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Enzyme Nomenclature
Information on EC 1.14.13.142 - 3-ketosteroid 9alpha-monooxygenase
Word Map on EC 1.14.13.142
- 1.14.13.142
- 3-ketosteroids
- cholesterol
-
rieske
- tuberculosis
-
two-component
-
bile
- erythropolis
- rhodochrous
- 4-androstene-3,17-dione
-
cholic
- iron
-
mouth
- oxygenases
- coa
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.142
-
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RECOMMENDED NAME
GeneOntology No.
3-ketosteroid 9alpha-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
androsta-1,4-diene-3,17-dione + NADH + H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
androsta-1,4-diene-3,17-dione,NADH:oxygen oxidoreductase (9alpha-hydroxylating)
The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It is a two-component system consisting of a terminal oxygenase (KshA) and a ferredoxin reductase (KshB). The oxygenase contains a Rieske-type iron-sulfur center and non-heme iron. The reductase component is a flavoprotein containing an NAD-binding domain and a plant-type iron-sulfur cluster. The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
terminal oxygenase of 3-ketosteroid 9alpha-hydroxylase
UniProt
terminal oxygenase of 3-ketosteroid 9alpha-hydroxylase
UniProt
gene kshA; the enzyme harbors a Rieske oxygenase, encoded by kshA
UniProt
gene kshB; the enzyme harbors a reductase, encoded by kshB
UniProt
gene kshA; the enzyme harbors a Rieske oxygenase, encoded by kshA
UniProt
gene kshB; the enzyme harbors a reductase, encoded by kshB
UniProt
component KshA of 3-ketosteroid 9alpha-hydroxylase
UniProt
component KshB of 3-ketosteroid 9alpha-hydroxylase
UniProt
gene kshA1 encodes an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase; isozyme KshA1
UniProt
gene kshA1, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase; isozyme KshA1
UniProt
gene kshA5 encodes an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase; isozyme KshA5
UniProt
gene kshA5, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase; isozyme KshA5
UniProt
gene kshA1 encodes an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase; isozyme KshA1
UniProt
gene kshA1, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase; isozyme KshA1
UniProt
gene kshA5 encodes an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase; isozyme KshA5
UniProt
gene kshA5, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase; isozyme KshA5
UniProt
gene kshB, encoding the ferredoxin reductase
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
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DELTAkshA and DELTAkshB deletion mutants are unable to use cholesterol and 4-androstene-3,17-dione as primary carbon and energy sources and are unable to metabolize 5alpha-androstane-3,17-dione. The deletion of either of these genes leads to rapid death of the microorganism in murine infection models and in macrophages
malfunction
gene deletion of kshA2 does not affect growth on 9alpha-hydroxy-4-androstene-3,17-dione, cholesterol, or cholic acid
malfunction
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DELTAkshA and DELTAkshB deletion mutants are unable to use cholesterol and 4-androstene-3,17-dione as primary carbon and energy sources and are unable to metabolize 5alpha-androstane-3,17-dione. The deletion of either of these genes leads to rapid death of the microorganism in murine infection models and in macrophages
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malfunction
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gene deletion of kshA2 does not affect growth on 9alpha-hydroxy-4-androstene-3,17-dione, cholesterol, or cholic acid
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metabolism
3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism
metabolism
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3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism
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physiological function
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3-ketosteroid 9alpha-hydroxylase is an essential factor in the pathogenesis of Mycobacterium tuberculosis
physiological function
3-ketosteroid 9alpha-hydroxylase is a key enzyme in microbial steroid degradation in Rhodococcus erythropolis strain SQ1 and is comprised of the terminal oxygenase component KshA1 and the oxygenase-reductase component KshB, a terminal oxygenase homologue KshA2 and homologue KshA3. Component KshA2 plays a role in preventing accumulation of toxic intracellular concentrations of 1,4-androstadiene-3,17-dione during steroid catabolism; 3-ketosteroid 9alpha-hydroxylase is a key enzyme in microbial steroid degradation in Rhodococcus erythropolis strain SQ1 and is comprised of the terminal oxygenase component KshA1 and the oxygenase-reductase component KshB, a terminal oxygenase homologue KshA2 and homologue KshA3. Component KshA2 plays a role in preventing accumulation of toxic intracellular concentrations of 1,4-androstadiene-3,17-dione during steroid catabolism
physiological function
3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid catabolism. Isozyme KshA1 is dedicated to cholic acid catabolism. Presence of multiple kshA genes in the Rhodococcus rhodochrous DSM43269 genome, each displaying unique steroid induction patterns and substrate ranges, appears to facilitate a dynamic and fine-tuned steroid catabolism, with C-9 alpha-hydroxylation occurring at different levels during microbial steroid degradation; 3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid catabolism. Isozyme KshA5 appears to be the most versatile enzyme, with the broadest substrate range but without a clear substrate preference. Presence of multiple kshA genes in the Rhodococcus rhodochrous DSM 43269 genome, each displaying unique steroid induction patterns and substrate ranges, appears to facilitate a dynamic and fine-tuned steroid catabolism, with C-9 alpha-hydroxylation occurring at different levels during microbial steroid degradation
physiological function
the enzyme plays a role of cholesterol catabolism, overview; the enzyme plays a role of cholesterol catabolism, overview
physiological function
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3-ketosteroid 9alpha-hydroxylase is an essential factor in the pathogenesis of Mycobacterium tuberculosis; the enzyme plays a role of cholesterol catabolism, overview; the enzyme plays a role of cholesterol catabolism, overview
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physiological function
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3-ketosteroid 9alpha-hydroxylase is a key enzyme in microbial steroid degradation in Rhodococcus erythropolis strain SQ1 and is comprised of the terminal oxygenase component KshA1 and the oxygenase-reductase component KshB, a terminal oxygenase homologue KshA2 and homologue KshA3. Component KshA2 plays a role in preventing accumulation of toxic intracellular concentrations of 1,4-androstadiene-3,17-dione during steroid catabolism; 3-ketosteroid 9alpha-hydroxylase is a key enzyme in microbial steroid degradation in Rhodococcus erythropolis strain SQ1 and is comprised of the terminal oxygenase component KshA1 and the oxygenase-reductase component KshB, a terminal oxygenase homologue KshA2 and homologue KshA3. Component KshA2 plays a role in preventing accumulation of toxic intracellular concentrations of 1,4-androstadiene-3,17-dione during steroid catabolism
