Mechanism of human placental aromatase: a new active site model.
Based on Akhtar's ferric peroxide mechanism and on recent studies in our own laboratory, we present a detailed proposal for aromatase action. This picture can account for the known stereochemical consequences at C-19 observed by others using isotopes of hydrogen and oxygen. The postulated process involves anchoring of the 19-hydroxymethyl and 19-oxo groups at the active site by a glutamate residue, which also serves to activate the 19-oxo group for attack by ferric peroxy species in the third oxidative step.
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Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185.
Robinson
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D000728:Androgens / Q000737:chemistry / Q000378:metabolism*; D001141:Aromatase / Q000378:metabolism*; D001665:Binding Sites; D004967:Estrogens / Q000737:chemistry / Q000378:metabolism; D005260:Female; D006801:Humans; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008962:Models, Theoretical; D008968:Molecular Conformation; D015394:Molecular Structure; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D013237:Stereoisomerism
D000728:Androgens; D004967:Estrogens; D001141:Aromatase