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Information on EC 1.14.15.30 - 3-ketosteroid 9alpha-monooxygenase and Organism(s) Rhodococcus rhodochrous and UniProt Accession F1CMX8
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1.14.15.30 3-ketosteroid 9alpha-monooxygenaseIUBMB Comments
The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It forms a two-component system with a ferredoxin reductase (KshB). The enzyme contains a Rieske-type iron-sulfur center and non-heme iron. 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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Word Map
- 1.14.15.30
- 3-ketosteroids
- cholesterol
-
rieske
- rhodochrous
- tuberculosis
- 4-androstene-3,17-dione
-
two-component
- oxygenases
-
cholic
- sterols
- erythropolis
- bile
-
mouth
- ruber
- coa
- smegmatis
- medicine
- drug development
The taxonomic range for the selected organisms is: Rhodococcus rhodochrous
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
+
2
+
2
+
=
+
2
+
+
2
reduced ferredoxin [iron-sulfur] cluster
+
2
+
=
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
Synonyms
ksha1, ksha2, kshab, ksha5, ksha3, 3-ketosteroid-9alpha-hydroxylase, 3-ketosteroid 9-alpha-hydroxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketosteroid 9alpha-hydroxylase
KSH
KshA
terminal oxygenase component of 3-ketosteroid 9alpha-hydroxylase
KshA1
KshA5
KshAB
KshB
reductase component of 3-ketosteroid 9alpha-hydroxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
KSH enzymes employ an electron transport chain that starts with the oxidation of NADH. The electrons are transferred to the flavin cofactor (FAD) of the ferredoxin reductase component KshB and then transported to the plant type iron-sulfur cluster of KshB. The Rieske iron-sulfur cluster of the KshA oxygenase component subsequently accepts the electrons from KshB. The electrons end up at the nonheme iron situated in the active site of KshA. The mononuclear iron is the site where O2 is bound and activated and the substrate is hydroxylated
-
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
KshAB-catalyzed 9alpha-hydroxylation of 3-ketosteroids. 1,4-Diene ketosteroids undergo subsequent nonenzymatic cleavage of ring B and aromatization of ring A
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
androsta-1,4-diene-3,17-dione,[reduced ferredoxin]:oxygen oxidoreductase (9alpha-hydroxylating)
The enzyme is involved in the cholesterol degradation pathway of several bacterial pathogens, such as Mycobacterium tuberculosis. It forms a two-component system with a ferredoxin reductase (KshB). The enzyme contains a Rieske-type iron-sulfur center and non-heme iron. The product of the enzyme is unstable, and spontaneously converts to 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione.
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-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA3 shows 28% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA3 shows 10% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA3 shows 124% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA3 shows 176% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA3 shows 94% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA3 shows 100% activity
-
-
?
4-cholestene-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA3 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA3 shows 112% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA3 shows 194% activity compared to 4-androstene-3,17-dione
-
-
?
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
? + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
1,4-androstadiene-3,17-dione + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
11beta-hydrocortisone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-11beta-hydrocortisone + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
19-nor-4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
3-oxo-23,24-bisnorchol-4-en-22-oate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorchol-4-en-22-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
3-oxo-23,24-bisnorchol-4-en-22-oate + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
3-oxo-23,24-bisnorchola-1,4-dien-22-oate-CoA + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
3-oxo-23,24-bisnorchola-1,4-diene-22-oate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorchola-1,4-diene-22-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
low activity
-
-
?
3-oxo-23,24-bisnorchola-1,4-diene-22-oate + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
3-oxo-23,24-bisnorchola-1,4-diene-22-oyl-CoA + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorchola-1,4-diene-22-oyl-CoA + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
3-oxo-23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
3-oxosteroid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxysteroid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-androstene-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
4-androstene-3,17-dione + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-cholestene-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
4-estren-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-estren-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-estren-3,17-dione + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-estren-3,17-dione + oxidized ferredoxin [iron-sulfur] cluster + H2O
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
5alpha-androstan-3,17-dione + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
5alpha-androstane-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-5alpha-androstane-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
5alpha-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
5beta-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5beta-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
testosterone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
testosterone + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
(17beta)-9,17-dihydroxyandrost-4-en-3-one + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
testosterone + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
? + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA1 shows 244% activity compared to 4-androstene-3,17-dione
-
-
?
