Application | Comment | Organism |
---|---|---|
drug development | the enzyme can be a target for inhibition in treatment of tuberculosis | Mycobacterium tuberculosis |
medicine | KSH inhibitory compounds may find application in combatting tuberculosis | Mycobacterium tuberculosis |
Cloned (Comment) | Organism |
---|---|
gene kshA1, Rhodococcus jostii RHA1 encodes four sterol catabolic gene clusters, each of which contains a kshA gene, namely ro04538 (kshA1), ro02490 (kshA2), ro05811 (kshA3) and ro09003 (kshA4) | Rhodococcus jostii |
gene kshA2, Rhodococcus jostii RHA1 encodes four sterol catabolic gene clusters, each of which contains a kshA gene, namely ro04538 (kshA1), ro02490 (kshA2), ro05811 (kshA3) and ro09003 (kshA4) | Rhodococcus jostii |
gene kshA3, Rhodococcus jostii RHA1 encodes four sterol catabolic gene clusters, each of which contains a kshA gene, namely ro04538 (kshA1), ro02490 (kshA2), ro05811 (kshA3) and ro09003 (kshA4) | Rhodococcus jostii |
gene kshA4, Rhodococcus jostii RHA1 encodes four sterol catabolic gene clusters, each of which contains a kshA gene, namely ro04538 (kshA1), ro02490 (kshA2), ro05811 (kshA3) and ro09003 (kshA4) | Rhodococcus jostii |
Rhodococcus rhodochrous DSM43269 expresses 5 KshA homologues | Rhodococcus rhodochrous |
Protein Variants | Comment | Organism |
---|---|---|
additional information | a kshA null mutant is constructed by gene deletion mutagenesis (strain RG32) to fully block opening of the steroids polycyclic ring structure of cholesterol and beta-sitosterol resulting in accumulation of 1,4-androstadiene-3,17-dione and 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid | Rhodococcus rhodochrous |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | contains non-heme Fe2+ | Mycobacterium tuberculosis | |
Fe2+ | the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations | Mycolicibacterium smegmatis | |
Fe2+ | the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations | Rhodococcus rhodochrous | |
Fe2+ | the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations | Rhodococcus erythropolis | |
Fe2+ | the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations | Rhodococcus jostii | |
Fe2+ | the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations | Mycobacterium tuberculosis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | Mycolicibacterium smegmatis | - |
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 + 2 H+ + O2 | Rhodococcus rhodochrous | - |
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 + 2 H+ + O2 | Rhodococcus erythropolis | - |
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 + 2 H+ + O2 | Rhodococcus jostii | - |
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 + 2 H+ + O2 | Mycobacterium tuberculosis | - |
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 + 2 H+ + O2 | Mycolicibacterium smegmatis mc2 155 | - |
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 + 2 H+ + O2 | Rhodococcus erythropolis SQ1 | - |
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 + 2 H+ + O2 | Mycobacterium tuberculosis H37Rv | - |
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 + 2 H+ + O2 | Rhodococcus rhodochrous DSM 43269 | - |
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 | Mycolicibacterium smegmatis | - |
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 rhodochrous | - |
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 erythropolis | - |
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 jostii | - |
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 | Mycobacterium tuberculosis | - |
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 | Mycolicibacterium smegmatis mc2 155 | - |
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 erythropolis SQ1 | - |
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 | Mycobacterium tuberculosis H37Rv | - |
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 rhodochrous DSM 43269 | - |
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P71875 | - |
- |
Mycobacterium tuberculosis | P71875 | isoform KshA | - |
Mycobacterium tuberculosis H37Rv | P71875 | - |
- |
Mycobacterium tuberculosis H37Rv | P71875 | isoform KshA | - |
Mycolicibacterium smegmatis | - |
- |
- |
Mycolicibacterium smegmatis mc2 155 | - |
- |
- |
Rhodococcus erythropolis | - |
- |
- |
Rhodococcus erythropolis SQ1 | - |
- |
- |
Rhodococcus jostii | - |
- |
- |
Rhodococcus jostii | Q0RXD9 | - |
- |
Rhodococcus jostii | Q0S812 | - |
- |
Rhodococcus rhodochrous | - |
- |
- |
Rhodococcus rhodochrous DSM 43269 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske iron-sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated | Rhodococcus rhodochrous | |
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske iron-sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated | Rhodococcus jostii | |
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske iron-sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated | Mycobacterium tuberculosis | |
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske ironĀsulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated | Mycolicibacterium smegmatis | |
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske ironĀsulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated | Rhodococcus erythropolis | |
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske ironĀsulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated | Rhodococcus jostii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 | - |
Mycolicibacterium smegmatis | 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 + 2 H+ + O2 | - |
Rhodococcus rhodochrous | 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 + 2 H+ + O2 | - |
Rhodococcus erythropolis | 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 + 2 H+ + O2 | - |
Rhodococcus jostii | 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 + 2 H+ + O2 | - |
Mycobacterium tuberculosis | 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 + 2 H+ + O2 | - |
Mycolicibacterium smegmatis mc2 155 | 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 + 2 H+ + O2 | - |
Rhodococcus erythropolis SQ1 | 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 + 2 H+ + O2 | - |
Mycobacterium tuberculosis H37Rv | 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 + 2 H+ + O2 | - |
Rhodococcus rhodochrous DSM 43269 | 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 + O2 | - |
Mycobacterium tuberculosis | 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 + O2 | - |
Mycobacterium tuberculosis H37Rv | 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 | - |
Mycolicibacterium smegmatis | 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 rhodochrous | 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 erythropolis | 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 jostii | 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 | - |