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physiological function
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3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid catabolism; 3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid catabolism. Isozyme KshA1 is dedicated to cholic acid catabolism. Presence of multiple kshA genes in the Rhodococcus rhodochrous DSM43269 genome, each displaying unique steroid induction patterns and substrate ranges, appears to facilitate a dynamic and fine-tuned steroid catabolism, with C-9 alpha-hydroxylation occurring at different levels during microbial steroid degradation; 3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid catabolism. Isozyme KshA5 appears to be the most versatile enzyme, with the broadest substrate range but without a clear substrate preference. Presence of multiple kshA genes in the Rhodococcus rhodochrous DSM 43269 genome, each displaying unique steroid induction patterns and substrate ranges, appears to facilitate a dynamic and fine-tuned steroid catabolism, with C-9 alpha-hydroxylation occurring at different levels during microbial steroid degradation
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additional information
KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme
additional information
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KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme
additional information
determination of the enzyme's substrate preference, three-dimensional structure modeling of KshA1, overview. The variable loop within the beta-sheet plays a role in the substrate preference of KshA enzymes; determination of the enzyme's substrate preference, three-dimensional structure modeling of KshA5, overview. The variable loop within the beta-sheet plays a role in the substrate preference of KshA enzymes
additional information
determination of the enzyme's substrate preference, three-dimensional structure modeling of KshA1, overview. The variable loop within the beta-sheet plays a role in the substrate preference of KshA enzymes; determination of the enzyme's substrate preference, three-dimensional structure modeling of KshA5, overview. The variable loop within the beta-sheet plays a role in the substrate preference of KshA enzymes
additional information
enzyme substrate binding pocket analysis using molecular modeling, overview. Modeling of substrates into KshA crystal structure using KshA structure PDB 2ZYL
additional information
enzyme substrate binding pocket analysis using molecular modeling, overview. Modeling of substrates into KshA crystal structure using KshA structure PDB 2ZYL
additional information
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enzyme substrate binding pocket analysis using molecular modeling, overview. Modeling of substrates into KshA crystal structure using KshA structure PDB 2ZYL
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additional information
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determination of the enzyme's substrate preference, three-dimensional structure modeling of KshA1, overview. The variable loop within the beta-sheet plays a role in the substrate preference of KshA enzymes; determination of the enzyme's substrate preference, three-dimensional structure modeling of KshA5, overview. The variable loop within the beta-sheet plays a role in the substrate preference of KshA enzymes; KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme; KshA and KshB together constitute the KSH enzyme
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,4-androstadiene-3,17-dione + O2 + NADH + H+
3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione + H2O + NAD+
1-(5alpha)-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + NAD+ + H2O
11beta-hydrocortisone + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + NAD+ + H2O
3-oxo-23,24-bisnorchol-4-en-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
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-
-
?
3-oxo-23,24-bisnorchol-4-en-22-oic acid-CoA + O2 + NADH + H+
?
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-
-
?
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
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-
-
?
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA + O2 + NADH + H+
?
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-
?
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + NADH + H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + NAD+ + H2O
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate-CoA + NADH + H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate-CoA + NAD+ + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-4-ene-22-oate + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oate + NAD+ + H2O
3-oxo-23,24-bisnorcholesta-4-ene-22-oic acid + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oic acid + NAD+ + H2O
3-oxo-23,24-bisnorcholesta-4-ene-22-oyl-CoA + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oyl-CoA + NAD+ + H2O
4-androstene-17beta-ol-3-one + NADH + H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + NAD+ + H2O
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-
-
?
4-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + NAD+ + H2O
4-androstene-3,17-dione + O2 + NADH + H+
9alpha-hydroxy-4-androstene-3,17-dione + H2O + NAD+
4-androstene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-4-en-3,17-dione + H2O + NAD+
4-pregnene-3,20-dione + NADH + H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + NAD+ + H2O
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-
-
?
5alpha-androstane-17beta-ol-3-one + NADH + H+ + O2
9alpha,17beta-dihydroxy-5alpha-androstane-3-one + NAD+ + H2O
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-
-
?
5alpha-androstane-17beta-ol-3-one + NADH + H+ + O2
? + NAD+ + H2O
i.e. stanolon, the wild type homologue KshA5 shows 100% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-17beta-ol-3-one + O2 + NADH + H+
? + H2O + NAD+
i.e. stanolon, isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + NAD+ + H2O
-
-
-
?
5beta-androstane-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-5beta-androstane-3,17-dione + NAD+ + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + NADH + H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
1,4-androstadiene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA1 shows 244% activity compared to 4-androstene-3,17-dione
-
-
?
1,4-androstadiene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 51% activity compared to 4-androstene-3,17-dione
-
-
?
1,4-androstadiene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA1 shows 244% activity compared to 4-androstene-3,17-dione
-
-
?
1,4-androstadiene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 51% activity compared to 4-androstene-3,17-dione
-
-
?
1,4-androstadiene-3,17-dione + O2 + NADH + H+
3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione + H2O + NAD+
best substrate, the substrate is twice as efficient as : 4-androstene-3,17-dione
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-
ir
1,4-androstadiene-3,17-dione + O2 + NADH + H+
3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione + H2O + NAD+
best substrate, the substrate is twice as efficient as : 4-androstene-3,17-dione
-
-
ir
1-(5alpha)-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + NAD+ + H2O
-
-
-
?
1-(5alpha)-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + NAD+ + H2O
-
-
-
?
