A possible evolutionary relationship between plant trypsin inhibitor, alpha-amylase inhibitor, and mammalian pancreatic secretory trypsin inhibitor (Kazal).
The amino acid sequence of the carboxyl-terminal half of barley trypsin inhibitor was found to be significantly similar to the whole sequence of bovine pancreatic secretory trypsin inhibitor (Kazal). Kazal type inhibitors and related proteins are known for the extraordinary mode of divergence among animals, and the present observation extends this to a plant for the first time. The present observation together with our previous finding of sequence homology between barley trypsin inhibitor and wheat alpha-amylase inhibitor (Odani, S., Koide, T., & Ono, T. (1982) FEBS Lett. 141, 279-282) suggest an unusual evolutionary relationship between cereal enzyme inhibitors and animal proteinase inhibitors of the Kazal type.
D000595:Amino Acid Sequence; D005075:Biological Evolution; D010940:Plant Proteins; D010944:Plants / Q000201:enzymology; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000235:genetics*; D014361:Trypsin Inhibitors / Q000235:genetics*; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
D010940:Plant Proteins; D014361:Trypsin Inhibitors; D014359:Trypsin Inhibitor, Kazal Pancreatic; D000516:alpha-Amylases