메뉴 건너뛰기




Volumn 275, Issue 10, 2008, Pages 2617-2631

Kinetic analysis of effector modulation of butyrylcholinesterase-catalysed hydrolysis of acetanilides and homologous esters

Author keywords

Aryl acylamidase; Benzalkonium; Butyrylcholinesterase; Serotonin; Tyramine

Indexed keywords

ACETANILIDE DERIVATIVE; ARYL ACYLAMIDASE; BENZALKONIUM; CHOLINESTERASE; ESTER DERIVATIVE; ESTERASE; PROPANIL; SEROTONIN; TYRAMINE;

EID: 42649137543     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06409.x     Document Type: Article
Times cited : (20)

References (74)
  • 3
    • 0000425486 scopus 로고
    • The possible biological function of pseudocholinesterase
    • Clitherow JW, Mitchard M Harper NJ (1963) The possible biological function of pseudocholinesterase. Nature 199, 1000 1001.
    • (1963) Nature , vol.199 , pp. 1000-1001
    • Clitherow, J.W.1    Mitchard, M.2    Harper, N.J.3
  • 4
    • 0028238432 scopus 로고
    • Serum pseudocholinesterase and very-low-density lipoprotein metabolism
    • Kutty KM Payne RH (1994) Serum pseudocholinesterase and very-low-density lipoprotein metabolism. J Clin Lab Anal 8, 247 250.
    • (1994) J Clin Lab Anal , vol.8 , pp. 247-250
    • Kutty, K.M.1    Payne, R.H.2
  • 5
    • 0037012468 scopus 로고    scopus 로고
    • Acetylcholinesterase knockouts establish central cholinergic pathway and can use butyrylcholinesterase to hydrolyze acetylcholine
    • Mesulam MM, Guillozet A, Shaw P, Levey A, Duysen EG Lockridge O (2003) Acetylcholinesterase knockouts establish central cholinergic pathway and can use butyrylcholinesterase to hydrolyze acetylcholine. Neuroscience 110, 627 639.
    • (2003) Neuroscience , vol.110 , pp. 627-639
    • Mesulam, M.M.1    Guillozet, A.2    Shaw, P.3    Levey, A.4    Duysen, E.G.5    Lockridge, O.6
  • 6
    • 0033568704 scopus 로고    scopus 로고
    • Structural roles of acetylcholinesterase variants in biology and pathology
    • Grisaru D, Sternfeld M, Eldor A, Glick D Soreq H (1999) Structural roles of acetylcholinesterase variants in biology and pathology. Eur J Biochem 264, 672 686.
    • (1999) Eur J Biochem , vol.264 , pp. 672-686
    • Grisaru, D.1    Sternfeld, M.2    Eldor, A.3    Glick, D.4    Soreq, H.5
  • 7
    • 0033956134 scopus 로고    scopus 로고
    • The key role of butyrylcholinesterase during neurogenesis and neural disorders: An antisense-5′-butyrylcholinesterase study
    • Mack A Robitzki A (2000) The key role of butyrylcholinesterase during neurogenesis and neural disorders: an antisense-5′-butyrylcholinesterase study. Prog Neurobiol 60, 607 628.
    • (2000) Prog Neurobiol , vol.60 , pp. 607-628
    • MacK, A.1    Robitzki, A.2
  • 8
    • 33845970588 scopus 로고    scopus 로고
    • Nonenzymatic functions of acetylcholinesterase splice variants in the developmental neurotoxicity of organophosphates: Chlorpyrifos, chlorpyrifos oxon, and diazinon
    • Jameson RR, Seidler FJ Slotkin TA (2007) Nonenzymatic functions of acetylcholinesterase splice variants in the developmental neurotoxicity of organophosphates: chlorpyrifos, chlorpyrifos oxon, and diazinon. Environ Health Perspect 115, 65 70.
    • (2007) Environ Health Perspect , vol.115 , pp. 65-70
    • Jameson, R.R.1    Seidler, F.J.2    Slotkin, T.A.3
  • 9
    • 0033607448 scopus 로고    scopus 로고
    • Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase
    • Munoz FJ, Aldunate R Inestrosa NC (1999) Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase. NeuroReport 10, 3621 3625.
