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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 + 2 reduced ferredoxin [iron-sulfur] cluster + 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 + O2
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 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 + 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-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-oxo-23,24-bisnorcholest-4-en-22-oyl-CoA + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholest-4-en-22-oyl-CoA + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate-CoA + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
r
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-CoA + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-CoA + 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 + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-androsten-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + 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-androstene-3,17-dione + O2 + NADH + H+
? + H2O + NAD+
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
cholestenone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
cholic acid + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
dehydroepiandrosterone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
dehydroepiandrosterone + NADH + H+ + O2
3beta,9alpha-dihydroxy-5-androstene-17-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
phytosterol + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
pregnenolone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
sodium acetate + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
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 + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
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
?
-
-
-
?
additional information
?
-
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
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
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
A0A0F7JI94; D2Y640
-
-
-
?
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
A0A0F7JI94; D2Y640
-
-
-
?
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
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
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
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
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
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
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
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
-
-
?
1,4-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
-
-
?
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 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 + 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 + 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 + O2
9alpha-hydroxy-1,4-androstadiene-3,17-dione + 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
-
-
-
?
1,4-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
-
-
-
?
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 KshA3 shows 28% 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
-
-
?
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 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
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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 KshA3 shows 10% 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
-
-
?
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 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
-
-
-
?
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
-
-
?
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 KshA3 shows 124% 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-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 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 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 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 KshA3 shows 176% 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
-
-
?
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 KshA3 shows 176% activity compared to 4-androstene-3,17-dione
-
-
?
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 + 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-bisnorchol-4-en-22-oate + reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
3-oxo-23,24-bisnorchola-1,4-dien-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-bisnorchola-1,4-dien-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-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-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-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-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-oxo-23,24-bisnorcholest-4-en-22-oyl-CoA + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholest-4-en-22-oyl-CoA + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
3-oxo-23,24-bisnorcholest-4-en-22-oyl-CoA + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholest-4-en-22-oyl-CoA + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-CoA + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-CoA + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-CoA + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
9alpha-hydroxy-3-oxo-23,24-bisnorcholesta-1,4-dien-22-oyl-CoA + 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
-
-
-
?
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-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 KshA3 shows 94% 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-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 + 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
A0A0F7JI94; D2Y640
-
-
-
?
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
A0A0F7JI94; D2Y640
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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 + 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
-
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-androsten-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-androsten-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
A0A0F7JI94; D2Y640
-
-
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
A0A0F7JI94; D2Y640
-
-
-
?
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 + 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 KshA3 shows 23% 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 KshA3 shows 112% 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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
ir
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
-
-
-
ir
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
-
-
-
?
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 KshA3 shows 194% 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
-
-
?
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
-
-
-
?
cholestenone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
cholestenone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
cholic acid + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
cholic acid + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
dehydroepiandrosterone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
dehydroepiandrosterone + 2 reduced ferredoxin [iron-sulfur] cluster + H+ + O2
?
-
-
-
?
dehydroepiandrosterone + NADH + H+ + O2
3beta,9alpha-dihydroxy-5-androstene-17-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
dehydroepiandrosterone + NADH + H+ + O2
3beta,9alpha-dihydroxy-5-androstene-17-one + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
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
?
-
cholesterol-degrading KshAMtb from Mycobacterium tuberculosis has the highest catalytic efficiency for CoA-thioesterified substrates, substrate specificity comparisons of KSH enzymes, overview
-
-
?
additional information
?
-
-
cholesterol-degrading KshAMtb from Mycobacterium tuberculosis has the highest catalytic efficiency for CoA-thioesterified substrates, substrate specificity comparisons of KSH enzymes, overview
-
-
?
additional information
?
-
KSH of Mycobacterium tuberculosis can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids
-
-
?
additional information
?
-
KSH of Mycobacterium tuberculosis can use 3-ketosteroids as substrates and shows high preference for the CoA thioester intermediate of cholesterol side chain degradation compared to the tested C17-ketosteroids
-
-
?
additional information
?
-
substrate specificity, overview. KshAB also transforms CoA thioester steroids
-
-
?
additional information
?
-
substrate specificity, overview. KshAB also transforms CoA thioester steroids
-
-
?
additional information
?
-
cholesterol-degrading KshAMtb from Mycobacterium tuberculosis has the highest catalytic efficiency for CoA-thioesterified substrates, substrate specificity comparisons of KSH enzymes, overview
-
-
?
additional information
?
-
A0A0F7JI94; D2Y640
Mycobacterium neoaurum strain JC-12 is a 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione producing strain
-
-
?
additional information
?