1-(5alpha)-androstene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA1 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 99% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA1 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 99% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 28% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 68% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 68% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 28% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
11beta-hydrocortisone + NADH + H+ + O2
9alpha-hydroxy-11beta-hydrocortisone + NAD+ + H2O
-
-
-
?
11beta-hydrocortisone + NADH + H+ + O2
9alpha-hydroxy-11beta-hydrocortisone + NAD+ + H2O
-
-
-
?
11beta-hydrocortisone + O2 + NADH + H+
? + H2O + NAD+
i.e. stanolon, isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
11beta-hydrocortisone + O2 + NADH + H+
? + H2O + NAD+
i.e. stanolon, isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + NAD+ + H2O
-
-
-
?
19-nor-4-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + NAD+ + H2O
-
-
-
?
19-nor-4-androstene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
i.e. nordion, the wild type homologue KshA1 shows 24% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
i.e. nordion, the wild type homologue KshA5 shows 111% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 24% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 10% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 78% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 107% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 78% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 24% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 10% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 107% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor cholesta-4-ene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 500% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor cholesta-4-ene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 124% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor cholesta-4-ene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor cholesta-4-ene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 80% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor cholesta-4-ene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor cholesta-4-ene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 500% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor cholesta-4-ene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 124% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor-cholesta-1,4-diene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 423% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor-cholesta-1,4-diene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 176% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor-cholesta-1,4-diene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 22% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor-cholesta-1,4-diene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 43% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor-cholesta-1,4-diene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 22% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bis-nor-cholesta-1,4-diene-22-oic acid + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 176% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholesta-4-ene-22-oic acid + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA1 shows 548% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholesta-4-ene-22-oic acid + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 88% activity compared to 4-androstene-3,17-dione
-
-
?
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + NADH + H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + NAD+ + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + NADH + H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + NAD+ + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-4-ene-22-oate + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oate + NAD+ + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-4-ene-22-oate + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oate + NAD+ + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-4-ene-22-oic acid + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oic acid + NAD+ + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-4-ene-22-oic acid + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oic acid + NAD+ + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-4-ene-22-oyl-CoA + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oyl-CoA + NAD+ + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-4-ene-22-oyl-CoA + NADH + H+ + O2
3-oxo-9alpha-hydroxy-23,24-bisnorcholesta-4-ene-22-oyl-CoA + NAD+ + H2O
-
-
-
?
3-oxosteroid + NADH + H+ + O2
9alpha-hydroxysteroid + NAD+ + H2O
-
-
-
?
3-oxosteroid + NADH + H+ + O2
9alpha-hydroxysteroid + NAD+ + H2O
-
-
-
?
4-androstene-17beta-ol-3-one + NADH + H+ + O2
? + NAD+ + H2O
i.e. testosterone, the wild type homologue KshA1 shows 158% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + NADH + H+ + O2
? + NAD+ + H2O
i.e. testosterone, the wild type homologue KshA5 shows 113% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 127% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 94% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 101% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 113% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + NAD+ + H2O
-
-
-
?
4-androstene-3,17-dione + NADH + H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + NAD+ + H2O
-
-
-
?
4-androstene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA1 shows 100% activity
-
-
?
4-androstene-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 100% activity
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
9alpha-hydroxy-4-androstene-3,17-dione + H2O + NAD+
-
-
-
-
4-androstene-3,17-dione + O2 + NADH + H+
9alpha-hydroxy-4-androstene-3,17-dione + H2O + NAD+
-
-
-
-
4-androstene-3,17-dione + O2 + NADH + H+
9alpha-hydroxy-4-androstene-3,17-dione + H2O + NAD+
-
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
9alpha-hydroxy-4-androstene-3,17-dione + H2O + NAD+
-
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-4-en-3,17-dione + H2O + NAD+
-
-
-
ir
4-androstene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-4-en-3,17-dione + H2O + NAD+
-
-
-
ir
4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
-
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 100% activity
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 100% activity
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 100% activity
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 100% activity
-
-
?
4-cholestene-3-one + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 13% activity compared to 4-androstene-3,17-dione
-
-
?
4-cholestene-3-one + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
4-cholestene-3-one + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 26% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + NADH + H+ + O2
? + NAD+ + H2O
i.e. progesterone, the wild type homologue KshA1 shows 372% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + NADH + H+ + O2
? + NAD+ + H2O
i.e. progesterone, the wild type homologue KshA5 shows 65% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 423% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 112% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 99% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 67% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA1 shows 12% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 73% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
-
-
-
-
?
5alpha-androstane-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
-
-
-
-
?
5alpha-androstane-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 9% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 64% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 80% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA1 shows 19% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + NADH + H+ + O2
? + NAD+ + H2O
the wild type homologue KshA5 shows 99% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA1 shows 19% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA4 shows 58% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + NADH + H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + NADH + H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + NADH + H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + NADH + H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
ir
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
ir
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
isozyme KshA1 shows 288% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
isozyme KshA3 shows 194% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
isozyme KshA4 shows 89% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
isozyme KshA5 shows 49% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + O2 + NADH + H+
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + H2O + NAD+
-
-
-
?
additional information
?
-
substrate specificity, overview. KshAB also transforms CoA thioester steroids
-
-
-
additional information
?
-
substrate specificity, overview. KshAB also transforms CoA thioester steroids
-
-
-
additional information
?
-
substrate specificity, overview. KshAB also transforms CoA thioester steroids
-
-
-
additional information
?
-
substrate specificity, overview. KshAB also transforms CoA thioester steroids
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
the KshA1 homologue has a narrow substrate range with a high preference for 23,24-bisnorcholesta-4-ene-22-oic acid and 23,24-bisnorcholesta-1,4-diene-22-oic acid and preference to a lesser extent for 1,4-androstadiene-3,17-dione and 4-pregnene-3,20-dione (progesterone)
-
-
-
additional information
?
-
the KshA1 homologue has a narrow substrate range with a high preference for 23,24-bisnorcholesta-4-ene-22-oic acid and 23,24-bisnorcholesta-1,4-diene-22-oic acid and preference to a lesser extent for 1,4-androstadiene-3,17-dione and 4-pregnene-3,20-dione (progesterone)
-
-
-
additional information
?