    • (1999) NeuroReport , vol.10 , pp. 3621-3625
    • Munoz, F.J.1    Aldunate, R.2    Inestrosa, N.C.3
  • 10
    • 0037716469 scopus 로고    scopus 로고
    • Bioactivity of a peptide derived from acetylcholinesterase: Electrophysiological characterization in guinea-pig hippocampus
    • Bon CL Greenfield SA (2003) Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus. Eur J Neurosci 17, 1991 1995.
    • (2003) Eur J Neurosci , vol.17 , pp. 1991-1995
    • Bon, C.L.1    Greenfield, S.A.2
  • 11
    • 14344255818 scopus 로고    scopus 로고
    • Are there non-catalytic functions of acetylcholinesterases? Lessons from mutant animal models
    • Cousin X, Strähle U Chatonnet A (2005) Are there non-catalytic functions of acetylcholinesterases? Lessons from mutant animal models BioEssays 27, 189 200.
    • (2005) BioEssays , vol.27 , pp. 189-200
    • Cousin, X.1    Strähle, U.2    Chatonnet, A.3
  • 12
    • 0028079652 scopus 로고
    • Cholinesterases display genuine arylacylamidase activity but are totally devoid of intrinsic peptidase activities
    • Checler F, Grassi J Vincent J-P (1994) Cholinesterases display genuine arylacylamidase activity but are totally devoid of intrinsic peptidase activities. J Neurochem 62, 756 763.
    • (1994) J Neurochem , vol.62 , pp. 756-763
    • Checler, F.1    Grassi, J.2    Vincent, J.-P.3
  • 13
    • 0027435432 scopus 로고
    • Noncholinergic functions of cholinesterases
    • Balasubramanian AS Banumathy CD (1993) Noncholinergic functions of cholinesterases. FASEB J 7, 1354 1358.
    • (1993) FASEB J , vol.7 , pp. 1354-1358
    • Balasubramanian, A.S.1    Banumathy, C.D.2
  • 14
    • 16544387273 scopus 로고    scopus 로고
    • Aryl acylamidase activity on acetylcholinesterase is high during early chicken brain development
    • Boopathy R Layer PG (2004) Aryl acylamidase activity on acetylcholinesterase is high during early chicken brain development. Prot J 23, 325 333.
    • (2004) Prot J , vol.23 , pp. 325-333
    • Boopathy, R.1    Layer, P.G.2
  • 16
    • 24644469273 scopus 로고    scopus 로고
    • Toxicological implications of esterases - From molecular structures to functions
    • Satoh T (2005) Toxicological implications of esterases - from molecular structures to functions. Toxicol Appl Pharmacol 207, S11 S18.
    • (2005) Toxicol Appl Pharmacol , vol.207
    • Satoh, T.1
  • 17
    • 33645958909 scopus 로고    scopus 로고
    • Carboxylesterases - Detoxifying enzymes and targets for drug therapy
    • Potter PM Wadkins RM (2006) Carboxylesterases - detoxifying enzymes and targets for drug therapy. Curr Med Chem 13, 1045 1054.
    • (2006) Curr Med Chem , vol.13 , pp. 1045-1054
    • Potter, P.M.1    Wadkins, R.M.2
  • 18
    • 33745031316 scopus 로고    scopus 로고
    • Enzymes involved in the bioconversion of ester-based prodrugs
    • Liederer BM Borchardt RT (2006) Enzymes involved in the bioconversion of ester-based prodrugs. J Pharm Sci 95, 1177 1195.
    • (2006) J Pharm Sci , vol.95 , pp. 1177-1195
    • Liederer, B.M.1    Borchardt, R.T.2
  • 20
    • 0016540289 scopus 로고
    • The carboxylesterases/amidases of mammalian liver and their possible significance
    • Junge W Krisch K (1975) The carboxylesterases/amidases of mammalian liver and their possible significance. CRC Crit Rev Food Sci Nutr 3, 371 434.
    • (1975) CRC Crit Rev Food Sci Nutr , vol.3 , pp. 371-434
    • Junge, W.1    Krisch, K.2
  • 21
    • 0000191215 scopus 로고
    • Role of carboxylesterases in xenobiotic metabolism
    • Satoh T (1987) Role of carboxylesterases in xenobiotic metabolism. Rev Biochem Toxicol 8, 155 181.
