Any feedback?
Literature summary for 1.14.15.15 extracted from
- Putative helix F contributes to regioselectivity of hydroxylation in mitochondrial cytochrome P450 27A (2001), Biochemistry, 40, 7621-7629.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of wild-type and mutant enzymes in Escherichia coli | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F207A/I211A/F215A | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
| F207K | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
| F207K/I211K/F215K | site-directed mutagenesis, nearly no expression of the mutant in Escherichia coli | Homo sapiens |
| F215A | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
| F215K | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
| I211K | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
| I211K/F215K | site-directed mutagenesis, the mutant shows altered substrate regiospecificity compared to the wild-type enzyme | Homo sapiens |
| additional information | expression and subcellular distribution of the P450 27A1 mutants, overview | Homo sapiens |
| 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 |
| 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 |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Homo sapiens | 5739 | - |
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 | Homo sapiens | - |
(25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O | - |
? |  |
| cholesterol + reduced adrenodoxin + O2 | Homo sapiens | - |
27-hydroxycholesterol + oxidized adrenodoxin + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli | Homo sapiens |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 | - |
Homo sapiens | (25R)-5beta-cholestane-3alpha,7alpha,12alpha,26-tetraol + oxidized adrenodoxin + H2O | - |
? | |
| 5beta-cholestane-3alpha,7alpha,12alpha-triol + reduced adrenodoxin + O2 | - |
Homo sapiens | (25R)-5beta-cholestane-3alpha,7alpha,12alpha,27-tetraol + oxidized adrenodoxin + H2O | - |
? | |
| cholesterol + reduced adrenodoxin + O2 | - |
Homo sapiens | 27-hydroxycholesterol + oxidized adrenodoxin + H2O | - |
? | |
| 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 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the region between helices F and G, the F-G loop, is proposed to contribute to membrane binding in microsomal P450s | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| cytochrome P450 27A | - |
Homo sapiens |
| P450 27A1 | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| adrenodoxin | required | Homo sapiens | |
| NADPH | - |
Homo sapiens | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
