BRENDA - Enzyme Database

Characterization of a second Rhodococcus erythropolis SQ1 3-ketosteroid 9alpha-hydroxylase activity comprising a terminal oxygenase homologue, KshA2, active with oxygenase-reductase component KshB

Van Der Geize, R.; Hessels, G.; Nienhuis-Kuiper, M.; Dijkhuizen, L.; Appl. Environ. Microbiol. 74, 7197-7203 (2008)

Data extracted from this reference:

Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.14.15.30
Rhodococcus erythropolis
B2ZFP6
terminal oxygenase homologue KshA2
-
1.14.15.30
Rhodococcus erythropolis
B5TYS8
KshA3
-
1.14.15.30
Rhodococcus erythropolis SQ1
B2ZFP6
terminal oxygenase homologue KshA2
-
1.14.15.30
Rhodococcus erythropolis SQ1
B5TYS8
KshA3
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.15.30
4-androstene-3,17-dione + O2 + NADH + H+
-
717119
Rhodococcus erythropolis
9alpha-hydroxyandrosta-4-en-3,17-dione + H2O + NAD+
-
-
-
ir
1.14.15.30
4-androstene-3,17-dione + O2 + NADH + H+
-
717119
Rhodococcus erythropolis SQ1
9alpha-hydroxyandrosta-4-en-3,17-dione + H2O + NAD+
-
-
-
ir
1.14.15.30
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717119
Rhodococcus erythropolis
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
ir
1.14.15.30
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717119
Rhodococcus erythropolis SQ1
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
ir
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.14.15.30
[2Fe-2S]-center
;
Rhodococcus erythropolis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.14.15.30
[2Fe-2S]-center
-
Rhodococcus erythropolis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.14.15.30
4-androstene-3,17-dione + O2 + NADH + H+
-
717119
Rhodococcus erythropolis
9alpha-hydroxyandrosta-4-en-3,17-dione + H2O + NAD+
-
-
-
ir
1.14.15.30
4-androstene-3,17-dione + O2 + NADH + H+
-
717119
Rhodococcus erythropolis SQ1
9alpha-hydroxyandrosta-4-en-3,17-dione + H2O + NAD+
-
-
-
ir
1.14.15.30
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717119
Rhodococcus erythropolis
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
ir
1.14.15.30
androsta-1,4-diene-3,17-dione + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
-
717119
Rhodococcus erythropolis SQ1
9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
ir
Expression
EC Number
Organism
Commentary
Expression
1.14.15.30
Rhodococcus erythropolis
expression of kshA2 is induced in parent strain Rhodococcus erythropolis SQ1 in the presence of androsta-1,4-diene-3,17-dione or 9alpha-hydroxy-4-androstene-3,17-dione or a metabolite thereof
up
General Information
EC Number
General Information
Commentary
Organism
1.14.15.30
malfunction
gene deletion of kshA2 does not affect growth on 9alpha-hydroxy-4-androstene-3,17-dione, cholesterol, or cholic acid
Rhodococcus erythropolis
1.14.15.30
physiological function
3-ketosteroid 9alpha-hydroxylase is a key enzyme in microbial steroid degradation in Rhodococcus erythropolis strain SQ1 and is comprised of the terminal oxygenase component KshA1 and the oxygenase-reductase component KshB, a terminal oxygenase homologue KshA2 and homologue KshA3. Component KshA2 plays a role in preventing accumulation of toxic intracellular concentrations of 1,4-androstadiene-3,17-dione during steroid catabolism; 3-ketosteroid 9alpha-hydroxylase is a key enzyme in microbial steroid degradation in Rhodococcus erythropolis strain SQ1 and is comprised of the terminal oxygenase component KshA1 and the oxygenase-reductase component KshB, a terminal oxygenase homologue KshA2 and homologue KshA3. Component KshA2 plays a role in preventing accumulation of toxic intracellular concentrations of 1,4-androstadiene-3,17-dione during steroid catabolism
Rhodococcus erythropolis
General Information (protein specific)
EC Number
General Information
Commentary
Organism
1.14.15.30
malfunction
gene deletion of kshA2 does not affect growth on 9alpha-hydroxy-4-androstene-3,17-dione, cholesterol, or cholic acid
Rhodococcus erythropolis
1.14.15.30
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
Rhodococcus erythropolis
Expression (protein specific)
EC Number
Organism
Commentary
Expression
1.14.15.30
Rhodococcus erythropolis
expression of kshA2 is induced in parent strain Rhodococcus erythropolis SQ1 in the presence of androsta-1,4-diene-3,17-dione or 9alpha-hydroxy-4-androstene-3,17-dione or a metabolite thereof
up