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
? + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA5 shows 51% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
1-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 68% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA1 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
1-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androst-1-en-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA5 shows 99% activity compared to 4-androstene-3,17-dione
-
-
?
11beta-hydrocortisone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-11beta-hydrocortisone + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
11beta-hydrocortisone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-11beta-hydrocortisone + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
i.e. stanolon, isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
11beta-hydrocortisone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-11beta-hydrocortisone + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
19-nor-4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + 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 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + 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 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 24% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 78% activity compared to 4-androstene-3,17-dione
-
-
?
19-nor-4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-19-nor-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 107% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 500% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 23% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 80% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA1 shows 548% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA5 shows 88% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 423% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 22% activity compared to 4-androstene-3,17-dione
-
-
?
23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-23,24-bisnorcholesta-1,4-dien-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 43% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-androstene-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + 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 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + 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 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 127% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 101% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-4-androstene-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 113% activity compared to 4-androstene-3,17-dione
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA1 shows 100% activity
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA5 shows 100% activity
-
-
?
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 KshA4 shows 100% activity
-
-
?
4-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
isozyme KshA5 shows 100% activity
-
-
?
4-cholestene-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 13% activity compared to 4-androstene-3,17-dione
-
-
?
4-cholestene-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxycholest-4-en-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 26% activity compared to 4-androstene-3,17-dione
-
-
?
4-estren-3,17-dione + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-estren-3,17-dione + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-estren-3,17-dione + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-estren-3,17-dione + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
-
?
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
i.e. progesterone, the wild type homologue KshA1 shows 372% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
i.e. progesterone, the wild type homologue KshA5 shows 65% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 423% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 99% activity compared to 4-androstene-3,17-dione
-
-
?
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 67% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-5alpha-androstane-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
5alpha-androstane-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-5alpha-androstane-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
i.e. stanolon, isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha,17beta-dihydroxy-5alpha-androstane-3-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
i.e. stanolon, the wild type homologue KshA5 shows 100% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
5alpha-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 9% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 64% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 80% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA1 shows 12% activity compared to 4-androstene-3,17-dione
-
-
?
5alpha-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5alpha-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA5 shows 73% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5beta-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
5beta-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5beta-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 19% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5beta-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 58% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5beta-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 93% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5beta-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA1 shows 19% activity compared to 4-androstene-3,17-dione
-
-
?
5beta-androstane-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-5beta-androstane-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
the wild type homologue KshA5 shows 99% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA1 shows 288% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA4 shows 89% activity compared to 4-androstene-3,17-dione
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
isozyme KshA5 shows 49% activity compared to 4-androstene-3,17-dione
-
-
?
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
?
-
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
?
-
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 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 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 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
?
-
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
?
-
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
?
-
enzyme KshA1 has the highest apparent catalytic efficiency (kcat/Km) for steroids with an isopropyl side chain at C17, such as 3-oxo-23,24-bisnorcholesta-1,4-diene-22-oate, substrate specificity comparisons of KSH enzymes, overview
-
-
?
additional information
?
-
enzyme KshA1 has the highest apparent catalytic efficiency (kcat/Km) for steroids with an isopropyl side chain at C17, such as 3-oxo-23,24-bisnorcholesta-1,4-diene-22-oate, substrate specificity comparisons of KSH enzymes, overview
-
-
?
additional information
?
-
enzyme KshA5 has the highest apparent catalytic efficiency for substrates with no C17 side chain, e.g. 4-estrendione, 5alpha-androstandione, and testosterone, substrate specificity comparisons of KSH enzymes, overview
-
-
?
additional information
?
-
enzyme KshA5 has the highest apparent catalytic efficiency for substrates with no C17 side chain, e.g. 4-estrendione, 5alpha-androstandione, and testosterone, substrate specificity comparisons of KSH enzymes, overview
-
-
?
additional information
?
-
-
KSH of Rhodococcus rhodochrous can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids
-
-
?
