Sandbox Reserved 382: Difference between revisions

Due to the membrane-bound nature of mammalian cytochromes P450 (CYP), the structural characterization is extremely difficult. Aromatase is a monomeric enzyme composed of a heme-prosthetic group and a single polypeptide chain consisting of 503 amino-acid residues. <ref> Ghosh, D., Griswold, J., Erman, M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals An Androgen Specific Active Site". [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref> One important feature of CYPs is the iron-containing porphyrin group at the enzyme active site. <ref> PMID: 16395678 </ref> Aromatase is anchored to the endoplasmic reticulum by the amino terminal transmembrane domain. The tertiary structure of Aromatase includes twelve major α-helices and ten β-strands<ref>Ghosh,D., Griswold,J., Erman,M., Pangborn, W. "X-ray Structure of Human Aromatase Reveals Androgen-Specific Active Site." [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2826573/] </ref>. An androstenedione molecule is bound to the active site of the enzyme. The active site of the enzyme can be found in the distal cavity of the heme-binding pocket. The reaction center of the enzyme is where the <scene name='Sandbox_Reserved_382/Heme_iron/1'>heme iron</scene> is located within the porphorin. The <scene name='Sandbox_Reserved_382/Ligand/1'>ligand</scene> is attached to the porphorin/heme group.