Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases.
D000595:Amino Acid Sequence; D001224:Aspartic Acid; D001665:Binding Sites; D002247:Carbon Isotopes; D002250:Carbon Radioisotopes; D002384:Catalysis; D002852:Chromatography, Ion Exchange; D010450:Endopeptidases / Q000032:analysis* / Q000378:metabolism; D006639:Histidine / Q000032:analysis; D006863:Hydrogen-Ion Concentration; D007093:Imidazoles / Q000032:analysis; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009231:Myxococcales / Q000201:enzymology; D011485:Protein Binding; D011487:Protein Conformation; D012694:Serine; D012697:Serine Endopeptidases; D013056:Spectrophotometry, Ultraviolet
D002247:Carbon Isotopes; D002250:Carbon Radioisotopes; D007093:Imidazoles; D001224:Aspartic Acid; D012694:Serine; D006639:Histidine; D010450:Endopeptidases; D012697:Serine Endopeptidases; C021826:myxobacter alpha-lytic proteinase