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Literature summary for 1.14.15.8 extracted from
- Function and engineering of the 15beta-hydroxylase CYP106A2 (2006), Biochem. Soc. Trans., 34, 1215-1218.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli, wild type and mutant S72A/V73I, the DELTA72 mutant, which lacks the first 72 amino acids, is not expressed in Escherichia coli at a detectable amount, suggesting that the truncated mutant cannot fold properly within the bacterial cell | Priestia megaterium |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | modelling of CYP106A2 and site-directed mutagenesis of the protein to check the accuracy of the computer-derived model of CYP106A2 | Priestia megaterium |
| S72A/V73I | mutant does not show a better stability in the crystallization process than the wild-type protein | Priestia megaterium |
General Stability
| General Stability | Organism |
|---|---|
| by adding the ligands imidazole and metyrapone, it is not possible to prevent CYP106A2 from degradation in the crystallization process | Priestia megaterium |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 47500 | - |
x * 47500 | Priestia megaterium |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Priestia megaterium | Q06069 | ATCC 13368 | - |
Storage Stability
| Storage Stability | Organism |
|---|---|
| 4°C, 4 weeks, degradation during storage | Priestia megaterium |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the specificity of hydroxylation in beta-position can be altered by the choice of the electron transfer system. Replacing the natural electron transfer partners by peroxides, the ratio of 15alpha-/15beta-hydroxylation of progesterone is increased 1.3fold | Priestia megaterium | ? | - |
? |  |
| progesterone + reduced megaredoxin + O2 | - |
Priestia megaterium | 15beta-hydroxyprogesterone + oxidized megaredoxin + H2O | - |
? | |
| testosterone + reduced adrenodoxin + O2 | - |
Priestia megaterium | 15beta-hydroxytestosterone + oxidized adrenodoxin + H2O | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 47500 | Priestia megaterium |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 15beta-hydroxylase | - |
Priestia megaterium |
| CYP106A2 | - |
Priestia megaterium |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| heme | - |
Priestia megaterium | |
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