BRENDA - Enzyme Database show
show all sequences of 1.14.15.30

3-Ketosteroid 9alpha-hydroxylase enzymes Rieske non-heme monooxygenases essential for bacterial steroid degradation

Petrusma, M.; van der Geize, R.; Dijkhuizen, L.; Antonie van Leeuwenhoek 106, 157-172 (2014)

Data extracted from this reference:

Application
Application
Commentary
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(Commentary)
Commentary
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); 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); 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); 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
Engineering
Amino acid exchange
Commentary
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
Metals/Ions
Commentary
Organism
Structure
Fe2+
contains non-heme 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
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 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; 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; 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
Rhodococcus rhodochrous
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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 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 + 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 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
-
-
?
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
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Mycolicibacterium smegmatis
-
-
-
Mycolicibacterium smegmatis mc2 155
-
-
-
Rhodococcus erythropolis
-
-
-
Rhodococcus erythropolis SQ1
-
-
-
Rhodococcus jostii
-
-
-
Rhodococcus rhodochrous
-
-
-
Rhodococcus rhodochrous DSM 43269
-
-
-
Mycobacterium tuberculosis
P71875
; isoform KshA
-
Mycobacterium tuberculosis H37Rv
P71875
; isoform KshA
-
Rhodococcus jostii
Q0RXD9
-
-
Rhodococcus jostii
Q0S812
-
-
Reaction
Reaction
Commentary
Organism
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 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
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 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 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 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; 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; 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; 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
Rhodococcus rhodochrous
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
744058
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
744058
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
744058
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
744058
Rhodococcus rhodochrous DSM 43269
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
More
typical head-to-tail trimer arrangement of KshA enzymes, structure overview
Mycobacterium tuberculosis
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 erythropolis
More
typical head-to-tail trimer arrangement of KshA enzymes, structure overview; typical head-to-tail trimer arrangement of KshA enzymes, structure overview; 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
Rhodococcus rhodochrous
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
flavin co-factor of the ferredoxin reductase component KshB
Mycobacterium tuberculosis
FAD
flavin co-factor of the ferredoxin reductase component KshB
Mycolicibacterium smegmatis
FAD
flavin co-factor of the ferredoxin reductase component KshB
Rhodococcus erythropolis
FAD
flavin co-factor of the ferredoxin reductase component KshB; flavin co-factor of the ferredoxin reductase component KshB; flavin co-factor of the ferredoxin reductase component KshB
Rhodococcus jostii
FAD
flavin co-factor of the ferredoxin reductase component KshB
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
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 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; 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; 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; 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
[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
Application (protein specific)
Application
Commentary
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(Commentary) (protein specific)
Commentary
Organism
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); 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 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 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
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
flavin co-factor of the ferredoxin reductase component KshB
Mycobacterium tuberculosis
FAD
flavin co-factor of the ferredoxin reductase component KshB
Mycolicibacterium smegmatis
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
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
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 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; 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
[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
Rhodococcus rhodochrous
Engineering (protein specific)
Amino acid exchange
Commentary
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 (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
contains non-heme 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
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 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
Rhodococcus rhodochrous
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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 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 + 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 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
-
-
?
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
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
-
744058
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
744058
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
744058
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
744058
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
744058
Rhodococcus rhodochrous DSM 43269
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
typical head-to-tail trimer arrangement of KshA enzymes, structure overview
Mycobacterium tuberculosis
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 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
Rhodococcus rhodochrous
General Information
General Information
Commentary
Organism
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
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 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; 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; 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
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
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
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; 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; 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
Rhodococcus rhodochrous
additional information
structure-function relationship of KSH enzymes and components, overview
Mycobacterium tuberculosis
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 erythropolis
additional information
structure-function relationship of KSH enzymes and components, overview; structure-function relationship of KSH enzymes and components, overview; structure-function relationship of KSH enzymes and components, overview
Rhodococcus jostii
additional information
structure-function relationship of KSH enzymes and components, overview
Rhodococcus rhodochrous
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; the enzyme is essential for the pathogenicity of Mycobacterium tuberculosis
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
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
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; 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; 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
General Information (protein specific)
General Information
Commentary
Organism
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
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 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
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
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
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
Rhodococcus rhodochrous
additional information
structure-function relationship of KSH enzymes and components, overview
Mycobacterium tuberculosis
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 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
Rhodococcus rhodochrous
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; the enzyme is essential for the pathogenicity of Mycobacterium tuberculosis
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
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
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
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
Other publictions for EC 1.14.15.30
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745648
Guevara
Functional characterization o ...
Rhodococcus ruber, Rhodococcus ruber Chol-4
J. Steroid Biochem. Mol. Biol.
172
176-187
2017
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1
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1
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4
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6
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22
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22
1
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4
4
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746503
Zhang
Efficient 9alpha-hydroxy-4-an ...
Mycolicibacterium neoaurum, Mycolicibacterium neoaurum JC-12
SpringerPlus
5
1207
2016
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1
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1
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5
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8
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2
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1
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10
2
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1
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5
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8
