Phenylethanolamine N-methyltransferase kinetics: bovine versus recombinant human enzyme

Phenylethanolamine N-methyltransferase kinetics: bovine versus recombinant human enzyme Structure-Based Drug Design of Bisubstrate Inhibitors of Phenylethanolamine N-Methyltransferase Possessing Low Nanomolar Affinity at Both Substrate Binding Domains¹ Conformational requirements of substrates for activity with phenylethanolamine N-methyltransferase Stereochemical aspects of phenylethanolamine analogs as substrates of phenylethanolamine N-methyltransferase Molecular Recognition of Sub-micromolar Inhibitors by the Epinephrine-Synthesizing Enzyme Phenylethanolamine N-Methyltransferase Inhibitors of phenylethanolamine N-methyltransferase and epinephrine biosynthesis. 1. Chloro-Substituted 1,2,3,4-tetrahydroisoquinolines Conformationally defined adrenergic agents. 15. Conformationally restricted and conformationally defined tyramine analogs as inhibitors of phenylethanolamine N-methyltransferase Structural, Mutagenic, and Kinetic Analysis of the Binding of Substrates and Inhibitors of Human PhenylethanolamineN-Methyltransferase Conformational preference for the binding of biaryl substrates and inhibitors to the active site of phenylethanolamine N-methyltransferase (PNMT) Importance of the aromatic ring in adrenergic amines. 5. Nonaromatic analogs of phenylethanolamine as inhibitors of phenylethanolamine N-methyltransferase: role of hydrophobic and steric interactions