-
the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids
-
-
-
additional information
?
-
the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids
-
-
-
additional information
?
-
the wild type homologue KshA1 shows no activity with 5alpha-androstane-17beta-ol-3-one (stanolon), 5-cholestene-3beta-ol (cholesterol), 3alpha-hydroxy-5alpha-pregnane-20-one, 11beta-hydrocortisone, 3beta-hydroxy-5alpha-androstane-17-one, and 9alpha-hydroxy-4-androstene-3,17-dione
-
-
-
additional information
?
-
the wild type homologue KshA1 shows no activity with 5alpha-androstane-17beta-ol-3-one (stanolon), 5-cholestene-3beta-ol (cholesterol), 3alpha-hydroxy-5alpha-pregnane-20-one, 11beta-hydrocortisone, 3beta-hydroxy-5alpha-androstane-17-one, and 9alpha-hydroxy-4-androstene-3,17-dione
-
-
-
additional information
?
-
the wild type homologue KshA5 shows no activity with 5-cholestene-3beta-ol, 3alpha-hydroxy-5beta-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, and 9alpha-hydroxy-4-androstene-3,17-dione
-
-
-
additional information
?
-
the wild type homologue KshA5 shows no activity with 5-cholestene-3beta-ol, 3alpha-hydroxy-5beta-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, and 9alpha-hydroxy-4-androstene-3,17-dione
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
substrate specificities of KshA variants, overview. No activity by all enzymes with 3alpha-hydroxy-5alpha-pregnane-20-one, 9alpha-hydroxy-4-androstene-3,17-dione, 5-cholestene-3beta-ol, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
substrate specificities of KshA variants, overview. No activity by all enzymes with 3alpha-hydroxy-5alpha-pregnane-20-one, 9alpha-hydroxy-4-androstene-3,17-dione, 5-cholestene-3beta-ol, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 4-cholestene-3-one, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
the KshA1 homologue has a narrow substrate range with a high preference for 23,24-bisnorcholesta-4-ene-22-oic acid and 23,24-bisnorcholesta-1,4-diene-22-oic acid and preference to a lesser extent for 1,4-androstadiene-3,17-dione and 4-pregnene-3,20-dione (progesterone)
-
-
-
additional information
?
-
the KshA1 homologue has a narrow substrate range with a high preference for 23,24-bisnorcholesta-4-ene-22-oic acid and 23,24-bisnorcholesta-1,4-diene-22-oic acid and preference to a lesser extent for 1,4-androstadiene-3,17-dione and 4-pregnene-3,20-dione (progesterone)
-
-
-
additional information
?
-
the wild type homologue KshA1 shows no activity with 5alpha-androstane-17beta-ol-3-one (stanolon), 5-cholestene-3beta-ol (cholesterol), 3alpha-hydroxy-5alpha-pregnane-20-one, 11beta-hydrocortisone, 3beta-hydroxy-5alpha-androstane-17-one, and 9alpha-hydroxy-4-androstene-3,17-dione
-
-
-
additional information
?
-
the wild type homologue KshA1 shows no activity with 5alpha-androstane-17beta-ol-3-one (stanolon), 5-cholestene-3beta-ol (cholesterol), 3alpha-hydroxy-5alpha-pregnane-20-one, 11beta-hydrocortisone, 3beta-hydroxy-5alpha-androstane-17-one, and 9alpha-hydroxy-4-androstene-3,17-dione
-
-
-
additional information
?
-
substrate specificities of KshA variants, overview. No activity by all enzymes with 3alpha-hydroxy-5alpha-pregnane-20-one, 9alpha-hydroxy-4-androstene-3,17-dione, 5-cholestene-3beta-ol, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
substrate specificities of KshA variants, overview. No activity by all enzymes with 3alpha-hydroxy-5alpha-pregnane-20-one, 9alpha-hydroxy-4-androstene-3,17-dione, 5-cholestene-3beta-ol, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
no activity with 5alpha-androstane-3,17-dione, 5beta-androstane-3,17-dione, 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, 5alpha-androstane-17beta-ol-3-one (stanolon) and 11beta-hydrocortisone
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
isozyme KshA5 is the most versatile isoenzyme, with the broadest substrate range but without a clear substrate preference. It shows no activity with 5-cholestene-3beta-ol (cholesterol), 5alpha-androstane-17-one, 3alpha-hydroxy-5alpha-pregnane-20-one, and 3beta-hydroxy-5alpha-androstane-17-one
-
-
-
additional information
?
-
the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids
-
-
-
additional information
?
-
the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids
-
-
-
additional information
?
-
the wild type homologue KshA5 shows no activity with 5-cholestene-3beta-ol, 3alpha-hydroxy-5beta-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, and 9alpha-hydroxy-4-androstene-3,17-dione
-
-
-
additional information
?
-
the wild type homologue KshA5 shows no activity with 5-cholestene-3beta-ol, 3alpha-hydroxy-5beta-pregnane-20-one, 3beta-hydroxy-5alpha-androstane-17-one, and 9alpha-hydroxy-4-androstene-3,17-dione
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-oxo-23,24-bisnorchol-4-en-22-oic acid-CoA + O2 + NADH + H+
?
P71875, P9WJ93
-
-
-
?
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA + O2 + NADH + H+
?
P71875, P9WJ93
-
-
-
?
androsta-1,4-diene-3,17-dione + NADH + H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
androsta-1,4-diene-3,17-dione + NADH + H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
F1CMX0, F1CMY8
-
-
-
?
androsta-1,4-diene-3,17-dione + NADH + H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + NAD+ + H2O
F1CMX0, F1CMY8
-
-
-
?
additional information
?
-
B6V6V5
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMX0
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMX3
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMX6
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMX8
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMY8
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
-
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
B6V6V5
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMX0
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMX3
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMX6
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMX8
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
-
-
-
additional information
?
