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Literature summary extracted from

  • Van Der Geize, R.; Hessels, G.; Nienhuis-Kuiper, M.; Dijkhuizen, L.
    Characterization of a second Rhodococcus erythropolis SQ1 3-ketosteroid 9alpha-hydroxylase activity comprising a terminal oxygenase homologue, KshA2, active with oxygenase-reductase component KshB (2008), Appl. Environ. Microbiol., 74, 7197-7203.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.15.30 4-androstene-3,17-dione + O2 + NADH + H+
-
 Rhodococcus erythropolis 9alpha-hydroxyandrosta-4-en-3,17-dione + H2O + NAD+
-
 ir
1.14.15.30 4-androstene-3,17-dione + O2 + NADH + H+
-
 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
-
 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
-
 Rhodococcus erythropolis SQ1 9alpha-hydroxyandrosta-1,4-diene-3,17-dione + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
 ir

Synonyms

EC Number Synonyms Comment Organism
1.14.15.30 3-ketosteroid 9alpha-hydroxylase
-
 Rhodococcus erythropolis
1.14.15.30 KSH
-
 Rhodococcus erythropolis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.15.30 [2Fe-2S]-center
-
 Rhodococcus erythropolis

Expression

EC Number Organism Comment 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 Comment 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