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Literature summary for 1.14.15.30 extracted from

  • Petrusma, M.; Dijkhuizen, L.; van Der Geize, R.
    Structural features in the KshA terminal oxygenase protein that determine substrate preference of 3-ketosteroid 9alpha-hydroxylase enzymes (2012), J. Bacteriol., 194, 115-121.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli C41(DE3) cells Rhodococcus rhodochrous
expression of chimeric kshA mutant genes, KshA1A5beta and KshA5A1beta, in Escherichia coli, coexpression of the His-tagged KshA mutants with His-tagged KshB, molar ratio of KshA5A1/KshB is 1:8, low expression level of soluble KshA5A1alpha enzyme Rhodococcus rhodochrous

Protein Variants

Protein Variants Comment Organism
D230E/S232T/F238Y site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Rhodococcus rhodochrous
D230E/S232T/F238Y the mutant of isoform KshA1 shows no 3-ketosteroid 9alpha-hydroxylase activity Rhodococcus rhodochrous
D242W site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Rhodococcus rhodochrous
D242W the mutant of isoform KshA1 exhibits 3-ketosteroid 9alpha-hydroxylase activity Rhodococcus rhodochrous
E236D/T238S/Y244F site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Rhodococcus rhodochrous
E236D/T238S/Y244F the mutant of isoform KshA5 shows no 3-ketosteroid 9alpha-hydroxylase activity Rhodococcus rhodochrous
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 Rhodococcus rhodochrous
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 Rhodococcus rhodochrous
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 Rhodococcus rhodochrous
Q209T/A210G site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Rhodococcus rhodochrous
Q209T/A210G the mutant of isoform KshA1 exhibits 3-ketosteroid 9alpha-hydroxylase activity Rhodococcus rhodochrous
T207V/T209S/Y211F/H213R/S214G/T215Q/G216A site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Rhodococcus rhodochrous
T207V/T209S/Y211F/H213R/S214G/T215Q/G216A the mutant of isoform KshA5 exhibits 3-ketosteroid 9alpha-hydroxylase activity Rhodococcus rhodochrous
V201T/S203T/F205Y/R207H/G208S/Q209T/A210G site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Rhodococcus rhodochrous
V201T/S203T/F205Y/R207H/G208S/Q209T/A210G the mutant of isoform KshA1 exhibits 3-ketosteroid 9alpha-hydroxylase activity Rhodococcus rhodochrous
W248D site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme Rhodococcus rhodochrous
W248D the mutant of isoform KshA5 exhibits 3-ketosteroid 9alpha-hydroxylase activity Rhodococcus rhodochrous

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic analysis of the activity of KshA mutants with 4-23,24-bisnorcholesta-4-ene-22-oic acid Rhodococcus rhodochrous
0.01
-
23,24-bisnorcholesta-4-ene-22-oic acid Km less than 0.01 mM, isoform KshA1, in 50mMTris-HCl buffer (pH 7.0), temperature not specified in the publication Rhodococcus rhodochrous
0.01
-
23,24-bisnorcholesta-4-ene-22-oic acid Km less than 0.01 mM, isoform KshA5, in 50 mM Tris-HCl buffer (pH 7.0), temperature not specified in the publication Rhodococcus rhodochrous

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the enzyme contains a nonheme Fe2+ Rhodococcus rhodochrous

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 Rhodococcus rhodochrous
-
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?

Organism

Organism UniProt Comment Textmining
Rhodococcus rhodochrous F1CMX0 gene kshA1, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase
-
Rhodococcus rhodochrous F1CMX0 isozyme KshA1
-
Rhodococcus rhodochrous F1CMX3 gene kshB, encoding the ferredoxin reductase
-
Rhodococcus rhodochrous F1CMY8 gene kshA5, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase
-
Rhodococcus rhodochrous F1CMY8 isozyme KshA5
-
Rhodococcus rhodochrous DSM 43269 F1CMX0 gene kshA1, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase
-
Rhodococcus rhodochrous DSM 43269 F1CMX0 isozyme KshA1
-
Rhodococcus rhodochrous DSM 43269 F1CMX3 gene kshB, encoding the ferredoxin reductase
-
Rhodococcus rhodochrous DSM 43269 F1CMY8 gene kshA5, encoding an isoform of the oxygenase component of 3-ketosteroid 9alpha-hydroxylase
-
Rhodococcus rhodochrous DSM 43269 F1CMY8 isozyme KshA5
-

Purification (Commentary)

Purification (Comment) Organism
copurification of recombinant His-tagged KshA mutants with His-tagged KshB Rhodococcus rhodochrous

