Human butyrylcholinesterase

K21. Khan, S., Hemalatha, R., Jeyaseelan, L., Oomen, A., and Zachariah, A., Neuroparalysis and oxime efficacy in organophosphate poisoning A study of butyrylcholinesterase. Human Exp. Toxicol. 20,169-174 (2001). 

Jbilo, O., Bartels, C.F., Chatonnet, A., Toutant,J.P. and Lockridge, O. (1994) Tissue distribution of human acetylcholinesterase and butyrylcholinesterase messenger RNA. Toxicon 32, 1445-1457. 

Fidder, A., Hulst, A.G., De Ruiter, R., Van Der Schans, M.J., Benschop, H.P., and Langenberg, J.P., (2002). Retrospective detection of exposure to organophosphorus anticholinesterases mass spectrometric analysis of phosphylated human butyrylcholinesterase. Chem. Res. Toxicol., 15, 582-590. 

Li B, Sedlacek M, Manoharan I, Boopathy R, Duysen EG, Masson P, Lockridge O (2005) Butyrylcholinesterase, paraoxonase, and albumin esterase, but no carboxylesterase, are present in human plasma. Biochem Pharmacol 70 1673-1684... 

Esterases that contribute to human drug metabolism fall into three major classes the cholinesterases (acetylcholinesterase, pseudocholinesterase, butyrylcholinesterase, etc.),... 

Inhibition of the two principal human cholinesterases, acetylcholinesterase and pseudocholinesterase, may not always result in visible neurological effects (Sundlof et al. 1984). Acetylcholinesterase, also referred to as true cholinesterase, red blood cell cholinesterase, or erythrocyte cholinesterase is found in erythrocytes, lymphocytes, and at nerve synapses (Goldfrank et al. 1990). Inhibition of erythrocyte or lymphocyte acetylcholinesterase is theoretically a reflection of the degree of synaptic cholinesterase inhibition in nervous tissue, and therefore a more accurate indicator than pseudocholinesterase activity of inhibited nervous tissue acetylcholinesterase (Fitzgerald and Costa 1993 Sundlof et al. 1984). Pseudocholinesterase (also referred to as cholinesterase, butyrylcholinesterase, serum cholinesterase, or plasma cholinesterase) is found in the plasma, serum, pancreas, brain, and liver and is an indicator of exposure to a cholinesterase inhibitor. 

To help the reader gain a better understanding of the three-dimensional structure of the catalytic site of an esterase, Fig. 3.8 presents the 3D structure of human butyrylcholinesterase (EC 3.1.1.8) obtained by homology modeling [42], The overall structure of the enzyme is shown in Fig. 3.8, a, while Fig. 3.8,b shows a closeup of the active site with the catalytic triad highlighted and the close spatial relationship of the Ser-His-Glu residues revealed. 

Thioesters play a paramount biochemical role in the metabolism of fatty acids and lipids. Indeed, fatty acyl-coenzyme A thioesters are pivotal in fatty acid anabolism and catabolism, in protein acylation, and in the synthesis of triacylglycerols, phospholipids and cholesterol esters [145], It is in these reactions that the peculiar reactivity of thioesters is of such significance. Many hydrolases, and mainly mitochondrial thiolester hydrolases (EC 3.1.2), are able to cleave thioesters. In addition, cholinesterases and carboxylesterases show some activity, but this is not a constant property of these enzymes since, for example, carboxylesterases from human monocytes were found to be inactive toward some endogenous thioesters [35] [146], In contrast, allococaine benzoyl thioester was found to be a good substrate of pig liver esterase, human and mouse butyrylcholinesterase, and mouse acetylcholinesterase [147],... 

C. B. Millard, O. Lockridge, C. A. Broomfield, Design and Expression of Organophos-phorus Acid Anhydride Hydrolase Activity in Human Butyrylcholinesterase , Biochemistry 1995, 34, 15925-15933. 

Levels of solanaceous glycoalkaloids can be significant, occasionally causing toxicity in humans and livestock. Symptoms of potato poisoning include gastrointestinal disturbances, apathy, drowsiness, mental confusion, visual disturbances, dizziness, hallucinations, and trembling. Symptoms may perist 2-24 hours after consumption, and one recent outbreak showed reduced butyrylcholinesterase levels six days later, which then returned to normal in 4 to 5 weeks. 

