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[Identification of the reactive sites of kidney bean proteinase inhibitor]. 1982

V V Mosolov, and T A Valueva, and E L Malova, and G V Kolosova, and A N Cheban

The protein proteinase inhibitor from kidney bean (isoinhibitor, pI 4.3) is a double-headed inhibitor with independent reactive sites for trypsin and chymotrypsin. The reactive site of the inhibitor for trypsin is Lys (22)- Ser (23) in the sequense ...-Lys-Ser-Ile-Pro-Ala-Glx-Cys-Arg-..., the reactive site for chymotrypsin is Leu (64)-Ser (65) in the sequence ...-Thr-Leu-Ser-Ile-Pro-Ala-Glx-Cys-Arg-... .

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D002918 Chymotrypsin A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side. Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D014361 Trypsin Inhibitors Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds. Trypsin Inhibitor,Inhibitor, Trypsin,Inhibitors, Trypsin

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