Transition state structure and rate determination for the acylation stage of acetylcholinesterase catalyzed hydrolysis of (acetylthio)choline

Journal of the American Chemical Society

Volumn 122, Issue 13, 2000, Pages 2981-2987

  Malany, Siobhan ^a,b   Sawai, Monali ^a   Sikorski, R Steven ^a   Seravalli, Javier ^a,d   Quinn, Daniel M ^a   Radić, Zoran ^b   Taylor, Palmer ^b   Kronman, Chanoch ^c   Velan, Baruch ^c   Shafferman, Avigdor ^c  

^a E11 SSH   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c ISRAEL INSTITUTE FOR BIOLOGICAL RESEARCH   (Israel)

^d UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; ISOTOPE; SOLVENT;

ACYLATION; ARTICLE; CATALYSIS; DIFFUSION; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; NONLINEAR SYSTEM; VISCOSITY;

EID: 0034607435     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja9933590     Document Type: Article

References (46)

1. Abbreviations: ACh, acetylcholine; AChE, acetylcholinesterase; Ala, alanine; ATCh, (acetylthio)choline; DTNB, 5,5′-dithiobis(2-nitrobenzoic acid); Glu, glutamate; Gln, glutamine; His, histidine; HuAChE, human AChE.; MAChE, mouse AChE; Ser, serine; TcAChE, Torpedo californica AChE; TX100, Triton X-100.
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45. A preliminary account of the work described in this paper was reported in the following reference: Malany, S.; Sikorski, R. S.; Seravalli, J.; Medhekar, R.; Quinn, D. M.; Radić, Z.; Taylor, P.; Velan, B.; Kronman, C.; Shafferman, A. In Structure and Function of Cholinesterases and Related Proteins; Doctor, B. P., Taylor, P., Quinn, D. M., Rotundo, R. L., Gentry, M. K., Eds.; Plenum Press: New York and London, 1998; pp 197-202.
46. 2 distance at 1.48 Å, calculated according to eq 10 with f = 0.76 and D(1) = 1.413 Å; this procedure is the same as that used to generate the transition state model described in Table 2 and Figure 3. As before, this new transition state model bears appreciable structural similarity to its cognate tetrahedral intermediate, particularly with respect to bond angles in which the carbonyl carbon is the central atom.