[Comparative study of enzymatic activity of cholinesterases of different origin in thionaphthylacetate hydrolysis reactions].
A comparative determination of kinetic parameters V and Km in the reaction of hydrolysis thionaphthylacetate and well known substrate acetylthiocholine by choline esterases from different sources was conducted. It is shown that butyrylcholine esterases hydrolyze thionaphthylacetate with velocity comparable with that of hydrolysis of acetylthiocholine, while acetylcholine esterases and propionylcholine esterases hydrolyze this substrate several times slower than acetylthiocholine. The values of Km in the reactions of hydrolysis of thionaphthylacetate for all studied cholinesterases is an order higher than for acetylthiocholine except cholinesterase of blood serum of fish. This value for the latter enzyme is practically equal.
Zhukovskiĭ
Iu G
IuG
Kuznetsova
L P
LP
Sochilina
E E
EE
Veksler
K V
KV
D000122:Acetylthiocholine / Q000737:chemistry; D000818:Animals; D002417:Cattle; D002802:Cholinesterases / Q000737:chemistry* / Q000378:metabolism; D005399:Fishes; D006801:Humans; D006868:Hydrolysis; D007700:Kinetics; D009281:Naphthalenes / Q000737:chemistry*; D013379:Substrate Specificity
C482606:1-thionaphthylacetate; D009281:Naphthalenes; D000122:Acetylthiocholine; D002802:Cholinesterases