EC Number | Cloned (Comment) | Organism |
---|---|---|
1.14.15.6 | hybrid proteins AAC-mCYP11A1, Bcs1p(183)-mCYP11A1, Su9(1-116)-mCYP11A1, preAd-mCYP11A1, DLD(1-72)-mCYP11A1 and COXIV-mCYP11A1 expressed in Saccharomyces cerevisiae strain 2805. Escherichia coli strain JM109 transformed with the plasmid pTrc99(A)/Ad-mCYP11A1 | synthetic construct |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.14.15.6 | additional information | all of the addressing sequences, containing transmembrane domains, provide effective insertion of the hybrid proteins AAC-mCYP11A1, Bcs1p(1-83)-mCYP11A1, DLD(1-72)-mCYP11A1 and Su9(1-116)-mCYP11A1 into the mitochondrial inner membrane. preAd-mCYP11A1 hybrid molecules are translocated across the inner membrane and tightly associated with the membrane on its matrix side but not membrane inserted. The mechanism of Ad-mCYP11A1 hybrid topogenesis in Escherichia coli cells differs from that of the topogenesis of its precursor form in yeast mitochondria | synthetic construct | - |
- |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.15.6 | synthetic construct | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.15.6 | 22(R)-hydroxycholesterol + reduced adrenodoxin + O2 | mitochondria containing the AAC-mCYP11A1 hybrid have the highest cholesterol side-chain cleavage activity in the reconstituted system. Ad-mCYP11A1 hybrid demonstrates only residual enzyme activity | synthetic construct | ? + oxidized adrenodoxin + H2O | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.14.15.6 | CYP11A1 | - |
synthetic construct |
1.14.15.6 | cytochrome P450scc | - |
synthetic construct |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.15.6 | adrenodoxin | - |
synthetic construct |