The copper-enzyme family of dopamine beta-monooxygenase and peptidylglycine alpha-hydroxylating monooxygenase: resolving the chemical pathway for substrate hydroxylation.
Klinman
Judith P
JP
Department of Chemistry and Molecular and Cell Biology, University of California, Berkeley, California 94720, USA. klinman@berkeley.edu
D000818:Animals; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D004298:Dopamine / Q000737:chemistry*; D004299:Dopamine beta-Hydroxylase / Q000737:chemistry*; D006418:Heme / Q000737:chemistry; D006859:Hydrogen / Q000737:chemistry; D007501:Iron / Q000737:chemistry; D006899:Mixed Function Oxygenases / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D009097:Multienzyme Complexes / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry; D011487:Protein Conformation; D013379:Substrate Specificity; D014965:X-Rays
D009097:Multienzyme Complexes; D006418:Heme; D003300:Copper; D006859:Hydrogen; D007501:Iron; D006899:Mixed Function Oxygenases; D004299:Dopamine beta-Hydroxylase; C035189:peptidylglycine monooxygenase; D010100:Oxygen; D004298:Dopamine