-
F1CMY8
all KSH enzymes with KshADSM43269 isozymes are C-9alpha-hydroxylases acting on a wide range of 3-oxosteroids, but not on 3-hydroxysteroids
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-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
Rieske-type Fe-S cluster, Rieske monooxygenase
[2Fe-2S]-center
8.2 mol of iron and 2.4 mol of sulfur per mol of KshA protomer
additional information
a Rieske nonheme monooxygenase; a Rieske nonheme monooxygenase
-
additional information
a Rieske nonheme monooxygenase; a Rieske nonheme monooxygenase
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
the enzyme contains a nonheme Fe2+; the enzyme contains a nonheme Fe2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
1,4-Androstadiene-3,17-dione
in 0.1 M potassium phosphate, pH 7.0, at 25°C
0.01
23,24-bisnorcholesta-4-ene-22-oic acid
Km less than 0.01 mM, isoform KshA1, in 50mMTris-HCl buffer (pH 7.0), temperature not specified in the publication; Km less than 0.01 mM, isoform KshA5, in 50 mM Tris-HCl buffer (pH 7.0), temperature not specified in the publication
0.003
3-oxo-23,24-bisnorchol-4-en-22-oic acid
in 0.1 M potassium phosphate, pH 7.0, at 22°C
0.0068
3-oxo-23,24-bisnorchol-4-en-22-oic acid-CoA
in 0.1 M potassium phosphate, pH 7.0, at 22°C
0.07
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid
in 0.1 M potassium phosphate, pH 7.0, at 22°C
0.017
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA
in 0.1 M potassium phosphate, pH 7.0, at 22°C
0.07
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
-
0.017
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate-CoA
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
-
0.003
3-oxo-23,24-bisnorcholesta-4-ene-22-oate
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
0.0068
3-oxo-23,24-bisnorcholesta-4-ene-22-oyl-CoA
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
0.024
4-androstene-3,17-dione
in 0.1 M potassium phosphate, pH 7.0, at 25°C
0.024
4-androstene-3,17-dione
in 0.1 M potassium phosphate, pH 7.0, at 22°C; pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
0.1 - 1
androsta-1,4-diene-3,17-dione
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
0.11
androsta-1,4-diene-3,17-dione
in 0.1 M potassium phosphate, pH 7.0, at 22°C
0.09
O2
apparent Km value, in the presence of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA, in 0.1 M potassium phosphate, pH 7.0, at 22°C
1.2
O2
in the presence of 1,4-androstadiene-3,17-dione, Km above 1.2 mM, in 0.1 M potassium phosphate, pH 7.0, at 25°C
additional information
additional information
kinetic analysis of the activity of KshA mutants with 4-23,24-bisnorcholesta-4-ene-22-oic acid; kinetic analysis of the activity of KshA mutants with 4-23,24-bisnorcholesta-4-ene-22-oic acid
-
additional information
additional information
kinetic analysis of the activity of KshA mutants with 4-23,24-bisnorcholesta-4-ene-22-oic acid; kinetic analysis of the activity of KshA mutants with 4-23,24-bisnorcholesta-4-ene-22-oic acid
-
additional information
additional information
steady-state kinetic parameters for KshAB, overview; steady-state kinetic parameters for KshAB, overview
-
additional information
additional information
steady-state kinetic parameters for KshAB, overview; steady-state kinetic parameters for KshAB, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
1,4-Androstadiene-3,17-dione
Mycobacterium tuberculosis
P71875
in 0.1 M potassium phosphate, pH 7.0, at 25°C
0.08
3-oxo-23,24-bisnorchol-4-en-22-oic acid
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
0.61
3-oxo-23,24-bisnorchol-4-en-22-oic acid-CoA
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
0.25
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
2.7
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
0.25
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
-
2.7
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate-CoA
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
-
0.08
3-oxo-23,24-bisnorcholesta-4-ene-22-oate
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
0.61
3-oxo-23,24-bisnorcholesta-4-ene-22-oyl-CoA
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
0.8
androsta-1,4-diene-3,17-dione
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C; pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
0.07
4-androstene-3,17-dione
Mycobacterium tuberculosis
P71875
in 0.1 M potassium phosphate, pH 7.0, at 25°C
0.07
4-androstene-3,17-dione
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C; pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
2.5
O2
Mycobacterium tuberculosis
P71875, P9WJ93
apparent Km value, in the presence of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA, in 0.1 M potassium phosphate, pH 7.0, at 22°C
7
O2
Mycobacterium tuberculosis
P71875
in the presence of 1,4-androstadiene-3,17-dione, kcat above 7 1/sec, in 0.1 M potassium phosphate, pH 7.0, at 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.6
1,4-Androstadiene-3,17-dione
Mycobacterium tuberculosis
P71875
in 0.1 M potassium phosphate, pH 7.0, at 25°C
5451
30
3-oxo-23,24-bisnorchol-4-en-22-oic acid
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
41908
90
3-oxo-23,24-bisnorchol-4-en-22-oic acid-CoA
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
41910
3.5
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
41909
160
3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
41911
3.57
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
194803
158.8
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate-CoA
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
194805
26.67
3-oxo-23,24-bisnorcholesta-4-ene-22-oate
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
194802
89.71
3-oxo-23,24-bisnorcholesta-4-ene-22-oyl-CoA
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
194804
2.917
4-androstene-3,17-dione
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
1186
3
4-androstene-3,17-dione
Mycobacterium tuberculosis
P71875
in 0.1 M potassium phosphate, pH 7.0, at 25°C
1186
3
4-androstene-3,17-dione
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
1186
7.27
androsta-1,4-diene-3,17-dione
Mycobacterium tuberculosis
P71875, P9WJ93
pH 7.0, 22°C, KshAB; pH 7.0, 22°C, KshAB
28534
7.6
androsta-1,4-diene-3,17-dione
Mycobacterium tuberculosis
P71875, P9WJ93