Kuznetsova LP, Nikol skaya EB, Sochilina EE, Inhibition of human blood acetylcholinesterase and butyrylcholinesterase by some alkaloids,/EvolBiochem Physiol 38 35-39, 2002. 

Primo-Parmo SL, Bartels CF, Wiersema B, van der Spek AF, Innis JW, LaDu BN. Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene. Am J Hum Genet 1996 58 52-64. 

Langenberg, Retrospective detection of exposure to organophosphorus anticholinesterases mass spectrometric analysis of phosphylated human butyrylcholinesterase, Chem. Res. Toxicol., 15, 582-590 (2002). 

Nachon F, Asojo OA, Borgstahl G, Masson P, Lockridge O (2005) Role of water in aging of human butyrylcholinesterase inhibited by echothiophate the crystal structure suggests two alternative mechanisms of aging, Biochemistry 44 1154-1162... 

Lapidot-Iifson Y, et al. Coamplification of human acetylcholinesterase and butyrylcholinesterase genes in blood cells correlation with various leukemias and abnormal megakaryocytopoiesis. Proc. Natl. Acad. Sci. USA, 1989, 86(12), 4715-4719. 

Kaplay SS (1976) Acetylcholinesterase and butyrylcholinesterase of developing human brain. Biol Neonate 28 65-73... 

Borovikova, L.V., Ivanova, S., Zhang, M., Yang, H., Botchkina, G.I., Watkins, L.R., Wang, H., Abumrad, N., Eaton, J.W., Tracey, K.J. (2000b). Vagus nerve stimulation attenuates the systemic inflammatory response to endotoxin. Nature 405 458-62. Brandeis, R., Raveh, L., Grunwald, J., Cohen, E., Ashani, Y. (1993). Prevention of soman-induced cognitive deficits by pretreatment with human butyrylcholinesterase in rats. Pharmacol. Biochem. Behav. 46 889-96. 

Kolarich, D., Weber, A., Pabst, M., Stadlmann, J., Teschner, W., Ehrlich, H., Schwarz, H.P., Altmann, F. (2008). Glyco-proteomic characterization of butyrylcholinesterase from human plasma. Proteomics 8 254-63. 

B. R., Cerasoli, D.M., Federko, J.M., Luo, C., Saxena, A., Doctor, B.P., Olson, C. (2005). Protection against soman or VX poisoning by human butyrylcholinesterase in guinea pigs and cynomolgus monkeys. Chem. Biol. Interact. 157-8 205-10. 

C.B., Broomfield, C.A. (1997). A single amino acid substitution, Glyll7His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase. Biochemistry 36 786-95. 

Millard, C.B., Lockridge, O., Broomfield, C.A. (1995). Design and expression of organophosphoms acid anhydride hydrolase activity in human butyrylcholinesterase. Biochemistry 34 15925-33. 

Ngamelue, M.N., Homma, K., Lockridge, O., Asojo, O.A. (2007). Crystallization and X-ray stmebue of full-length recombinant human butyrylcholinesterase. Acta Crystallogr. Sect. F Struct. Biol. Cry St. Commun. 63 723-7. 

Raveh, L., Grunwald, J., Marcus, D., Papier, Y., Cohen, E., Ashani, Y. (1993). Human butyrylcholinesterase as a general prophylactic antidote for nerve agent toxicity. In vitro and in vivo quantitative characterization. Biochem. Pharmacol. 45 2465-74. 

AChE - acetylcholinesterase BChE - butyrylcholinesterase CarbE - carboxylesterase CVX - Chinese VX hr wt - human recombinant wild-type k at catalytic constant for hydrolysis PONl - paraoxonase 1 VR - Russian VX... 

Lockridge, O., Schopfer, L.M., Winger G., Woods, J.H. (2005). Large scale purification of butyrylcholinesterase from human plasma suitable for injection into monkeys a potential new therapeutic for protection against cocaine and nerve agent toxicity. J. Med. GBR Def. 5 1-20. 

Saxena, A., Chun man, L., Doctor, B.P. (2008). Developing procedures for the large-scale purification of human serum butyrylcholinesterase. Protein Express. Purif. 61 191-6. 

Saxena, A., Redman, A.M.G., Jiang, X., Lockridge, O., Doctor, B.P. (1999). Differences in active-site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase. Chem. Biol. Interact. 119-20 61-9. 

---