[Conformational aspects of beta-trypsin interaction with substrates and pancreatic trypsin inhibitor. III. Catalytic act of trypsin and its inhibition].
Basing on the results of the theoretical conformational analysis of the nonbonded and valence complexes of trypsin with substrate molecules, the catalytical act of the enzyme is described in details as a spontaneous process. Conformational aspects of interactions of trypsin with pancreatic trypsin inhibitor are analysed. The complete inhibition process and the geometry of the enzyme-inhibitor complex are described in details. The point amino acid replacements, which will provide for an exclusion of BPTI inhibition and will radically change the specificity of the enzyme are proposed.
E M
EM
Popov
N M
NM
Godzhaev
R E
RE
Aliev
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle; D002918:Chymotrypsin / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000378:metabolism*
D014361:Trypsin Inhibitors; D014359:Trypsin Inhibitor, Kazal Pancreatic; D002918:Chymotrypsin; D014357:Trypsin
Konformatsionnye aspekty vzaimodeĭstviia beta-tripsina s substratami i pankreaticheskim tripsinovym ingibitorom. III. Kataliticheskiĭ akt tripsina i ego ingibirovanie.