NATURAL SUBSTRATE
NATURAL 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 + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S]-center
-
a Rieske iron-sulfur cluster of the KshA oxygenase component and a plant type iron-sulfur cluster of KshB. The oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The Rieske iron-sulfur cluster and the non-heme Fe2+ catalytic centre are located relatively far away from each other, but the typical head-to-tail trimer arrangement positions the Rieske Fe2-S2 in close proximity to the non-heme Fe2+ of the neighbouring KshA subunit, enabling transport of electrons between KshA subunits
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
-
the oxygenase component, which performs the substrate hydroxylation, is an iron-sulfur protein and contains a non-heme iron situated at the active site. The iron is bidentate bound to the carboxyl group of the aspartate leaving two sites available for exogenous ligands. This metal centre is more labile compared to the covalently bound heme-iron. Non-heme iron is a highly catalytic platform able to bind O2 and steroid substrate simultaneously in different orientations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-oxo-23,24-bisnorchol-4-en-22-oate
substrate inhibition
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
strong substrate inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
1,4-androstadiene-3,17-dione
isoform KshA1, at pH 7.0 and 22°C
0.0061
5alpha-androstan-3,17-dione
isoform KshA5, at pH 7.0 and 22°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
0.01
23,24-bisnorcholesta-4-ene-22-oic acid
Km less than 0.01 mM, isoform KshA5, in 50 mM Tris-HCl buffer (pH 7.0), temperature not specified in the publication
0.0012
3-oxo-23,24-bisnorchol-4-en-22-oate
pH 7.0, 22°C
0.0012
3-oxo-23,24-bisnorchol-4-en-22-oate
isoform KshA5, at pH 7.0 and 22°C
0.0022
3-oxo-23,24-bisnorchol-4-en-22-oate
pH 7.0, 22°C
0.0022
3-oxo-23,24-bisnorchol-4-en-22-oate
isoform KshA1, at pH 7.0 and 22°C
0.002
3-oxo-23,24-bisnorchola-1,4-dien-22-oate-CoA
isoform KshA1, at pH 7.0 and 22°C
0.5
3-oxo-23,24-bisnorchola-1,4-dien-22-oate-CoA
isoform KshA1, at pH 7.0 and 22°C
0.0005
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
pH 7.0, 22°C
0.0005
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
isoform KshA5, at pH 7.0 and 22°C
0.001
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
pH 7.0, 22°C
0.001
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
isoform KshA1, at pH 7.0 and 22°C
0.002
3-oxo-23,24-bisnorchola-1,4-diene-22-oyl-CoA
pH 7.0, 22°C
0.5
3-oxo-23,24-bisnorchola-1,4-diene-22-oyl-CoA
pH 7.0, 22°C
0.0008
4-Estren-3,17-dione
isoform KshA5, at pH 7.0 and 22°C
0.4
4-Estren-3,17-dione
isoform KshA1, at pH 7.0 and 22°C
additional information
additional information
steady-state kinetic analysis
-
additional information
additional information
steady-state kinetic analysis
-
additional information
additional information
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
-
additional information
additional information
kinetic analysis of the activity of KshA mutants with 4-23,24-bisnorcholesta-4-ene-22-oic acid
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.8
5alpha-androstan-3,17-dione
isoform KshA5, at pH 7.0 and 22°C
0.7
1,4-androstadiene-3,17-dione
isoform KshA5, at pH 7.0 and 22°C
1.3
1,4-androstadiene-3,17-dione
isoform KshA1, at pH 7.0 and 22°C
0.6
3-oxo-23,24-bisnorchol-4-en-22-oate
isoform KshA5, at pH 7.0 and 22°C
2.6
3-oxo-23,24-bisnorchol-4-en-22-oate
isoform KshA1, at pH 7.0 and 22°C
1.1
3-oxo-23,24-bisnorchola-1,4-dien-22-oate-CoA
isoform KshA1, at pH 7.0 and 22°C
1.7
3-oxo-23,24-bisnorchola-1,4-dien-22-oate-CoA
isoform KshA1, at pH 7.0 and 22°C
0.5
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
pH 7.0, 22°C
0.5
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
isoform KshA5, at pH 7.0 and 22°C
0.9
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
pH 7.0, 22°C
0.9
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
isoform KshA1, at pH 7.0 and 22°C
1.1
3-oxo-23,24-bisnorchola-1,4-diene-22-oyl-CoA
pH 7.0, 22°C
1.7
3-oxo-23,24-bisnorchola-1,4-diene-22-oyl-CoA
pH 7.0, 22°C
0.5
4-Estren-3,17-dione
isoform KshA1, at pH 7.0 and 22°C
0.8
4-Estren-3,17-dione
isoform KshA5, at pH 7.0 and 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
27
1,4-androstadiene-3,17-dione
isoform KshA1, at pH 7.0 and 22°C
140
5alpha-androstan-3,17-dione
isoform KshA5, at pH 7.0 and 22°C
500
3-oxo-23,24-bisnorchol-4-en-22-oate
isoform KshA5, at pH 7.0 and 22°C