    • (1987) Rev Biochem Toxicol , vol.8 , pp. 155-181
    • Satoh, T.1
  • 22
    • 0019768441 scopus 로고
    • The aryl acylamidases and their relationship to cholinesterases in human serum, erythrocyte and liver
    • George ST Balasubramanian AS (1981) The aryl acylamidases and their relationship to cholinesterases in human serum, erythrocyte and liver. Eur J Biochem 121, 177 186.
    • (1981) Eur J Biochem , vol.121 , pp. 177-186
    • George, S.T.1    Balasubramanian, A.S.2
  • 23
    • 0020346289 scopus 로고
    • Brain aryl acylamidase
    • Hsu LL (1982) Brain aryl acylamidase. Int J Biochem 14, 1037 1042.
    • (1982) Int J Biochem , vol.14 , pp. 1037-1042
    • Hsu, L.L.1
  • 24
    • 0026040248 scopus 로고
    • The nucleotide and deduced amino acid sequences of porcine liver proline-β-naphthylamidase. Evidence for identity with carboxylesterase
    • Matsushima M, Inoue H, Ichinose M, Tsukada S, Miki K, Kurokawa K, Takahashi T Takahashi K (1991) The nucleotide and deduced amino acid sequences of porcine liver proline-β-naphthylamidase. Evidence for identity with carboxylesterase. FEBS Lett 293, 37 41.
    • (1991) FEBS Lett , vol.293 , pp. 37-41
    • Matsushima, M.1    Inoue, H.2    Ichinose, M.3    Tsukada, S.4    Miki, K.5    Kurokawa, K.6    Takahashi, T.7    Takahashi, K.8
  • 25
    • 33746837711 scopus 로고    scopus 로고
    • Diisopropylfluorophosphate-sensitive aryl acylamidase activity of fatty acid free human serum albumin
    • Manoharan I Boopathy R (2006) Diisopropylfluorophosphate-sensitive aryl acylamidase activity of fatty acid free human serum albumin. Arch Biochem Biophys 452, 186 188.
    • (2006) Arch Biochem Biophys , vol.452 , pp. 186-188
    • Manoharan, I.1    Boopathy, R.2
  • 26
    • 34547814760 scopus 로고    scopus 로고
    • Aryl acylamidase activity of human serum albumin with o-nitrotrifluoroacetanilide as the substrate
    • Masson P, Froment M-T, Darvesh S, Schopfer LM Lockridge O (2007) Aryl acylamidase activity of human serum albumin with o-nitrotrifluoroacetanilide as the substrate. J Enz Inhib Med Chem 22, 463 469.
    • (2007) J Enz Inhib Med Chem , vol.22 , pp. 463-469
    • Masson, P.1    Froment, M.-T.2    Darvesh, S.3    Schopfer, L.M.4    Lockridge, O.5
  • 27
    • 0040630211 scopus 로고
    • Retinal melatonin is metabolized within the eye of Xenopus laevis
    • Cahill GM Besharse JC (1989) Retinal melatonin is metabolized within the eye of Xenopus laevis. Proc Natl Acad Sci USA 86, 1098 1102.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 1098-1102
    • Cahill, G.M.1    Besharse, J.C.2
  • 28
    • 4243148518 scopus 로고    scopus 로고
    • Organophosphate toxicology: Safety aspects of non acetylcholinesterase secondary targets
    • Cassida J Quistad GB (2004) Organophosphate toxicology: safety aspects of non acetylcholinesterase secondary targets. Chem Toxicol 17, 983 998.
    • (2004) Chem Toxicol , vol.17 , pp. 983-998
    • Cassida, J.1    Quistad, G.B.2
  • 29
    • 0142039868 scopus 로고    scopus 로고
    • Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
    • Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps J-C Nachon F (2003) Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem 278, 41141 41147.
    • (2003) J Biol Chem , vol.278 , pp. 41141-41147
    • Nicolet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.-C.4    Nachon, F.5
  • 30
    • 0021772470 scopus 로고
    • Chemical modification of acetylcholinesterase from eel and basal ganglia: Effect on the acetylcholinesterase and aryl acylamidase activities
    • Majundar R Balasubramanian AS (1984) Chemical modification of acetylcholinesterase from eel and basal ganglia: effect on the acetylcholinesterase and aryl acylamidase activities. Biochemistry 23, 4088 4093.
