[Kinetics of trypsin-catalyzed hydrolysis of some arginine-containing peptide methyl esters].
The kinetics of trypsin-catalyzed hydrolysis (at pH 8.5) of methyl esters of some synthetic dipeptides containing the residues of both arginine and L(D)-p-fluorophenylalanine or L(D)-tyrosine has been studied. The digestion of Tos-(pF)Phe-Arg-OMe was shown as unfollowing the Michaelis-Menten kinetic since in the reaction course the substrate activation is observed and while the reaction product is the enzymatic process inhibitor. In contrast to this, the hydrolysis of other substrates studied, follows the normal Michaelis-Menten kinetic.
Poiarkova
S A
SA
Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine, Kyiv.
Chetyrkina
S N
SN
Kibirev
V K
VK
D000409:Alanine / Q000737:chemistry; D001120:Arginine / Q000737:chemistry*; D002384:Catalysis / Q000187:drug effects; D004151:Dipeptides / Q000737:chemistry* / Q000378:metabolism*; D004789:Enzyme Activation; D004952:Esters / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis / Q000187:drug effects; D007700:Kinetics; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*; D014361:Trypsin Inhibitors / Q000494:pharmacology; D014443:Tyrosine / Q000737:chemistry
D004151:Dipeptides; D004952:Esters; D014361:Trypsin Inhibitors; D014443:Tyrosine; D001120:Arginine; D014357:Trypsin; D000409:Alanine