1200
3-oxo-23,24-bisnorchol-4-en-22-oate
isoform KshA1, at pH 7.0 and 22°C
3.7
3-oxo-23,24-bisnorchola-1,4-dien-22-oate-CoA
isoform KshA1, at pH 7.0 and 22°C
600
3-oxo-23,24-bisnorchola-1,4-dien-22-oate-CoA
isoform KshA1, at pH 7.0 and 22°C
900
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
pH 7.0, 22°C
900
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
isoform KshA1, at pH 7.0 and 22°C
1000
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
pH 7.0, 22°C
1000
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
isoform KshA5, at pH 7.0 and 22°C
3.7
3-oxo-23,24-bisnorchola-1,4-diene-22-oyl-CoA
pH 7.0, 22°C
600
3-oxo-23,24-bisnorchola-1,4-diene-22-oyl-CoA
pH 7.0, 22°C
1.2
4-Estren-3,17-dione
isoform KshA1, at pH 7.0 and 22°C
1000
4-Estren-3,17-dione
isoform KshA5, at pH 7.0 and 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
3-oxo-23,24-bisnorchola-1,4-diene-22-oate
pH 7.0, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
additional information
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
additional information
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
additional information
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism
evolution
-
KSH is classified as a group I RO in this classification system. Group I contains a broad range of mono- and dioxygenases with low amino acid sequence similarity and various protein sizes. The oxygenases are alpha-monomers. KshA contains a Rieske domain, coordinating the Rieske Fe2-S2 cluster, and a catalytic domain with the typical helix-Grip fold, which is part of the StAR (steroidogenic acute regulatory protein) related lipid transfer (START) domain superfamily. The catalytic domain is composed of a beta-sheet flanked by alpha-helices
malfunction
-
deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione
metabolism
3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism
physiological function
additional information
physiological function
3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid catabolism
physiological function
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
physiological function
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
KshA is the oxygenase component of 3-ketosteroid 9alpha-hydroxylase, a Rieske oxygenase involved in the bacterial degradation of steroids
physiological function
KshA is the oxygenase component of 3-ketosteroid 9alpha-hydroxylase, a Rieske oxygenase involved in the bacterial degradation of steroids. KshA1 has a role in bile acid catabolism
physiological function
-
the 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation. KSH initiates opening of the steroid polycyclic ring structure
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
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
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
additional information
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 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 KshA5, overview. The variable loop within the beta-sheet plays a role in the substrate preference of KshA enzymes
additional information
KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme
additional information
KshA and KshB together constitute the KSH enzyme
additional information
-
KshA and KshB together constitute the KSH enzyme
additional information
-
structure-function relationship of KSH enzymes and components, overview
additional information
the enzyme has a steroid-binding pocket with the substrate's C17 oriented toward the active site opening. Comparisons suggest that Tyr245 and Phe297 are determinants of KshA1 specificity. The enzyme has a flexible 16-residue mouth loop, which in some structures completely occlude the substrate-binding pocket from the bulk solvent
additional information
the enzyme has a steroid-binding pocket with the substrate's C17 oriented toward the active site opening. Comparisons suggest that Tyr245 and Phe297 are determinants of KshA1 specificity. The enzyme has a flexible 16-residue mouth loop, which in some structures completely occlude the substrate-binding pocket from the bulk solvent
additional information
the enzyme has a steroid-binding pocket with the substrate's C17 oriented toward the active site opening. The enzyme has a flexible 16-residue mouth loop, which in some structures completely occlude the substrate-binding pocket from the bulk solvent. The catalytic iron andalpha-helices harboring its ligands are displaced up to 4.4 A in theKshA5substrate complexes as compared with substrate-free KshA, suggesting that Rieske oxygenases may have a dynamic nature similar to cytochrome P450