    • (1984) Biochemistry , vol.23 , pp. 4088-4093
    • Majundar, R.1    Balasubramanian, A.S.2
  • 31
    • 0022384920 scopus 로고
    • Chemical modification of the bifunctional pseudocholinesterase. Effect on the pseudocholinesterase and aryl acylamidase activities
    • Boopathy R Balasubramanian AS (1985) Chemical modification of the bifunctional pseudocholinesterase. Effect on the pseudocholinesterase and aryl acylamidase activities. Eur J Biochem 151, 351 360.
    • (1985) Eur J Biochem , vol.151 , pp. 351-360
    • Boopathy, R.1    Balasubramanian, A.S.2
  • 32
    • 0032524964 scopus 로고    scopus 로고
    • Inhibition of cholinesterase-associated aryl acylamidase activity by anticholinesterase agents: Focus on drugs potentially effective in Alzheimer's disease
    • Costagli C Galli A (1998) Inhibition of cholinesterase-associated aryl acylamidase activity by anticholinesterase agents: focus on drugs potentially effective in Alzheimer's disease. Biochem Pharmacol 55, 1733 1737.
    • (1998) Biochem Pharmacol , vol.55 , pp. 1733-1737
    • Costagli, C.1    Galli, A.2
  • 36
    • 0020595327 scopus 로고
    • Carboxylesterases in rat and human sera and their relationship to serum aryl acylamidases and cholinesterases
    • Tsujita T Okuda H (1983) Carboxylesterases in rat and human sera and their relationship to serum aryl acylamidases and cholinesterases. Eur J Biochem 133, 215 220.
    • (1983) Eur J Biochem , vol.133 , pp. 215-220
    • Tsujita, T.1    Okuda, H.2
  • 37
    • 0026528244 scopus 로고
    • Cholinesterases exhibiting aryl acylamidase activity in human amniotic fluid
    • Jayanthi LD, Balasubramanian N Balasubramanian AS (1992) Cholinesterases exhibiting aryl acylamidase activity in human amniotic fluid. Clin Chim Acta 205, 157 166.
    • (1992) Clin Chim Acta , vol.205 , pp. 157-166
    • Jayanthi, L.D.1    Balasubramanian, N.2    Balasubramanian, A.S.3
  • 38
    • 0032476123 scopus 로고    scopus 로고
    • Aryl acylamidase activity exhibited by butyrylcholinesterase is higher in chick than in horse, but much lower than in fetal calf serum
    • Weitnauer E, Robitzki A Layer PG (1998) Aryl acylamidase activity exhibited by butyrylcholinesterase is higher in chick than in horse, but much lower than in fetal calf serum. Neurosci Lett 254, 153 156.
    • (1998) Neurosci Lett , vol.254 , pp. 153-156
    • Weitnauer, E.1    Robitzki, A.2    Layer, P.G.3
  • 39
    • 0032216883 scopus 로고    scopus 로고
    • Serum butyrylcholinesterase of non-human primate shows amine sensitive aryl acyl amidase and metallopeptidase activities and characteristics similar to those of the human serum enzyme
    • Bhanumathy CD, Rao RV Balasubramanian AS (1998) Serum butyrylcholinesterase of non-human primate shows amine sensitive aryl acyl amidase and metallopeptidase activities and characteristics similar to those of the human serum enzyme. Indian J Biochem Biophys 35, 146 156.
    • (1998) Indian J Biochem Biophys , vol.35 , pp. 146-156
    • Bhanumathy, C.D.1    Rao, R.V.2    Balasubramanian, A.S.3
  • 40
    • 0037301587 scopus 로고    scopus 로고
    • Enantiomer affects of huperzine a on the aryl acylamidase activity of human cholinesterases
    • Darvesh S, Walsh R Martin E (2003) Enantiomer affects of huperzine A on the aryl acylamidase activity of human cholinesterases. Cell Mol Neurobiol 23, 93 100.
    • (2003) Cell Mol Neurobiol , vol.23 , pp. 93-100
    • Darvesh, S.1    Walsh, R.2    Martin, E.3
  • 42
    • 0034457136 scopus 로고    scopus 로고
    • Distinct effect of benzalkonium on the esterase and aryl acylamidase activities of butyrylcholinesterase
    • Jaganathan L Boopathy R (2000) Distinct effect of benzalkonium on the esterase and aryl acylamidase activities of butyrylcholinesterase. Bioorg Chem 28, 242 251.
