Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine | Oryctolagus cuniculus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme is not affected by cardiolipin and dilauroylphosphatidylcholine | Oryctolagus cuniculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Oryctolagus cuniculus | 5739 | - |
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 | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
25-hydroxyvitamin D + NADPH + O2 | Oryctolagus cuniculus | - |
1alpha,25-dihydroxyvitamin D + NADP+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
full-length and truncated enzyme forms | - |
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 (Comment) | Organism |
---|---|
full-length and truncated enzyme forms from liver mitochondria | Oryctolagus cuniculus |
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 Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
25-hydroxyvitamin D + NADPH + O2 | - |
Oryctolagus cuniculus | 1alpha,25-dihydroxyvitamin D + NADP+ + H2O | - |
? | |
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 | 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 | Comment | Organism |
---|---|---|
CYP27A | - |
Oryctolagus cuniculus |
More | cf. EC 1.14.13.15 | Oryctolagus cuniculus |
vitamin D3 25-hydroxylase | - |
Oryctolagus cuniculus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Oryctolagus cuniculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADPH | - |
Oryctolagus cuniculus |