title: Structural features of two kininase I-type enzymes revealed by molecular cloning.
abstract: Kininase I-type carboxypeptidases remove a single C-terminal Arg residue from kinins. The circulating kininase I (carboxypeptidase N) contains two types of subunits: a 50 kDa catalytic subunit and an 83 kDa carrier subunit which protects the active subunit in blood. The 83 kDa subunit contains 12 leucine-rich tandem repeats, similar in sequence to other proteins with binding functions. Human carboxypeptidase M is a widely distributed "tissue kininase I" bound to plasma membranes. It has 41% sequence identity with the 50 kDa subunit of carboxypeptidase N and may regulate the activity of kinins and other peptides at the cell surface.
authors: Laboratory of Peptide Research, University of Illinois College of Medicine, Chicago 60612.
authors: R A
authors: RA
authors: Skidgel
authors: F
authors: F
authors: Tan
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D016384:Consensus Sequence; D058851:GPI-Linked Proteins; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000737:chemistry / Q000235:genetics*; D008666:Metalloendopeptidases / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D012091:Repetitive Sequences, Nucleic Acid; D017386:Sequence Homology, Amino Acid
chemical_list: D058851:GPI-Linked Proteins; C058479:carboxypeptidase M; D001121:Lysine Carboxypeptidase; D008666:Metalloendopeptidases