    • (2000) Bioorg Chem , vol.28 , pp. 242-251
    • Jaganathan, L.1    Boopathy, R.2
  • 43
    • 0024371283 scopus 로고
    • Human cerebrospinal fluid acetylcholinesterase and butyrylcholinesterase. Evidence for identity between the serum and cerebrospinal fluid butyrylcholinesterase
    • Rao RV, Gnanamuthu C Balasubramanian AS (1989) Human cerebrospinal fluid acetylcholinesterase and butyrylcholinesterase. Evidence for identity between the serum and cerebrospinal fluid butyrylcholinesterase. Clin Chim Acta 183, 135 146.
    • (1989) Clin Chim Acta , vol.183 , pp. 135-146
    • Rao, R.V.1    Gnanamuthu, C.2    Balasubramanian, A.S.3
  • 44
    • 0031043533 scopus 로고    scopus 로고
    • Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase
    • Masson P, Legrand P, Bartels CF, Froment M-T, Schopfer LM Lockridge O (1997) Role of aspartate 70 and tryptophan 82 in binding of succinyldithiocholine to human butyrylcholinesterase. Biochemistry 36, 2266 2277.
    • (1997) Biochemistry , vol.36 , pp. 2266-2277
    • Masson, P.1    Legrand, P.2    Bartels, C.F.3    Froment, M.-T.4    Schopfer, L.M.5    Lockridge, O.6
  • 45
    • 0027273738 scopus 로고
    • Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant
    • Masson P, Adkins S, Gouet P Lockridge O (1993) Recombinant human butyrylcholinesterase G390V, the fluoride-2 variant, expressed in Chinese hamster ovary cells, is a low affinity variant. J Biol Chem 268, 14329 14341.
    • (1993) J Biol Chem , vol.268 , pp. 14329-14341
    • Masson, P.1    Adkins, S.2    Gouet, P.3    Lockridge, O.4
  • 46
    • 0029058743 scopus 로고
    • Substrate dependence of amiloride- and soman-induced conformation changes of butyrylcholinesterase as evidenced by high-pressure perturbation
    • Cléry C, Heiber-Langer I, Channac L, David L, Balny C Masson P (1995) Substrate dependence of amiloride- and soman-induced conformation changes of butyrylcholinesterase as evidenced by high-pressure perturbation. Biochim Biophys Acta 1250, 19 28.
    • (1995) Biochim Biophys Acta , vol.1250 , pp. 19-28
    • Cléry, C.1    Heiber-Langer, I.2    Channac, L.3    David, L.4    Balny, C.5    Masson, P.6
  • 47
    • 0036182499 scopus 로고    scopus 로고
    • Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion
    • Stojan J, Golicnik G, Froment M-T, Estour F Masson P (2002) Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion. Eur J Biochem 269, 1154 1161.
    • (2002) Eur J Biochem , vol.269 , pp. 1154-1161
    • Stojan, J.1    Golicnik, G.2    Froment, M.-T.3    Estour, F.4    Masson, P.5
  • 48
    • 34247869688 scopus 로고    scopus 로고
    • Multi-site inhibition of human plasma cholinesterase by cationic phenoxazine and phenothiazine dyes
    • Kucukkilinc T Ozer I (2007) Multi-site inhibition of human plasma cholinesterase by cationic phenoxazine and phenothiazine dyes. Arch Biochem Biophys 461, 294 298.
    • (2007) Arch Biochem Biophys , vol.461 , pp. 294-298
    • Kucukkilinc, T.1    Ozer, I.2
  • 49
    • 0029665127 scopus 로고    scopus 로고
    • Asp70 in the peripheral anionic site of human butyrylcholinesterase
    • Masson P, Froment M-T, Bartels C Lockridge O (1996) Asp70 in the peripheral anionic site of human butyrylcholinesterase. Eur J Biochem 235, 36 48.