-
A0A0F7JI94; D2Y640
KshB, the reductase component of KSH, accepts electrons from NADH and transfers it to oxygenase component KshA, the cooperation of KshA and KshB is critically important for maintaining KSH activity
-
-
?
additional information
?
-
A0A0F7JI94; D2Y640
Mycobacterium neoaurum strain JC-12 is a 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione producing strain
-
-
?
additional information
?
-
A0A0F7JI94; D2Y640
KshB, the reductase component of KSH, accepts electrons from NADH and transfers it to oxygenase component KshA, the cooperation of KshA and KshB is critically important for maintaining KSH activity
-
-
?
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 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
-
-
?
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
-
-
?
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
?
-
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 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
?
-
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
?
-
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
?
-
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 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
?
-
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
?
-
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
?
-
-
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
?
-
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
?
-
-
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
?
-
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
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?
additional information
?
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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
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-
?
additional information
?
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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
?
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the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids
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?
additional information
?
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the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids
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-
?
additional information
?
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the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids
-
-
?
additional information
?
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-
the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids
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-
?
additional information
?
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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
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-
?
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
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-
?
additional information
?
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-
isozyme KshA2 is only able to act on substrates with a short side chain in Rhodococcus ruber
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-
?
additional information
?
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isozyme KshA2 is only able to act on substrates with a short side chain in Rhodococcus ruber
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?
additional information
?
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isozyme KshA2 is only able to act on substrates with a short side chain in Rhodococcus ruber
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?
additional information
?
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isozyme KshA2 is only able to act on substrates with a short side chain in Rhodococcus ruber
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?
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evolution
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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
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
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
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
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
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
-
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
-
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
-
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
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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
-
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
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
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
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
malfunction
-
deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione. A kshA disruption mutant of Mycobacterium smegmatis mc2 155 incubated with sitosterol accumulates 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione
malfunction
deletion of the gene encoding the reductase component KshB of 3-ketosteroid 9alpha-hydroxylase in Rhodococcus equi strain USA-18 disrupts sterol catabolism, leading to the accumulation of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid and 1,4-androstadiene-3,17-dione
malfunction
Rhodococcus ruber strains devoid of any KshAB activity (DELTAkshB or DELTAkshA1,2,3 strains) are able to grow in cholesterol although 10times slower than the wild-type strain. This growth is due to the degradation of the side chain, a process that has been described to occur at different steps of the pathway being independent of the polycyclic ring opening. In the strain the side chain degradation process does not depend on any KshAB activity
malfunction
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deletion of the gene encoding the reductase component KshB of 3-ketosteroid 9alpha-hydroxylase in Rhodococcus equi strain USA-18 disrupts sterol catabolism, leading to the accumulation of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid and 1,4-androstadiene-3,17-dione
-
malfunction
-
deletion of KSH activity in sterol degrading bacteria results in blockage of steroid ring opening and is used to produce valuable C19-steroids such as 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione. A kshA disruption mutant of Mycobacterium smegmatis mc2 155 incubated with sitosterol accumulates 4-androstene-3,17-dione and 1,4-androstadiene-3,17-dione
-
malfunction
-
Rhodococcus ruber strains devoid of any KshAB activity (DELTAkshB or DELTAkshA1,2,3 strains) are able to grow in cholesterol although 10times slower than the wild-type strain. This growth is due to the degradation of the side chain, a process that has been described to occur at different steps of the pathway being independent of the polycyclic ring opening. In the strain the side chain degradation process does not depend on any KshAB activity
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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
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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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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
-
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
-
malfunction
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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
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metabolism
3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism
metabolism
the enzyme is essential for the steroid metabolism
metabolism
A0A0F7JI94; D2Y640
3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid metabolism and can catalyze the transformation of 4-androstene-3,17-dione to 9alpha-hydroxy-4-androstene-3,17-dione
