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Literature summary for 1.14.15.30 extracted from
- Functional characterization of 3-ketosteroid 9alpha-hydroxylases in Rhodococcus ruber strain chol-4 (2017), J. Steroid Biochem. Mol. Biol., 172, 176-187 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene kshA, DNA and amino acid sequence determination and analysis, sequence comparisons | Rhodococcus ruber |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of chol-4 enzyme DELTAkshA1,2,3 deletion mutants, genetic complementation of the DELTAkshA1,2,3 strain with KshA1 perfectly restores growth in CHO or cholic acid but not in androsta-4-ene-3,17-dione, androsta-1,4-diene-3,17-dione or DHEA, whereas the DELTAkshA2,3 does it to certain point. Mutant DELTAKshA3 can only grow using cholesterol as carbon source. KshA2 is only able to act on substrates with a short side chain | Rhodococcus ruber |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | Rhodococcus ruber | - |
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? |  |
| 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | Rhodococcus ruber Chol-4 | - |
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | Rhodococcus ruber | - |
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | Rhodococcus ruber Chol-4 | - |
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodococcus ruber | - |
- |
- |
| Rhodococcus ruber | I0B6I9 | KshA | - |
| Rhodococcus ruber Chol-4 | - |
- |
- |
| Rhodococcus ruber Chol-4 | I0B6I9 | KshA | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| 1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber Chol-4 | 9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Rhodococcus ruber | 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Rhodococcus ruber Chol-4 | 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | 9alpha-hydroxy-4-androsten-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| 4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber Chol-4 | 9alpha-hydroxy-4-androsten-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Rhodococcus ruber | 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Rhodococcus ruber Chol-4 | 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| cholestenone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | ? | - |
? | |
| cholestenone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber Chol-4 | ? | - |
? | |
| cholic acid + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | ? | - |
? | |
| cholic acid + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber Chol-4 | ? | - |
? | |
| dehydroepiandrosterone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | ? | - |
? | |
| dehydroepiandrosterone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber Chol-4 | ? | - |
? | |
| dehydroepiandrosterone + NADH + H+ + O2 | - |
Rhodococcus ruber | 3beta,9alpha-dihydroxy-5-androstene-17-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| dehydroepiandrosterone + NADH + H+ + O2 | - |
Rhodococcus ruber Chol-4 | 3beta,9alpha-dihydroxy-5-androstene-17-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
| additional information | isozyme KshA2 is only able to act on substrates with a short side chain in Rhodococcus ruber | Rhodococcus ruber | ? | - |
? | |
| additional information | isozyme KshA2 is only able to act on substrates with a short side chain in Rhodococcus ruber | Rhodococcus ruber Chol-4 | ? | - |
? | |
| phytosterol + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | ? | - |
? | |
| pregnenolone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | ? | - |
? | |
| sodium acetate + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | ? | - |
? | |
| testosterone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2 | - |
Rhodococcus ruber | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | enzyme domain structure, molecular modelling of KshA, structure comparisons of KshAB enzyme, detailed overview | Rhodococcus ruber |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| 3-ketosteroid 9alpha-hydroxylase | - |
Rhodococcus ruber |
| 3-ketosteroid-9alpha-hydroxylase | - |
Rhodococcus ruber |
| androsta-1,4-diene-3,17-dione, NADH:oxygen oxidoreductase (9alpha-hydroxylating) | - |
Rhodococcus ruber |
| KshA | - |
Rhodococcus ruber |
| KshA1 | isoform | Rhodococcus ruber |
| KshA2 | isoform | Rhodococcus ruber |
| KshA3 | isoform | Rhodococcus ruber |
| KshAB | - |
Rhodococcus ruber |
| KshB | - |
Rhodococcus ruber |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | Rhodococcus ruber strains devoid of any KshAB activity (DELTAkshB or DELTAkshA1,2,3 strains) are able to grow in cholesterol although 10times slower than the wild-type strain. This growth is due to the degradation of the side chain, a process that has been described to occur at different steps of the pathway being independent of the polycyclic ring opening. In the strain the side chain degradation process does not depend on any KshAB activity | Rhodococcus ruber |
| metabolism | isoform KshA1 is a more versatile enzyme related to the cholic acid catabolism, although it also collaborates with KshA2 or KshA3 activities in the catabolism of steroids | Rhodococcus ruber |
| additional information | molecular modelling of KshA, structure comparisons of KshAB enzyme, detailed overview | Rhodococcus ruber |
| physiological function | 3-ketosteroid-9alpha-hydroxylase is a key enzyme in the general scheme of the bacterial steroid catabolism in combination with a 3-ketosteroid-DELTA1-dehydrogenase activity (KstD), being both responsible of the steroid nucleus (rings A/B) breakage. KshAB initiates the opening of the steroid ring by the 9alpha-hydroxylation of the C9 carbon of 4-ene-3-oxosteroids (e.g. AD) or 1,4-diene-3-oxosteroids (e.g. ADD), transforming them into 9alpha-hydroxy-4-androsten-3,17-dione or 9alpha-hydroxy-1,4-androstadiene-3,17-dione, respectively | Rhodococcus ruber |
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Release 2023.1 (January 2023)
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