in 0.1 M potassium phosphate, pH 7.0, at 22°C
28534
2.45
O2
Mycobacterium tuberculosis
P71875
in the presence of 1,4-androstadiene-3,17-dione, in 0.1 M potassium phosphate, pH 7.0, at 25°C
9
29
O2
Mycobacterium tuberculosis
P71875, P9WJ93
apparent Km value, in the presence of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA, in 0.1 M potassium phosphate, pH 7.0, at 22°C
9
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview
additional information
cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview
additional information
cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview
additional information
cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview
additional information
cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview
additional information
-
cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview
additional information
-
cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview; cell growth on different steroids as a sole carbon and energy source with different isozymes, overview
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme comprises a Rieske oxygenase, encoded by kshA, and a reductase, encoded by kshB; the enzyme comprises a Rieske oxygenase, encoded by kshA, and a reductase, encoded by kshB
additional information
the enzyme comprises a Rieske oxygenase, encoded by kshA, and a reductase, encoded by kshB; the enzyme comprises a Rieske oxygenase, encoded by kshA, and a reductase, encoded by kshB
additional information
-
the enzyme comprises a Rieske oxygenase, encoded by kshA, and a reductase, encoded by kshB; the enzyme comprises a Rieske oxygenase, encoded by kshA, and a reductase, encoded by kshB
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
component KshA, sitting drop vapor diffusion method, using 1.1 M sodium malonate, 0.1 M HEPES, pH 7.0, and 0.5% (v/v) Jeffamine M600
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurification of recombinant His-tagged KshA mutants with His-tagged KshB; copurification of recombinant His-tagged KshA mutants with His-tagged KshB; copurification of recombinant His-tagged KshA mutants with His-tagged KshB
Ni2+-NTA agarose column chromatography and Source15Q column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) and C41(DE3) cells; expressed in Escherichia coli BL21(DE3) and C41(DE3) cells; expressed in Escherichia coli BL21(DE3) and C41(DE3) cells; expressed in Escherichia coli BL21(DE3) and C41(DE3) cells; expressed in Escherichia coli BL21(DE3) and C41(DE3) cells; gene kshA1, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase, phylogenetic analysis and tree. Transcriptional analysis and functional complementation of kshA null mutant strain RG32 by genes kshA1-55, overview. recombinant expression of kshA in Escherichia coli strains Bl21(DE3) and C41(DE3); gene kshA5, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase, phylogenetic analysis and tree. Transcriptional analysis and functional complementation of kshA null mutant strain RG32 by genes kshA1-55, overview. kshA5 supports growth on any of the different classes of steroids tested, consistent with its broad expression induction pattern. Recombinant expression of kshA in Escherichia coli strains Bl21(DE3) and C41(DE3); gene kshB, recombinant expression of kshB in Escherichia coli strains Bl21(DE3) and C41(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli C41(DE3) cells; expressed in Escherichia coli C41(DE3) cells; expression of chimeric kshA mutant genes, KshA1A5beta and KshA5A1beta, in Escherichia coli, coexpression of the His-tagged KshA mutants with His-tagged KshB, molar ratio of KshA5A1/KshB is 1:8, low expression level of soluble KshA5A1alpha enzyme; expression of chimeric kshA mutant genes, KshA1A5beta and KshA5A1beta, in Escherichia coli, coexpression of the His-tagged KshA mutants with His-tagged KshB, molar ratio of KshA5A1/KshB is 1:8, low expression level of soluble KshA5A1alpha enzyme; expression of chimeric kshA mutant genes, KshA1A5beta and KshA5A1beta, in Escherichia coli, coexpression of the His-tagged KshA mutants with His-tagged KshB, molar ratio of KshA5A1/KshB is 1:8, low expression level of soluble KshA5A1alpha enzyme
the terminal oxygenase component of 3-ketosteroid 9alpha-hydroxylase is expressed in Escherichia coli BL21-lambdaDE3 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of kshA2 is induced in parent strain Rhodococcus erythropolis SQ1 in the presence of androsta-1,4-diene-3,17-dione or 9alpha-hydroxy-4-androstene-3,17-dione or a metabolite thereof
in wild type Rhodococcus rhodochrous strain DSM43269, ksh1 is specifically induced by cholic acid; in wild type Rhodococcus rhodochrous strain DSM43269, kshA2 is specifically induced by 4-androstene-3,17-dione, progesterone, and cholic acid; in wild type Rhodococcus rhodochrous strain DSM43269, kshA3 is specifically induced by 4-androstene-3,17-dione; in wild type Rhodococcus rhodochrous strain DSM43269, kshA4 is specifically induced by 4-androstene-3,17-dione, cholic acid, and cholesterol; in wild type Rhodococcus rhodochrous strain DSM43269, kshA5 is specifically induced by 4-androstene-3,17-dione, progesterone, cholic acid, and cholesterol
expression of kshA2 is induced in parent strain Rhodococcus erythropolis SQ1 in the presence of androsta-1,4-diene-3,17-dione or 9alpha-hydroxy-4-androstene-3,17-dione or a metabolite thereof
expression of kshA2 is induced in parent strain Rhodococcus erythropolis SQ1 in the presence of androsta-1,4-diene-3,17-dione or 9alpha-hydroxy-4-androstene-3,17-dione or a metabolite thereof
-
-
in wild type Rhodococcus rhodochrous strain DSM43269, ksh1 is specifically induced by cholic acid; in wild type Rhodococcus rhodochrous strain DSM43269, kshA2 is specifically induced by 4-androstene-3,17-dione, progesterone, and cholic acid; in wild type Rhodococcus rhodochrous strain DSM43269, kshA3 is specifically induced by 4-androstene-3,17-dione; in wild type Rhodococcus rhodochrous strain DSM43269, kshA4 is specifically induced by 4-androstene-3,17-dione, cholic acid, and cholesterol; in wild type Rhodococcus rhodochrous strain DSM43269, kshA5 is specifically induced by 4-androstene-3,17-dione, progesterone, cholic acid, and cholesterol
