A secondary isotope effect study of equine serum butyrylcholinesterase-catalyzed hydrolysis of acetylthiocholine

Chemico-Biological Interactions

Volumn 187, Issue 1-3, 2010, Pages 124-127

  Wiley, Kenneth L ^a   Tormos, Jose R ^a   Quinn, Daniel M ^a  

^a E11 SSH   (United States)

Author keywords

Butyrylcholinesterase; Catalytic mechanism; Isotope effects; Transition state structure

Indexed keywords

ACETYLTHIOCHOLINE; CHOLINESTERASE; RECOMBINANT ENZYME;

ACYLATION; ARTICLE; CATALYSIS; CONTROLLED STUDY; DECOMPOSITION; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; HYDROLYSIS; MICHAELIS MENTEN KINETICS;

EQUIDAE;

EID: 77955518702     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.05.007     Document Type: Article

References (13)

1. Quinn D.M. Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states. Chem. Rev. 1987, 87:955-979.
2. Rosenberry T.L. Acetylcholinesterase. Adv. Enzymol. Relat. Areas Mol. Biol. 1975, 43:103-218.
3. Masson P., Legrand P., Bartels C.F., Froment M.-T., Schopfer L.M., Lockridge O. Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase. Biochemistry 1997, 36:2266-2277.
4. N. Isaacs, Substitution reactions at carbon, Physical Organic Chemistry, Addison Wesley Longman Ltd., Harlow, England, 1995, pp. 418-536.
5. Hogg J.L. Secondary hydrogen isotope effects. Transition State of Biochemical Processes 1978, 201-224. Plenum Press, New York, London. R.D. Gandour, R.L. Schowen (Eds.).
6. Malany S., Sawai M., Sikorski R.S., Seravalli J., Quinn D.M., Radić Z., Taylor P., Kronman C., Velan B., Shafferman A. Transition state structure and rate determination for the acylation stage of acetylcholinesterase catalyzed hydrolysis of (acetylthio)choline. J. Am. Chem. Soc. 2000, 122:2981-2987.
7. Hammond G.S. A correlation of reaction rates. J. Am. Chem. Soc. 1955, 77:334-338.
8. Schowen R.L. Catalytic power and transition state stabilization. Transition State of Biochemical Processes 1978, 77-114. Plenum Press, New York, London. R.D. Gandour, R.L. Schowen (Eds.).
9. Tormos J.R., Wiley K.L., Seravalli J., Nachon F., Masson P., Nicolet Y., Quinn D.M. The reactant state for substrate-activated turnover of acetylthiocholine by butyrylcholinesterase is a tetrahedral intermediate. J. Am. Chem. Soc. 2005, 127:14538-14539.
10. Nicolet Y., Lockridge O., Masson P., Fontecilla-Camps J.C., Nachon F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J. Biol. Chem. 2003, 278:41141-41147.
11. Ellman G.L., Courtney K.D., Andres V., Featherstone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 1961, 7:88-95.
12. Northrop D.B. Determining the absolute magnitude of hydrogen isotope effects. Isotope Effects on Enzyme-Catalyzed Reactions 1977, 122-150. University Park Press, Baltimore, MD, USA. W.W. Cleland, M.H. O'Leary, D.B. Northrop (Eds.).
13. Cleland W.W. Secondary isotope effects on enzymatic reactions. Isotopes in Organic Chemistry 1987, vol. 7:61-113. Elsevier, Amsterdam.