Avtor/Urednik		Stojan, Rok; Stojan, Žiga; Stojan, Jure
Naslov		Holin-esteraze: struktura, delovanje ter inhibicija z naravnimi in sintetičnimi strupi
Prevedeni naslov		Cholinesterases: structure, mechanism and inhibition by natural and synthetic poisons
Tip		članek
Vir		Med Razgl
Vol. in št.		Letnik 47, št. 3
Leto izdaje		2008
Obseg		str. 293-307
Jezik		slo
Abstrakt		Cholinesterases are involved in terminating nerve impulses in the central nervous system and at the periphery. The high enzyme concentration at the cholinergic synapses is achieved by oligomerization on an anchoring, collagen-like peptide. The 3D structure of a monomer shows a buried active site, which is responsible for the effectiveness and specificity of the enzyme, but also for various pseudocooperative phenomena. Due to its important role, acetylcholinesterase is a target for various inhibitors, natural as well as artificial ones. Reversible inhibitors prevent substrate accommodation by stericaily blocking the active site and the irreversible ones act as acylating agents that modify the active site serine, the major participant in covalent catalysis. When irreversibly inhibited by potent nerve gases, cholinesterases can be reactivated, unless partial dealkylation of the bound inhibitor has occurred. This particular phenomenon, called aging of cholinesterases, along with generalized cytotoxic effect appear to be the cause of organophosphate-induced delayed neurotoxicity in nerve gas poisoned casualties.
Deskriptorji		CHOLINESTERASES CHOLINESTERASE INHIBITORS ACETYLCHOLINESTERASE BINDING SITES KINETICS ENZYME REACTIVATORS CHEMICAL WARFARE AGENTS