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1
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1
1
10
2
1
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1
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1
1
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743221
Yao
Characterization and engineer ...
Mycolicibacterium neoaurum, Mycolicibacterium neoaurum ATCC 25795, Mycolicibacterium neoaurum NwIB-01
Metab. Eng.
24
181-191
2014
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1
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1
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1
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3
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4
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1
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1
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1
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1
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744058
Petrusma
3-Ketosteroid 9alpha-hydroxyl ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2 155, Rhodococcus erythropolis, Rhodococcus erythropolis SQ1, Rhodococcus jostii, Rhodococcus rhodochrous, Rhodococcus rhodochrous DSM 43269
Antonie van Leeuwenhoek
106
157-172
2014
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2
2
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1
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5
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22
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15
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5
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28
5
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10
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2
4
14
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1
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7
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22
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28
7
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20
28
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745308
Penfield
Substrate specificities and c ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Rhodococcus rhodochrous, Rhodococcus rhodochrous DSM43269, Rhodococcus rhodochrous DSM 43269
J. Biol. Chem.
289
25523-25536
2014
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1
2
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4
19
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8
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18
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1
2
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54
2
2
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19
2
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3
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2
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3
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6
3
20
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8
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2
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54
3
3
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19
3
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4
6
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17
17
745698
Yeh
Deletion of the gene encoding ...
Rhodococcus hoagii 103S, Rhodococcus hoagii
Microb. Cell Fact.
13
130
2014
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1
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1
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4
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2
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1
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1
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1
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4
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4
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1
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1
1
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717737
Petrusma
Structural features in the Ksh ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous DSM 43269
J. Bacteriol.
194
115-121
2012
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1
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8
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2
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1
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3
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13
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1
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74
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1
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2
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3
4
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16
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4
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2
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3
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3
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74
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2
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1
2
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717735
Petrusma
Multiplicity of 3-ketosteroid- ...
Rhodococcus rhodochrous, Rhodococcus rhodochrous DSM 43269
J. Bacteriol.
193
3931-3940
2011
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1
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1
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4
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19
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1
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1
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75
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1
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1
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6
5
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5
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4
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6
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3
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75
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3
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1
3
11
5
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717854
Capyk
Activity of 3-ketosteroid 9alp ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
286
40717-40724
2011
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-
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13
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2
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9
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30
1
1
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11
1
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1
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21
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30
2
2
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19
2
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2
3
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13
19
713784
Wei
A new steroid-transforming str ...
Mycolicibacterium neoaurum, Mycolicibacterium neoaurum NwIB-01
Appl. Biochem. Biotechnol.
162
1446-1456
2010
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1
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1
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1
1
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716250
Hu
3-Ketosteroid 9alpha-hydroxyla ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Mol. Microbiol.
75
107-121
2010
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152
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4
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2
2
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717500
Fan
Cloning, heterologous expressi ...
Mycobacterium sp., Mycobacterium sp. NwIB-01
Chin. J. Biotechnol.
25
2014-2021
2009
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1
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1
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7
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1
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717784
Capyk
Characterization of 3-ketoster ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
J. Biol. Chem.
284
9937-9946
2009
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1
1
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3
3
717119
Van Der Geize
Characterization of a second R ...
Rhodococcus erythropolis, Rhodococcus erythropolis SQ1
Appl. Environ. Microbiol.
74
7197-7203
2008
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-
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9
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8
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1
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2
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8
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1
2
3
1
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-
717118
Andor
Generation of useful insertion ...
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
Appl. Environ. Microbiol.
72
6554-6559
2006
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1
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1
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2
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1
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1
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718125
Van Der Geize
Molecular and functional chara ...
Rhodococcus erythropolis, Rhodococcus erythropolis SQ1
Mol. Microbiol.
45
1007-1018
2002
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1
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1
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4
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8
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1
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2
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2
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2
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8
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