additional information
the enzyme has a steroid-binding pocket with the substrate's C17 oriented toward the active site opening. The enzyme has a flexible 16-residue mouth loop, which in some structures completely occlude the substrate-binding pocket from the bulk solvent. The catalytic iron andalpha-helices harboring its ligands are displaced up to 4.4 A in theKshA5substrate complexes as compared with substrate-free KshA, suggesting that Rieske oxygenases may have a dynamic nature similar to cytochrome P450
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
KshAB is a two-component Rieske oxygenase comprising an oxygenase (KshA) and a reductase (KshB), structures comparisons of different KSH enzymes
additional information
KshAB is a two-component Rieske oxygenase comprising an oxygenase (KshA) and a reductase (KshB), structures comparisons of different KSH enzymes
additional information
KshAB is a two-component Rieske oxygenase comprising an oxygenase (KshA) and a reductase (KshB), structures comparisons of different KSH enzymes. The substrate binding residues within the active site pocket are positioned nearly identically in enzyme KshA1 from Rhodococcus rhodochrous and KshA from Mycobacterium tuberculosis
additional information
KshAB is a two-component Rieske oxygenase comprising an oxygenase (KshA) and a reductase (KshB), structures comparisons of different KSH enzymes. The substrate binding residues within the active site pocket are positioned nearly identically in enzyme KshA1 from Rhodococcus rhodochrous and KshA from Mycobacterium tuberculosis
additional information
-
typical head-to-tail trimer arrangement of KshA enzymes, structure overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with 1,4-androstadiene-3,17-dione or 3-oxo-23,24-bisnorchola-1,4-dien-22-oate-CoA, hanging drop vapor diffusion method, using 500 mM NaH2PO4, 125 mM K2HPO4, 4% (w/v) PEG-1000 or 2% (w/v) PEG-3000, 20 mM Tris, 100 mM phosphate-citrate, pH 4.2
purified recombinant enzyme in complex with substrates androsta-1,4-diene-3,17-dione and 3-oxo-23,24-bisnorcholesta-1,4-diene-22-oate and enzyme KshA5. Attempts to crystallize KshA1 alone are unsuccessful, crystals are serendipitously obtained from a mixture of KshA1, KshA5, and 1,4-BNC-CoA. Pyramid-shaped light brown crystals grow over 2 weeks from a 0.0015 ml drop containing equal volumes of KshA1 with 1,4-BNC-CoA, KshA5, and well solution containing 500 mM NaH2PO4, 125 mM K2HPO4, 4% PEG 1000, 20 mM Tris, 100 mM phosphate-citrate, pH 4.2, X-ray diffraction structure determination and analysis at 2.45-2.52 A resolution
purified recombinant enzyme in complex with substrates androsta-1,4-diene-3,17-dione and 3-oxo-23,24-bisnorcholesta-1,4-diene-22-oate, KshA5 is crystallized in complex with 1,4-BNC-CoA using 0.8 M NaH2PO4, 0.2 M K2HPO4, 0.25 M (NH4)2SO4, 20 mM CHES, 40 mM NaCl, and 0.1 M phosphate-citrate, pH 4.2, and crystallized in complex with ADD using 0.8 M NaH2PO4, 0.2 M K2HPO4, 2% PEG 3000, 20 mM CHES, 0.1 M phosphate-citrate, pH 4.2, X-ray diffraction structure determination and analysis at 1.92 A and 2.6 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D230E/S232T/F238Y
D242W
E236D/T238S/Y244F
Q209T/A210G
T207V/T209S/Y211F/H213R/S214G/T215Q/G216A
V201T/S203T/F205Y/R207H/G208S/Q209T/A210G
W248D
additional information
D230E/S232T/F238Y
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
D230E/S232T/F238Y
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
D242W
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
E236D/T238S/Y244F
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
Q209T/A210G
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
T207V/T209S/Y211F/H213R/S214G/T215Q/G216A
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
V201T/S203T/F205Y/R207H/G208S/Q209T/A210G
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
W248D
the mutant of isoform KshA5 exhibits 3-ketosteroid 9alpha-hydroxylase activity
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 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 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 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 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 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 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 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
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