metabolism
isoform KshA1 is a more versatile enzyme related to the cholic acid catabolism, although it also collaborates with KshA2 or KshA3 activities in the catabolism of steroids
metabolism
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3-ketosteroid 9alpha-hydroxylase is a key enzyme in steroid metabolism and can catalyze the transformation of 4-androstene-3,17-dione to 9alpha-hydroxy-4-androstene-3,17-dione
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metabolism
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isoform KshA1 is a more versatile enzyme related to the cholic acid catabolism, although it also collaborates with KshA2 or KshA3 activities in the catabolism of steroids
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metabolism
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the enzyme is essential for the steroid metabolism
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metabolism
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3-ketosteroid-9alpha-hydroxylase is a key enzyme in steroid catabolism
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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
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 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
the enzyme plays a role of cholesterol catabolism, overview
physiological function
3-ketosteroid-9alpha-hydroxylase is a key enzyme in the general scheme of the bacterial steroid catabolism in combination with a 3-ketosteroid-DELTA1-dehydrogenase activity (KstD), being both responsible of the steroid nucleus (rings A/B) breakage. KshAB initiates the opening of the steroid ring by the 9alpha-hydroxylation of the C9 carbon of 4-ene-3-oxosteroids (e.g. AD) or 1,4-diene-3-oxosteroids (e.g. ADD), transforming them into 9alpha-hydroxy-4-androsten-3,17-dione or 9alpha-hydroxy-1,4-androstadiene-3,17-dione, respectively
physiological function
-
a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure
physiological function
a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure
physiological function
a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure
physiological function
a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key-enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure
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
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
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
physiological function
the enzyme is essential for the pathogenicity of Mycobacterium tuberculosis
physiological function
-
a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure
-
physiological function
-
3-ketosteroid-9alpha-hydroxylase is a key enzyme in the general scheme of the bacterial steroid catabolism in combination with a 3-ketosteroid-DELTA1-dehydrogenase activity (KstD), being both responsible of the steroid nucleus (rings A/B) breakage. KshAB initiates the opening of the steroid ring by the 9alpha-hydroxylation of the C9 carbon of 4-ene-3-oxosteroids (e.g. AD) or 1,4-diene-3-oxosteroids (e.g. ADD), transforming them into 9alpha-hydroxy-4-androsten-3,17-dione or 9alpha-hydroxy-1,4-androstadiene-3,17-dione, respectively
-
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
-
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
-
physiological function
-
3-ketosteroid 9alpha-hydroxylase is an essential factor in the pathogenesis of Mycobacterium tuberculosis
-
physiological function
-
a plant type iron-sulfur cluster of KshB. The 3-ketosteroid 9alpha-hydroxylase activity is a two component Rieske non-heme monooxygenase comprised of the oxygenase KshA and the reductase KshB, and is a key enzyme in bacterial steroid degradation, essential for the pathogenicity of Mycobacterium tuberculosis. KSH initiates opening of the steroid polycyclic ring structure
-
physiological function
-
the enzyme is essential for the pathogenicity of Mycobacterium tuberculosis
-
physiological function
-
the enzyme plays a role of cholesterol catabolism, overview
-
physiological function
-
KshA is the oxygenase component of 3-ketosteroid 9alpha-hydroxylase, a Rieske oxygenase involved in the bacterial degradation of steroids
-
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
-
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
-
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
-
physiological function
-
KshA is the oxygenase component of 3-ketosteroid 9alpha-hydroxylase, a Rieske oxygenase involved in the bacterial degradation of steroids
-
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
-
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
-
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
enzyme substrate binding pocket analysis using molecular modeling, overview. Modeling of substrates into KshA crystal structure using KshA structure PDB 2ZYL
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
-
molecular modelling of KshA, structure comparisons of KshAB enzyme, detailed overview
additional information
molecular modelling of KshA, structure comparisons of KshAB enzyme, detailed overview
additional information
-
structure-function relationship of KSH enzymes and components, overview
additional information
-
structure-function relationship of KSH enzymes and components, overview
additional information
-
structure-function relationship of KSH enzymes and components, overview
additional information
-
structure-function relationship of KSH enzymes and components, overview
additional information
structure-function relationship of KSH enzymes and components, overview
additional information
structure-function relationship of KSH enzymes and components, overview
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. 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
additional information
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structure-function relationship of KSH enzymes and components, overview
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additional information
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molecular modelling of KshA, structure comparisons of KshAB enzyme, detailed overview
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additional information
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structure-function relationship of KSH enzymes and components, overview
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additional information
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structure-function relationship of KSH enzymes and components, overview
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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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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
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additional information
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structure-function relationship of KSH enzymes and components, overview
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additional information
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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
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additional information
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KshA and KshB together constitute the KSH enzyme
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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
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additional information
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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
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additional information
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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
