The complete amino acid sequence of rat submaxillary gland tonin does contain the aspartic acid at the active site: confirmation by protein sequence analysis.
The revised amino acid sequence of rat submaxillary gland tonin, a serine protease, does contain the active site Asp residue. The active site of this kallikrein-related enzyme is thus made up of the same catalytic triad (Asp, Ser, and His) found in all known serine proteases. The important Asp residue has now been localized in a 16 amino acid peptide previously reported as missing in the tonin sequence. The complete amino acid sequence thus contains 235 residues corresponding to a molecular weight of 25,658, more in agreement with previously reported molecular weights. Moreover, the revised structure led (a) to the assignment of Arg, Asn, and Val residues instead of His, Asp, and Gly at positions 63, 165, and 169, respectively; (b) to the assignment of residues occupying an overlapping sequence at positions 165-171, and finally (c) to the localization of two N-glycosylation sites at positions 82 and 165. These results further document the close relationship of tonin to the ever expanding kallikrein family.
D000595:Amino Acid Sequence; D000818:Animals; D001224:Aspartic Acid; D001665:Binding Sites; D003488:Cyanogen Bromide; D007202:Indicators and Reagents; D010446:Peptide Fragments / Q000032:analysis; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D051381:Rats; D013363:Submandibular Gland / Q000201:enzymology*
D007202:Indicators and Reagents; D010446:Peptide Fragments; D001224:Aspartic Acid; D007703:Peptidyl-Dipeptidase A; D003488:Cyanogen Bromide