title: Further characterization of endopeptidase H2 a serine proteinase from human urine.
abstract: A human urine serine proteinase chymotrypsin like hydrolyzes the peptide bonds: Phe-Ser (kinin); Gly-Gly, Leu-Arg, Phe-Lys (neuropeptides) and Gln-Gln (substance P). Endopeptidase H2 hydrolyzes better oligopeptides with 4 to 18 aminoacid residues than larger peptides, it does not hydrolyzes kininogen or proenkephalin. The enzyme behaves as an oligoendopeptidase.
mesh_terms: D000595:Amino Acid Sequence; D001920:Bradykinin / Q000737:chemistry; D010450:Endopeptidases / Q000652:urine*; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D012697:Serine Endopeptidases / Q000652:urine*; D013373:Substance P / Q000737:chemistry; D013379:Substrate Specificity
chemical_list: D009842:Oligopeptides; D010446:Peptide Fragments; D013373:Substance P; D010450:Endopeptidases; D012697:Serine Endopeptidases; D001920:Bradykinin