Avtor/Urednik		Stojan, Jure
Naslov		Homology built model of acetylcholinesterase from Drosophila melanogaster
Tip		članek
Vir		J Enzym Inhib
Vol. in št.		Letnik 14
Leto izdaje		1999
Obseg		str. 193-201
Jezik		eng
Abstrakt		Acetylchotinesterases from Drosaphila melanogaster and Torpedo marmorata possess 35% identical residues. We built a homology model of the Drosophila enzyme on the basis of the known three-dimensional structure of Torpedo acetylcholinesterase, which revealed an oval rim of the active site gorge with an additional hollow which could accept small charged ligands more firmly than the corresponding surface in the Torpedo enzyme. This difference at the peripheral site, together with the kinetics of W 121A and W359L mutants, suggests coordinate action of important hydrophobic residues that form the active site gorge during the cstalytic process. It may also account for the activation-inhibition kinetic pattern which is characteristic for the insect enzyme.
Deskriptorji		ACETYLCHOLINESTERASE ACETYLCHOLINE CHOLINE COMPUTER SIMULATION MODELS, MOLECULAR MOLECULAR SEQUENCE DATA MUTATION DROSOPHILA MELANOGASTER SEQUENCE ALIGNMENT TORPEDO SEQUENCE HOMOLOGY, AMINO ACID