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Literature summary for 1.14.14.14 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)

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

Crystallization (Commentary)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P11511
-
-
Sus scrofa P79304
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

General Information

General Information Comment Organism
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
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