in wild type Rhodococcus rhodochrous strain DSM43269, ksh1 is specifically induced by cholic acid; in wild type Rhodococcus rhodochrous strain DSM43269, kshA2 is specifically induced by 4-androstene-3,17-dione, progesterone, and cholic acid; in wild type Rhodococcus rhodochrous strain DSM43269, kshA3 is specifically induced by 4-androstene-3,17-dione; in wild type Rhodococcus rhodochrous strain DSM43269, kshA4 is specifically induced by 4-androstene-3,17-dione, cholic acid, and cholesterol; in wild type Rhodococcus rhodochrous strain DSM43269, kshA5 is specifically induced by 4-androstene-3,17-dione, progesterone, cholic acid, and cholesterol
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-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D230E/S232T/F238Y
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutant of isoform KshA1 shows no 3-ketosteroid 9alpha-hydroxylase activity
D242W
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutant of isoform KshA1 exhibits 3-ketosteroid 9alpha-hydroxylase activity
E236D/T238S/Y244F
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutant of isoform KshA5 shows no 3-ketosteroid 9alpha-hydroxylase activity
Q209T/A210G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutant of isoform KshA1 exhibits 3-ketosteroid 9alpha-hydroxylase activity
T207V/T209S/Y211F/H213R/S214G/T215Q/G216A
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutant of isoform KshA5 exhibits 3-ketosteroid 9alpha-hydroxylase activity
V201T/S203T/F205Y/R207H/G208S/Q209T/A210G
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutant of isoform KshA1 exhibits 3-ketosteroid 9alpha-hydroxylase activity
W248D
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutant of isoform KshA5 exhibits 3-ketosteroid 9alpha-hydroxylase activity
D230E/S232T/F238Y
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
-
Q209T/A210G
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; the mutant of isoform KshA1 exhibits 3-ketosteroid 9alpha-hydroxylase activity
-
V201T/S203T/F205Y/R207H/G208S/Q209T/A210G
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme; site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
-
additional information
additional information
the insertion mutant 10A12 is blocked in 3-ketosteroid 9alpha-hydroxylation
additional information
-
the insertion mutant 10A12 is blocked in 3-ketosteroid 9alpha-hydroxylation
-
additional information
unmarked in frame gene deletion mutant of parent strain Rhodococcus erythropolis strain SQ1, designated strain RG2 (kshA mutant), is unable to grow on steroid substrates androsta-1,4-diene-3,17-dione and 4-androstene-3,17-dione, whereas growth on 9alpha-hydroxy-4-androstene-3,17-dione is not affected; unmarked in frame gene deletion mutant of parent strain Rhodococcus erythropolis strain SQ1, designated strain RG4 (kshB mutant), is unable to grow on steroid substrates androsta-1,4-diene-3,17-dione and 4-androstene-3,17-dione, whereas growth on 9alpha-hydroxy-4-androstene-3,17-dione is not affected. Strain RG4 is also impaired in sterol degradation
additional information
unmarked in frame gene deletion mutant of parent strain Rhodococcus erythropolis strain SQ1, designated strain RG2 (kshA mutant), is unable to grow on steroid substrates androsta-1,4-diene-3,17-dione and 4-androstene-3,17-dione, whereas growth on 9alpha-hydroxy-4-androstene-3,17-dione is not affected; unmarked in frame gene deletion mutant of parent strain Rhodococcus erythropolis strain SQ1, designated strain RG4 (kshB mutant), is unable to grow on steroid substrates androsta-1,4-diene-3,17-dione and 4-androstene-3,17-dione, whereas growth on 9alpha-hydroxy-4-androstene-3,17-dione is not affected. Strain RG4 is also impaired in sterol degradation
additional information
-
unmarked in frame gene deletion mutant of parent strain Rhodococcus erythropolis strain SQ1, designated strain RG2 (kshA mutant), is unable to grow on steroid substrates androsta-1,4-diene-3,17-dione and 4-androstene-3,17-dione, whereas growth on 9alpha-hydroxy-4-androstene-3,17-dione is not affected; unmarked in frame gene deletion mutant of parent strain Rhodococcus erythropolis strain SQ1, designated strain RG4 (kshB mutant), is unable to grow on steroid substrates androsta-1,4-diene-3,17-dione and 4-androstene-3,17-dione, whereas growth on 9alpha-hydroxy-4-androstene-3,17-dione is not affected. Strain RG4 is also impaired in sterol degradation
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additional information
a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol is severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked
additional information
a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol is severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked
additional information
a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol is severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked
additional information
a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol is severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked
additional information
a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol is severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked
additional information
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a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol is severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked
additional information
construction of chimeric KshA enzyme mutants with exchanged helix-grip fold beta-sheets that retain KSH activity. kshA1 E198 to V255 is exchanged for kshA5 E204 to I261. kshA1 I257 to I306 is exchanged for kshA5 I263 to V312, kshA5 E204 to I261 is exchanged for kshA1 E198 to V255, kshA5 I263 to V312 is exchanged for kshA1 I257 to I306, kshA1 209-QAREDTRPHANGQPKMIGS-227is exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and kshA5 215-TGREDVISGTNYDDPNAEL-233 is exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227; construction of chimeric KshA enzyme mutants with exchanged helix-grip fold beta-sheets that retain KSH activity. kshA1 E198 to V255 is exchanged for kshA5 E204 to I261. kshA1 I257 to I306 is exchanged for kshA5 I263 to V312, kshA5 E204 to I261 is exchanged for kshA1 E198 to V255, kshA5 I263 to V312 is exchanged for kshA1 I257 to I306, kshA1 209-QAREDTRPHANGQPKMIGS-227is exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and