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Literature summary extracted from

  • Zarate-Perez, F.; Velazquez-Fernandez, J.B.; Jennings, G.K.; Shock, L.S.; Lyons, C.E.; Hackett, J.C.
    Biophysical characterization of Aptenodytes forsteri cytochrome P450 aromatase (2018), J. Inorg. Biochem., 184, 79-87 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.14 expression in Escherichia coli Aptenodytes forsteri

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.14.14 anastrozole two-step binding mechanism, Kd value 0.0002 mM Aptenodytes forsteri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.14.14 0.0002
-
 androst-4-ene-3,17-dione pH 7.4, temperature not specified in the publication Aptenodytes forsteri

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.14 Aptenodytes forsteri A0A087RFY9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.14 19-hydroxyandrost-4-ene-3,17-dione + O2 + a reduced flavoprotein
-
 Aptenodytes forsteri 19-oxo-androst-4-ene-3,17-dione + 2 H2O + an oxidized flavoprotein
-
 ?
1.14.14.14 androst-4-ene-3,17-dione + 3 O2 + 3 reduced flavoproteins
-
 Aptenodytes forsteri estrone + formate + 4 H2O + 3 oxidized flavoproteins
-
 ?
1.14.14.14 additional information androstenedione is the preferred substrate, the affinity of the intermediates progressively decrease with increased oxidation Aptenodytes forsteri ?
-
-
1.14.14.14 testosterone + 3 O2 + 3 reduced flavoproteins
-
 Aptenodytes forsteri 17beta-estradiol + formate + 4 H2O + 3 oxidized flavoproteins
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.14.14 0.02
-
 androst-4-ene-3,17-dione pH 7.4, temperature not specified in the publication Aptenodytes forsteri