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T207V/T209S/Y211F/H213R/S214G/T215Q/G216A
V201T/S203T/F205Y/R207H/G208S/Q209T/A210G
D230E/S232T/F238Y
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
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V201T/S203T/F205Y/R207H/G208S/Q209T/A210G
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
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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
Q209T/A210G
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site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
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Q209T/A210G
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the mutant of isoform KshA1 exhibits 3-ketosteroid 9alpha-hydroxylase activity
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additional information
A0A0F7JI94; D2Y640
efficient 9alpha-hydroxy-4-androstene-3,17-dione production by engineered Bacillus subtilis co-expressing Mycobacterium neoaurum 3-ketosteroid 9alpha-hydroxylase and Bacillus subtilis glucose 1-dehydrogenase with NADH regeneration
additional information
recombinant coexpression of the enzyme KshA from Mycobacterium neoaurum strain NwIB-01 and the three homologues of ketosteroid-DELTA1-dehydrogenase (KstD) from Mycobacterium neoaurum ATCC257953 in Escherichia coli strain BL21(DE3)
additional information
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recombinant coexpression of the enzyme KshA from Mycobacterium neoaurum strain NwIB-01 and the three homologues of ketosteroid-DELTA1-dehydrogenase (KstD) from Mycobacterium neoaurum ATCC257953 in Escherichia coli strain BL21(DE3)
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additional information
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efficient 9alpha-hydroxy-4-androstene-3,17-dione production by engineered Bacillus subtilis co-expressing Mycobacterium neoaurum 3-ketosteroid 9alpha-hydroxylase and Bacillus subtilis glucose 1-dehydrogenase with NADH regeneration
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additional information
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recombinant coexpression of the enzyme KshA from Mycobacterium neoaurum strain NwIB-01 and the three homologues of ketosteroid-DELTA1-dehydrogenase (KstD) from Mycobacterium neoaurum ATCC257953 in Escherichia coli strain BL21(DE3)
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additional information
the insertion mutant 10A12 is blocked in 3-ketosteroid 9alpha-hydroxylation
additional information
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the insertion mutant 10A12 is blocked in 3-ketosteroid 9alpha-hydroxylation
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additional information
deletion of the gene encoding the reductase component KshB of 3-ketosteroid 9alpha-hydroxylase in Rhodococcus equi strain USA-18 by a PCR-targeted gene disruption method results in a mutant strain that accumulates up to 0.58 mg/ml 1,4-androstadiene-3,17-dione in the culture medium when 0.2% cholesterol is used as the carbon source. The mutant also accumulates 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid (DELTA1,4-BNC). 1,4-Androstadiene-3,17-dione in strain USA-18DELTAB8 preferentially imposes a feedback inhibition on the enzymes involved in the side chain oxidation of DELTA1,4-BNC, but not DELTA4-BNC. Mutant phenotypes, overview
additional information
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deletion of the gene encoding the reductase component KshB of 3-ketosteroid 9alpha-hydroxylase in Rhodococcus equi strain USA-18 by a PCR-targeted gene disruption method results in a mutant strain that accumulates up to 0.58 mg/ml 1,4-androstadiene-3,17-dione in the culture medium when 0.2% cholesterol is used as the carbon source. The mutant also accumulates 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid (DELTA1,4-BNC). 1,4-Androstadiene-3,17-dione in strain USA-18DELTAB8 preferentially imposes a feedback inhibition on the enzymes involved in the side chain oxidation of DELTA1,4-BNC, but not DELTA4-BNC. Mutant phenotypes, overview
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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
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
additional information
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 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
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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
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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
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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
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
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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
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
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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 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
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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
additional information
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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
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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 was severely impaired, but not completely blocked
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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
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additional information
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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
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additional information
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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
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additional information
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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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additional information
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construction of chol-4 enzyme DELTAkshA1,2,3 deletion mutants, genetic complementation of the DELTAkshA1,2,3 strain with KshA1 perfectly restores growth in CHO or cholic acid but not in androsta-4-ene-3,17-dione, androsta-1,4-diene-3,17-dione or DHEA, whereas the DELTAkshA2,3 does it to certain point. Mutant DELTAKshA3 can only grow using cholesterol as carbon source. KshA2 is only able to act on substrates with a short side chain
additional information
construction of chol-4 enzyme DELTAkshA1,2,3 deletion mutants, genetic complementation of the DELTAkshA1,2,3 strain with KshA1 perfectly restores growth in CHO or cholic acid but not in androsta-4-ene-3,17-dione, androsta-1,4-diene-3,17-dione or DHEA, whereas the DELTAkshA2,3 does it to certain point. Mutant DELTAKshA3 can only grow using cholesterol as carbon source. KshA2 is only able to act on substrates with a short side chain
additional information
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construction of chol-4 enzyme DELTAkshA1,2,3 deletion mutants, genetic complementation of the DELTAkshA1,2,3 strain with KshA1 perfectly restores growth in CHO or cholic acid but not in androsta-4-ene-3,17-dione, androsta-1,4-diene-3,17-dione or DHEA, whereas the DELTAkshA2,3 does it to certain point. Mutant DELTAKshA3 can only grow using cholesterol as carbon source. KshA2 is only able to act on substrates with a short side chain
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