Ionization behavior of the histidine residue in the catalytic triad of serine proteases. Mechanistic implications.
D001224:Aspartic Acid / Q000378:metabolism; D002247:Carbon Isotopes; D002250:Carbon Radioisotopes; D002384:Catalysis; D055598:Chemical Phenomena; D002621:Chemistry; D004355:Drug Stability; D010450:Endopeptidases / Q000096:biosynthesis / Q000378:metabolism*; D006639:Histidine / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007093:Imidazoles / Q000378:metabolism; D007477:Ions; D009682:Magnetic Resonance Spectroscopy; D009231:Myxococcales / Q000201:enzymology*; D011485:Protein Binding; D011522:Protons; D012694:Serine / Q000378:metabolism
D002247:Carbon Isotopes; D002250:Carbon Radioisotopes; D007093:Imidazoles; D007477:Ions; D011522:Protons; D001224:Aspartic Acid; D012694:Serine; D006639:Histidine; D010450:Endopeptidases