EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.15.15 | expression of wild-type and mutant enzymes in Escherichia coli | Homo sapiens |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.14.15.15 | F207A/I211A/F215A | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
1.14.15.15 | F207K | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
1.14.15.15 | F207K/I211K/F215K | site-directed mutagenesis, nearly no expression of the mutant in Escherichia coli | Homo sapiens |
1.14.15.15 | F215A | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
1.14.15.15 | F215K | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
1.14.15.15 | I211K | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
1.14.15.15 | I211K/F215K | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
1.14.15.15 | additional information | expression and subcellular distribution of the P450 27A1 mutants, overview | Homo sapiens |
1.14.15.15 | W235A | site-directed mutagenesis, the mutant is partly expressed as cytosolic enzyme, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
1.14.15.15 | Y238A | site-directed mutagenesis, the mutant is partly expressed as cytosolic enzyme, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.15.15 | additional information | - |
additional information | - |
Homo sapiens |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.15.15 | mitochondrion | - |
Homo sapiens | 5739 | - |
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 | Homo sapiens | - |
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O | - |
? | |
1.14.15.15 | cholesterol + reduced adrenodoxin + O2 | Homo sapiens | - |
27-hydroxycholesterol + oxidized adrenodoxin + H2O | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.15.15 | Homo sapiens | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.15.15 | recombinant wild-type and mutant enzymes from Escherichia coli | Homo sapiens |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.14.15.15 | additional information | - |
- |
Homo sapiens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.15.15 | 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 | - |
Homo sapiens | (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O | - |
? | |
1.14.15.15 | 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 | - |
Homo sapiens | (25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + oxidized adrenodoxin + H2O | - |
? | |
1.14.15.15 | cholesterol + reduced adrenodoxin + O2 | - |
Homo sapiens | 27-hydroxycholesterol + oxidized adrenodoxin + H2O | - |
? | |
1.14.15.15 | additional information | the regioselectivity of the reaction is determined by residues of the helix F loop, e.g. F207, I211, and F215, substrate regiospecificity of wild-type and mutant enzymes, overview, 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoic acid and 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-al are poor substrates | Homo sapiens | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.14.15.15 | More | the region between helices F and G, the F-G loop, is proposed to contribute to membrane binding in microsomal P450s | Homo sapiens |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.15.15 | cytochrome P450 27A | - |
Homo sapiens |
1.14.15.15 | P450 27A1 | - |
Homo sapiens |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.14.15.15 | 22 | - |
assay at room temperature | Homo sapiens |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.14.15.15 | 7.4 | - |
assay at | Homo sapiens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.15.15 | adrenodoxin | required | Homo sapiens | |
1.14.15.15 | NADPH | - |
Homo sapiens |