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Literature summary extracted from

  • Martin, L.L.; Holien, J.K.; Mizrachi, D.; Corbin, C.J.; Conley, A.J.; Parker, M.W.; Rodgers, R.J.
    Evolutionary comparisons predict that dimerization of human cytochrome P450 aromatase increases its enzymatic activity and efficiency (2015), J. Steroid Biochem. Mol. Biol., 154, 294-301 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.14.14 expression in Escherichia coli Homo sapiens
1.14.14.14 expression in Escherichia coli Sus scrofa

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.14.14 molecular dynamics simulations of the dimeric interfaces, i.e.residues 45-496 Homo sapiens
1.14.14.14 molecular modeling of structure Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
1.14.14.14 Homo sapiens P11511
-
-
1.14.14.14 Sus scrofa P79304
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.14.14 androst-4-ene-3,17-dione + 3 O2 + 3 reduced flavoproteins
-
 Homo sapiens estrone + formate + 4 H2O + 3 oxidized flavoproteins
-
 ?
1.14.14.14 androst-4-ene-3,17-dione + 3 O2 + 3 reduced flavoproteins
-
 Sus scrofa estrone + formate + 4 H2O + 3 oxidized flavoproteins
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.14.14 homodimer FRET and crtystallization data Homo sapiens
1.14.14.14 homodimer FRET and crystallization data Sus scrofa

Synonyms

EC Number Synonyms Comment Organism
1.14.14.14 Cyp19A3
-
 Sus scrofa
1.14.14.14 cytochrome P450 aromatase
-
 Homo sapiens
1.14.14.14 P450arom
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.14.14.14 physiological function dimerization of the human P450arom, primarily via salt bridges at the I-H loop, leads to greater activity and reduced release of intermediates compared to porcine aromatase Homo sapiens
1.14.14.14 physiological function dimerization of the human P450arom, primarily via salt bridges at the IĀ–H loop, leads to greater activity and reduced release of intermediates compared to porcine aromatase.The porcine gonadal P450arom has no ionic interaction at the I-H loop but forms a new intra-molecular salt bridge at the N termini of the I-helix that leads to locking of the substrate Sus scrofa