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
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
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
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
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
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 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 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 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 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 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 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 was severely impaired, but not completely blocked
additional information
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
additional information
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
additional information
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
additional information
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
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
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
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
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
additional information
-
a kshA null mutant is constructed by gene deletion mutagenesis (strain RG32) to fully block opening of the steroids polycyclic ring structure of cholesterol and beta-sitosterol resulting in accumulation of 1,4-androstadiene-3,17-dione and 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurification of recombinant His-tagged KshA mutants with His-tagged KshB
Ni-Sepharose column chromatography and Source 15Q column chromatography
recombinant KshA from Escherichia coli strains Bl21(DE3) and C41(DE3)
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
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
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)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in wild type Rhodococcus rhodochrous strain DSM43269, kshA3 is specifically induced by 4-androstene-3,17-dione
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, kshA4 is specifically induced by 4-androstene-3,17-dione, cholic acid, and cholesterol
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Petrusma, M.; Hessels, G.; Dijkhuizen, L.; van der Geize, R.
Multiplicity of 3-ketosteroid-9alpha-hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids
J. Bacteriol.
193
3931-3940
2011
Rhodococcus rhodochrous (B6V6V5), Rhodococcus rhodochrous (F1CMX0), Rhodococcus rhodochrous (F1CMX3), Rhodococcus rhodochrous (F1CMX6), Rhodococcus rhodochrous (F1CMX8), Rhodococcus rhodochrous (F1CMY8), Rhodococcus rhodochrous, Rhodococcus rhodochrous DSM 43269 (B6V6V5), Rhodococcus rhodochrous DSM 43269 (F1CMX0), Rhodococcus rhodochrous DSM 43269 (F1CMX3), Rhodococcus rhodochrous DSM 43269 (F1CMX6), Rhodococcus rhodochrous DSM 43269 (F1CMX8), Rhodococcus rhodochrous DSM 43269 (F1CMY8), Rhodococcus rhodochrous DSM 43269
Petrusma, M.; Dijkhuizen, L.; van Der Geize, R.
Structural features in the KshA terminal oxygenase protein that determine substrate preference of 3-ketosteroid 9alpha-hydroxylase enzymes
J. Bacteriol.
194
115-121
2012
Rhodococcus rhodochrous (F1CMX0), Rhodococcus rhodochrous (F1CMX3), Rhodococcus rhodochrous (F1CMY8), Rhodococcus rhodochrous DSM 43269 (F1CMX0), Rhodococcus rhodochrous DSM 43269 (F1CMX3), Rhodococcus rhodochrous DSM 43269 (F1CMY8), Rhodococcus rhodochrous DSM 43269
Petrusma, M.; van der Geize, R.; Dijkhuizen, L.
3-Ketosteroid 9alpha-hydroxylase enzymes Rieske non-heme monooxygenases essential for bacterial steroid degradation
Antonie van Leeuwenhoek
106
157-172
2014
Mycobacterium tuberculosis (P71875), Mycobacterium tuberculosis H37Rv (P71875), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2 155, Rhodococcus erythropolis, Rhodococcus erythropolis SQ1, Rhodococcus jostii, Rhodococcus jostii (Q0RXD9), Rhodococcus jostii (Q0S812), Rhodococcus rhodochrous, Rhodococcus rhodochrous DSM 43269
Penfield, J.S.; Worrall, L.J.; Strynadka, N.C.; Eltis, L.D.
Substrate specificities and conformational flexibility of 3-ketosteroid 9alpha-hydroxylases
J. Biol. Chem.
289
25523-25536
2014
Mycobacterium tuberculosis (P71875), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P71875), Rhodococcus rhodochrous (F1CMX0), Rhodococcus rhodochrous (F1CMY8), Rhodococcus rhodochrous DSM 43269 (F1CMX0), Rhodococcus rhodochrous DSM 43269 (F1CMY8), Rhodococcus rhodochrous DSM 43269
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