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the wild type homologue KshA1 shows 244% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous ? + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the wild type homologue KshA5 shows 51% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous ? + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the wild type homologue KshA1 shows 244% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous DSM 43269 ? + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1,4-androstadiene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the wild type homologue KshA5 shows 51% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous DSM 43269 ? + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
1-(5alpha)-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous 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 the wild type homologue KshA1 shows 23% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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 the wild type homologue KshA5 shows 99% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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
-
Rhodococcus rhodochrous DSM 43269 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
-
Rhodococcus rhodochrous 9alpha-hydroxy-11beta-hydrocortisone + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
11beta-hydrocortisone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the wild type homologue KshA5 shows 93% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 9alpha-hydroxy-11beta-hydrocortisone + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
11beta-hydrocortisone + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous DSM 43269 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
-
Rhodococcus rhodochrous 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 i.e. nordion, the wild type homologue KshA1 shows 24% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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 i.e. nordion, the wild type homologue KshA5 shows 111% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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
-
Rhodococcus rhodochrous DSM 43269 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 the wild type homologue KshA1 shows 548% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 9alpha-hydroxy-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
23,24-bisnorcholest-4-en-22-oic acid + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the wild type homologue KshA5 shows 88% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 9alpha-hydroxy-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
-
Rhodococcus rhodochrous 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
-
Rhodococcus rhodochrous DSM 43269 9alpha-hydroxy-3-oxo-23,24-bisnorcholest-4-en-22-oic acid + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
4-androstene-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous 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 i.e. testosterone, the wild type homologue KshA1 shows 158% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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 i.e. testosterone, the wild type homologue KshA5 shows 113% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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
-
Rhodococcus rhodochrous DSM 43269 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
-
Rhodococcus rhodochrous 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the wild type homologue KshA1 shows 100% activity Rhodococcus rhodochrous 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
4-androstene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 the wild type homologue KshA5 shows 100% activity Rhodococcus rhodochrous 9alpha-hydroxy-4-androstene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
4-pregnene-3,20-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous 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 i.e. progesterone, the wild type homologue KshA1 shows 372% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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 i.e. progesterone, the wild type homologue KshA5 shows 65% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 9alpha-hydroxy-4-pregnene-3,20-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
5alpha-androstane-17beta-ol-3-one + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
Rhodococcus rhodochrous 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 i.e. stanolon, the wild type homologue KshA5 shows 100% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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
-
Rhodococcus rhodochrous 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 the wild type homologue KshA1 shows 12% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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 the wild type homologue KshA5 shows 73% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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
-
Rhodococcus rhodochrous 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 the wild type homologue KshA1 shows 19% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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 the wild type homologue KshA5 shows 99% activity compared to 4-androstene-3,17-dione Rhodococcus rhodochrous 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
-
Rhodococcus rhodochrous 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
?
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) Rhodococcus rhodochrous ?
-
?
additional information the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids Rhodococcus rhodochrous ?
-
?
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 Rhodococcus rhodochrous ?
-
?
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 Rhodococcus rhodochrous ?
-
?
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 Rhodococcus rhodochrous ?
-
?
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) Rhodococcus rhodochrous DSM 43269 ?
-
?
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 Rhodococcus rhodochrous DSM 43269 ?
-
?
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 Rhodococcus rhodochrous DSM 43269 ?
-
?
additional information the KshA5 homologue has a broad substrate range with no apparent preference for any of the tested steroids Rhodococcus rhodochrous DSM 43269 ?
-
?
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 Rhodococcus rhodochrous DSM 43269 ?
-
?

Synonyms

Synonyms Comment Organism
3-ketosteroid 9alpha-hydroxylase
-
Rhodococcus rhodochrous
KSH
-
Rhodococcus rhodochrous
KshA terminal oxygenase component of 3-ketosteroid 9alpha-hydroxylase Rhodococcus rhodochrous
KshA1 isoform Rhodococcus rhodochrous
KshA5 isoform Rhodococcus rhodochrous
KshAB
-
Rhodococcus rhodochrous
KshB reductase component of 3-ketosteroid 9alpha-hydroxylase Rhodococcus rhodochrous

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
assay at Rhodococcus rhodochrous

Cofactor

Cofactor Comment Organism Structure
additional information a Rieske nonheme monooxygenase Rhodococcus rhodochrous
[2Fe-2S]-center
-
Rhodococcus rhodochrous

General Information

General Information Comment Organism
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 Rhodococcus rhodochrous
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 Rhodococcus rhodochrous