kshA5 215-TGREDVISGTNYDDPNAEL-233 is exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227; mutant KshA1A5beta is isoform KshA1 with beta sheet of KshA5 and the mutations kshA1 E198 to V255 exchanged for kshA5 E204 to I261, and exhibits 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA1A5alpha is isoform KshA1 with alpha helix of KshA5 and mutations kshA1 I257 to I306 exchanged for kshA5 I263 to V312, and shows not enzymatic activity. Mutant KshA1A5loop is isoform KshA1 with loop region of KshA5 and mutation kshA1 209-QAREDTRPHANGQPKMIGS-227 exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and exhibits 3-ketosteroid 9alpha-hydroxylase activity; mutant KshA5A1beta is isoform KshA5 with beta sheet of KshA1 and mutation kshA5 E204 to I261 exchanged for kshA1 E198 to V255, and exhibits 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA5A1alpha is isoform KshA5 with alpha helix of KshA1 and mutation kshA5 I263 to V312 exchanged for kshA1 I257 to I306, and shows initial 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA5A1loop is isoform KshA5 with loop region of KshA1 and mutation kshA5 215-TGREDVISGTNYDDPNAEL-233 exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227, and exhibits 3-ketosteroid 9alpha-hydroxylase activity
additional information
construction of chimeric KshA enzyme mutants with exchanged helix-grip fold beta-sheets that retain KSH activity. kshA1 E198 to V255 is exchanged for kshA5 E204 to I261. kshA1 I257 to I306 is exchanged for kshA5 I263 to V312, kshA5 E204 to I261 is exchanged for kshA1 E198 to V255, kshA5 I263 to V312 is exchanged for kshA1 I257 to I306, kshA1 209-QAREDTRPHANGQPKMIGS-227is exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and kshA5 215-TGREDVISGTNYDDPNAEL-233 is exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227; construction of chimeric KshA enzyme mutants with exchanged helix-grip fold beta-sheets that retain KSH activity. kshA1 E198 to V255 is exchanged for kshA5 E204 to I261. kshA1 I257 to I306 is exchanged for kshA5 I263 to V312, kshA5 E204 to I261 is exchanged for kshA1 E198 to V255, kshA5 I263 to V312 is exchanged for kshA1 I257 to I306, kshA1 209-QAREDTRPHANGQPKMIGS-227is exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and kshA5 215-TGREDVISGTNYDDPNAEL-233 is exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227; mutant KshA1A5beta is isoform KshA1 with beta sheet of KshA5 and the mutations kshA1 E198 to V255 exchanged for kshA5 E204 to I261, and exhibits 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA1A5alpha is isoform KshA1 with alpha helix of KshA5 and mutations kshA1 I257 to I306 exchanged for kshA5 I263 to V312, and shows not enzymatic activity. Mutant KshA1A5loop is isoform KshA1 with loop region of KshA5 and mutation kshA1 209-QAREDTRPHANGQPKMIGS-227 exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and exhibits 3-ketosteroid 9alpha-hydroxylase activity; mutant KshA5A1beta is isoform KshA5 with beta sheet of KshA1 and mutation kshA5 E204 to I261 exchanged for kshA1 E198 to V255, and exhibits 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA5A1alpha is isoform KshA5 with alpha helix of KshA1 and mutation kshA5 I263 to V312 exchanged for kshA1 I257 to I306, and shows initial 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA5A1loop is isoform KshA5 with loop region of KshA1 and mutation kshA5 215-TGREDVISGTNYDDPNAEL-233 exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227, and exhibits 3-ketosteroid 9alpha-hydroxylase activity
additional information
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a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol is severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; a 5fold kshA null mutant of strain DSM43269 (strain RG32) lacks genes kshA1, kshA2, kshA3, kshA4, and kshA5. Contrary to wild type DSM43269, the kshA null mutant strain RG32 shows no growth on progesterone, 4-androstene-3,17-dione, or cholic acid. Growth of strain RG32 on cholesterol was severely impaired, but not completely blocked; construction of chimeric KshA enzyme mutants with exchanged helix-grip fold beta-sheets that retain KSH activity. kshA1 E198 to V255 is exchanged for kshA5 E204 to I261. kshA1 I257 to I306 is exchanged for kshA5 I263 to V312, kshA5 E204 to I261 is exchanged for kshA1 E198 to V255, kshA5 I263 to V312 is exchanged for kshA1 I257 to I306, kshA1 209-QAREDTRPHANGQPKMIGS-227is exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and kshA5 215-TGREDVISGTNYDDPNAEL-233 is exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227; construction of chimeric KshA enzyme mutants with exchanged helix-grip fold beta-sheets that retain KSH activity. kshA1 E198 to V255 is exchanged for kshA5 E204 to I261. kshA1 I257 to I306 is exchanged for kshA5 I263 to V312, kshA5 E204 to I261 is exchanged for kshA1 E198 to V255, kshA5 I263 to V312 is exchanged for kshA1 I257 to I306, kshA1 209-QAREDTRPHANGQPKMIGS-227is exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and kshA5 215-TGREDVISGTNYDDPNAEL-233 is exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227; mutant KshA1A5beta is isoform KshA1 with beta sheet of KshA5 and the mutations kshA1 E198 to V255 exchanged for kshA5 E204 to I261, and exhibits 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA1A5alpha is isoform KshA1 with alpha helix of KshA5 and mutations kshA1 I257 to I306 exchanged for kshA5 I263 to V312, and shows not enzymatic activity. Mutant KshA1A5loop is isoform KshA1 with loop region of KshA5 and mutation kshA1 209-QAREDTRPHANGQPKMIGS-227 exchanged for kshA5 215-TGREDVISGTNYDDPNAEL-233, and exhibits 3-ketosteroid 9alpha-hydroxylase activity; mutant KshA5A1beta is isoform KshA5 with beta sheet of KshA1 and mutation kshA5 E204 to I261 exchanged for kshA1 E198 to V255, and exhibits 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA5A1alpha is isoform KshA5 with alpha helix of KshA1 and mutation kshA5 I263 to V312 exchanged for kshA1 I257 to I306, and shows initial 3-ketosteroid 9alpha-hydroxylase activity. Mutant KshA5A1loop is isoform KshA5 with loop region of KshA1 and mutation kshA5 215-TGREDVISGTNYDDPNAEL-233 exchanged for kshA1 209-QAREDTRPHANGQPKMIGS-227, and exhibits 3-ketosteroid 9alpha-hydroxylase activity
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