Cholinesterase: Substrate inhibition and substrate activation

Pflugers Archiv European Journal of Physiology

Volumn 440, Issue SUPPL. 5, 2000, Pages

  Reiner, E ^a   Simeon Rudolf, V ^a  

^a INSTITUTE FOR MEDICAL RESEARCH AND OCCUPATIONAL HEALTH   (Croatia)

Author keywords

Acetylcholinesterase; Apparent substrate inhibition and activation; Butyrylcholinesterase; Catalytic constants; Substrate inhibition and activation

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE; ACETYLTHIOCHOLINE; BENZOYLCHOLINE; BUTYRYLTHIOCHOLINE;

CHOLINERGIC SYSTEM; CONFERENCE PAPER; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME SUBSTRATE; PRIORITY JOURNAL; ARTICLE; CATALYSIS; ERYTHROCYTE; HORSE; HUMAN; HUMAN CELL; HYDROLYSIS; MICHAELIS CONSTANT; NONHUMAN; SUBSTRATE CONCENTRATION;

EID: 0033826918     PISSN: 00316768     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004240000029     Document Type: Conference Paper

References (8)

1. Substrate activation and thermal denaturation kinetics of the tetrameric and the trypsin-generated monomeric forms of the horse serum butyrylcholinesterase
2. Asp.70 in the peripheral anionic site of human butyrylcholinesterase
3. Role of the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives
4. Binding sites on acetylcholinesterase and butyrylcholinesterase for pyridinium and imidazolium oximes, and other reversible ligands
5. Michaelis constants and substrata inhibition constants for the reaction of acetylthiocholine with acetyl-cholinesterase and cholinesterase
6. Catalytic parameters for the hydrolysis of butyrylthiocholine by hum an serum butyrylcholinesterase variants
7. Kinetics of some complex enzyme reaction types