title: Structure of mouse submaxillary gland renin.
abstract: To determine the structural basis for the highly specific action of renin, structural features of the active site and the complete amino acid sequence of mouse submaxillary gland renin were determined. A rapid method was developed for a large scale purification of renin from mouse submaxillary gland. The active site of renin was shown to consist of 2 aspartyl residues, 2 tyrosyl residues and one arginyl residue, the structures analogous to the active site of pepsin and other acid proteases. Renin was found to consist of one heavy chain (Mr = 31,036) and one light chain (Mr = 5,458) connected by a disulfide bridge. Amino acid sequences of these chains were determined using overlapping peptides generated by cleavage with cyanogen bromide, trypsin, Staphylococcus aureus protease and Lysobacter enzymogenes endoproteinase Lys-C. Sequences involving 2 catalytically essential aspartyl residues 32 and 215, characteristic to acid proteases, were found identical with pepsin, penicillopepsin and chymosin. The sequence of L-chain was homologous with carboxyl terminal region of porcine pepsin in 46% of amino acid residues. H-chain showed 41% homology with 284 residues on the amino-terminal side of the porcine pepsin molecule. Residues identical in renin and acid proteases are distributed throughout the length of the molecules, suggesting a similarity in their overall structure.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001665:Binding Sites; D055598:Chemical Phenomena; D002621:Chemistry; D008297:Male; D051379:Mice; D008970:Molecular Weight; D011487:Protein Conformation; D012083:Renin / Q000032:analysis*; D013363:Submandibular Gland / Q000201:enzymology*
chemical_list: D000596:Amino Acids; D012083:Renin