus | - |
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
full-length and truncated enzyme forms | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the naturally occuring truncated enzyme form is formed by via proteolytic processing of CYP27A by endogenous protease | Oryctolagus cuniculus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| full-length and truncated enzyme forms from liver mitochondria | Oryctolagus cuniculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| kidney | truncated enzyme form | Oryctolagus cuniculus | - |
| liver | truncated enzyme form | Oryctolagus cuniculus | - |
| additional information | no truncated enzyme form in lung, testis, heart, or brain mitochondria | Oryctolagus cuniculus | - |
| small intestine | truncated enzyme form | Oryctolagus cuniculus | - |
| spleen | truncated enzyme form | Oryctolagus cuniculus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 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 |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | - |
? | |
| 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 | - |
Oryctolagus cuniculus | (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O | - |
? | |
| cholesterol + reduced adrenodoxin + O2 | - |
Oryctolagus cuniculus | 24-hydroxycholesterol + oxidized adrenodoxin + H2O | - |
? | |
| cholesterol + reduced adrenodoxin + O2 | - |
Oryctolagus cuniculus | 27-hydroxycholesterol + oxidized adrenodoxin + H2O | - |
? | |
| cholesterol + reduced adrenodoxin + O2 | - |
Oryctolagus cuniculus | 25-hydroxycholesterol + oxidized adrenodoxin + H2O | - |
? | |
| 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 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 52000, full-length enzyme form, SDS-PAGE, x * 51000, truncated enzyme form, SDS-PAGE | Oryctolagus cuniculus |
| More | amino acid sequence comparison of full-length and truncated enzyme forms | Oryctolagus cuniculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CYP27A | - |
Oryctolagus cuniculus |
| cytochrome P450c27 | - |
Oryctolagus cuniculus |
| More | cf. EC 1.14.13.13 | Oryctolagus cuniculus |
| sterol 27-hydroxylase | - |
Oryctolagus cuniculus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Oryctolagus cuniculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| adrenodoxin | - |
Oryctolagus cuniculus | |
| NADPH | - |
Oryctolagus cuniculus | |
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Release 2023.1 (January 2023)
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