Mycobacterium tuberculosis | 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 | - |
Mycolicibacterium smegmatis mc2 155 | 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 erythropolis SQ1 | 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 | - |
Mycobacterium tuberculosis H37Rv | 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 rhodochrous DSM 43269 | 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O | - |
? | |
additional information | KSH of Mycobacterium tuberculosis can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids | Mycobacterium tuberculosis | ? | - |
? | |
additional information | KSH of Rhodococcus rhodochrous can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids | Rhodococcus rhodochrous | ? | - |
? | |
additional information | KSH of Mycobacterium tuberculosis can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids | Mycobacterium tuberculosis H37Rv | ? | - |
? | |
additional information | KSH of Rhodococcus rhodochrous can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids | Rhodococcus rhodochrous DSM 43269 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | typical head-to-tail trimer arrangement of KshA enzymes, structure overview | Mycolicibacterium smegmatis |
More | typical head-to-tail trimer arrangement of KshA enzymes, structure overview | Rhodococcus rhodochrous |
More | typical head-to-tail trimer arrangement of KshA enzymes, structure overview | Rhodococcus erythropolis |
More | typical head-to-tail trimer arrangement of KshA enzymes, structure overview | Rhodococcus jostii |
More | typical head-to-tail trimer arrangement of KshA enzymes, structure overview | Mycobacterium tuberculosis |
Synonyms | Comment | Organism |
---|---|---|
3-ketosteroid 9-alpha-hydroxylase | - |
Mycobacterium tuberculosis |
3-ketosteroid 9alpha-hydroxylase | - |
Mycolicibacterium smegmatis |
3-ketosteroid 9alpha-hydroxylase | - |
Rhodococcus rhodochrous |
3-ketosteroid 9alpha-hydroxylase | - |
Rhodococcus erythropolis |
3-ketosteroid 9alpha-hydroxylase | - |
Rhodococcus jostii |
3-ketosteroid 9alpha-hydroxylase | - |
Mycobacterium tuberculosis |
KSH | - |
Mycolicibacterium smegmatis |
KSH | - |
Rhodococcus rhodochrous |
KSH | - |
Rhodococcus erythropolis |
KSH | - |
Rhodococcus jostii |
KSH | - |
Mycobacterium tuberculosis |
KshA | - |
Mycobacterium tuberculosis |
KshA | - |
Rhodococcus jostii |
KshA1 | - |
Rhodococcus jostii |
KshA2 | - |
Rhodococcus jostii |
KshA3 | - |
Rhodococcus jostii |
KshA4 | - |
Rhodococcus jostii |
KshB | - |
Mycobacterium tuberculosis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | flavin co-factor of the ferredoxin reductase component KshB | Mycolicibacterium smegmatis | |
FAD | flavin co-factor of the ferredoxin reductase component KshB | Rhodococcus rhodochrous | |
FAD | flavin co-factor of the ferredoxin reductase component KshB | Rhodococcus erythropolis | |
FAD | flavin co-factor of the ferredoxin reductase component KshB | Rhodococcus jostii | |
FAD | flavin co-factor of the ferredoxin reductase component KshB | Mycobacterium tuberculosis | |
[2Fe-2S]-center | a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits | Mycolicibacterium smegmatis | |
[2Fe-2S]-center | a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits | Rhodococcus rhodochrous | |
[2Fe-2S]-center | a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits | Rhodococcus erythropolis | |
[2Fe-2S]-center | a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits | Rhodococcus jostii | |
[2Fe-2S]-center | a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits | Mycobacterium tuberculosis | |
[2Fe-2S]-center | a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an ironsulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits | Rhodococcus jostii |
General Information | Comment | Organism |
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evolution | KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices | Mycolicibacterium smegmatis |
evolution | KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices | Rhodococcus rhodochrous |
evolution | KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices | Rhodococcus erythropolis |
evolution | KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices | Rhodococcus jostii |
evolution | KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices | Mycobacterium tuberculosis |
malfunction | deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione | Rhodococcus rhodochrous |
malfunction | deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione | Rhodococcus erythropolis |
malfunction | deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione | Rhodococcus jostii |
malfunction | deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione | Mycobacterium tuberculosis |
malfunction | deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione. A kshA disruption mutant of Mycobacterium smegmatis mc2 155 incubated with sitosterol accumulates 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione | Mycolicibacterium smegmatis |
additional information | structure-function relationship of KSH enzymes and components, overview | Mycolicibacterium smegmatis |
additional information | structure-function relationship of KSH enzymes and components, overview | Rhodococcus rhodochrous |
additional information | structure-function relationship of KSH enzymes and components, overview | Rhodococcus erythropolis |
additional information | structure-function relationship of KSH enzymes and components, overview | Rhodococcus jostii |
additional information | structure-function relationship of KSH enzymes and components, overview | Mycobacterium tuberculosis |
physiological function | a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure | Mycolicibacterium smegmatis |
physiological function | a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure | Rhodococcus jostii |
physiological function | a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure | Mycobacterium tuberculosis |
physiological function | a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key-enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure | Rhodococcus jostii |
physiological function | the 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation. KSH initiates opening of the steroid polycyclic ring structure | Rhodococcus rhodochrous |
physiological function | the 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key-enzyme in bacterial steroid degradation. KSH initiates opening of the steroid polycyclic ring structure | Rhodococcus erythropolis |
physiological function | the enzyme is essential for the pathogenicity of Mycobacterium tuberculosis | Mycobacterium tuberculosis |