The inhibition of a leaf proteinase by L-lysine homopolymers.
The role of interlinked positively charged amino acids in the mechanism of inhibition of a monomeric trypsin-like proteinase has been investigated using high molecular mass L-lysine homopolymers ranging from 3.8 to 109 kDa. The data show that the degree of polymerization enhances the inhibitory efficiency which is maximal for homopolymers with more than eighteen interlinked lysine residues. The inhibition is cooperative and, under the maximal inhibition conditions, nine lysine residues of the polymer are involved in the electrostatic binding to the enzyme. A limited conformational change of the protein molecule accompanies the transition from a fully active to a fully inactivated enzyme.
Amato
C
C
Istituto di Biofisica, CNR, Pisa, Italy.
Vaccari
L
L
Balestreri
E
E
Felicioli
R
R
D010450:Endopeptidases / Q000378:metabolism*; D008239:Lysine / Q000494:pharmacology*; D000455:Medicago sativa / Q000201:enzymology*; D011108:Polymers / Q000494:pharmacology; D011480:Protease Inhibitors / Q000494:pharmacology*; D011487:Protein Conformation
D011108:Polymers; D011480:Protease Inhibitors; D010450:Endopeptidases; D008239:Lysine