N-Terminal amino acid sequence of rat tonin: homology with serine proteases.
In this paper, we present the amino-terminal sequence of rat tonin, an endopeptidase responsible for the conversion of angiotensinogen, the tetradecapeptide renin substrate, or angiotensin I to angiotensin II. It is shown that isoleucine and proline occupy the amino- and carboxy-terminal residues respectively. The N-terminal sequence analysis permitted the identification of 34 out of the first 40 residues of the single polypeptide chain composed of 272 amino acids. These results showed an extensive homology with the sequence of many serine proteases of the trypsin-chymotrypsin family. This information, coupled with the slow inhibition of tonin by diisopropylfluorophosphate, classified this enzyme as a selective endopeptidase of the active serine protease family.
D000595:Amino Acid Sequence; D000818:Animals; D010450:Endopeptidases; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D007703:Peptidyl-Dipeptidase A; D051381:Rats; D012694:Serine; D013045:Species Specificity; D013363:Submandibular Gland / Q000201:enzymology
D010446:Peptide Fragments; D012694:Serine; D010450:Endopeptidases; D010447:Peptide Hydrolases; D007703:Peptidyl-Dipeptidase A