    • (1996) Eur J Biochem , vol.235 , pp. 36-48
    • Masson, P.1    Froment, M.-T.2    Bartels, C.3    Lockridge, O.4
  • 50
    • 0025642471 scopus 로고
    • Ligand exclusion on acetylcholinesterase
    • Berman HA Leonard K (1990) Ligand exclusion on acetylcholinesterase. Biochemistry 29, 10640 10649.
    • (1990) Biochemistry , vol.29 , pp. 10640-10649
    • Berman, H.A.1    Leonard, K.2
  • 51
    • 0003518480 scopus 로고
    • J. Wiley & Sons, New York, NY, pp. reprinted in 1993, Wiley Classic Library Edition, ISBN 0-471-30309-7).
    • Segel IH (1975) Enzyme kinetics. J. Wiley & Sons, New York, NY, pp. 161 272 (reprinted in 1993, Wiley Classic Library Edition, ISBN 0-471-30309-7).
    • (1975) Enzyme Kinetics. , pp. 161-272
    • Segel, I.H.1
  • 52
    • 0032774638 scopus 로고    scopus 로고
    • Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates
    • Masson P, Xie W, Froment M-T, Levitsky V, Fortier P-L, Albaret C Lockridge O (1999) Interaction between the peripheral site residues of human butyrylcholinesterase, D70 and Y332, in binding and hydrolysis of substrates. Biochim Biophys Acta 1433, 281 293.
    • (1999) Biochim Biophys Acta , vol.1433 , pp. 281-293
    • Masson, P.1    Xie, W.2    Froment, M.-T.3    Levitsky, V.4    Fortier, P.-L.5    Albaret, C.6    Lockridge, O.7
  • 53
    • 0035847069 scopus 로고    scopus 로고
    • Effects of mutations of active site residues and amino acids interacting with the Ω loop on substrate activation of butyrylcholinesterase
    • Masson P, Xie W, Froment M-T Lockridge O (2001) Effects of mutations of active site residues and amino acids interacting with the Ω loop on substrate activation of butyrylcholinesterase. Biochim Biophys Acta 1544, 166 176.
    • (2001) Biochim Biophys Acta , vol.1544 , pp. 166-176
    • Masson, P.1    Xie, W.2    Froment, M.-T.3    Lockridge, O.4
  • 54
    • 1942520265 scopus 로고    scopus 로고
    • Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate
    • Stojan J, Brochier L, Alies C, Colletier JP Fournier D (2004) Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate. Eur J Biochem 271, 1364 1371.
    • (2004) Eur J Biochem , vol.271 , pp. 1364-1371
    • Stojan, J.1    Brochier, L.2    Alies, C.3    Colletier, J.P.4    Fournier, D.5
  • 56
    • 0030780763 scopus 로고    scopus 로고
    • Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase
    • Saxena A, Redman AMG, Jiang X, Lockridge O Doctor BP (1997) Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase. Biochemistry, 36, 14642 14651.
    • (1997) Biochemistry , vol.36 , pp. 14642-14651
    • Saxena, A.1    Redman, A.M.G.2    Jiang, X.3    Lockridge, O.4    Doctor, B.P.5
  • 57
    • 0037162748 scopus 로고    scopus 로고
    • Theory supplemented by experiment. Electronic effects on the rotational stability of the amide group in p-substituted acetanilides
    • Ilieva S, Hadjieva B Galabov B (2002) Theory supplemented by experiment. Electronic effects on the rotational stability of the amide group in p-substituted acetanilides. J Org Chem 67, 6210 6215.
    • (2002) J Org Chem , vol.67 , pp. 6210-6215
    • Ilieva, S.1    Hadjieva, B.2    Galabov, B.3
  • 58
  • 59
  • 60
    • 1542533734 scopus 로고    scopus 로고
    • Is aromaticity essential for trapping the catalytic histidine 447 in human acetylcholinesterase?
    • Kaplan D, Barak D, Ordentlich A, Kronman C, Velan B Shafferman A (2004) Is aromaticity essential for trapping the catalytic histidine 447 in human acetylcholinesterase? Biochemistry 43, 3129 3136.
    • (2004) Biochemistry , vol.43 , pp. 3129-3136
    • Kaplan, D.1    Barak, D.2    Ordentlich, A.3    Kronman, C.4    Velan, B.5    Shafferman, A.6
  • 61
    • 34247550159 scopus 로고    scopus 로고
    • Crystal structures of acetylcholinesterase in complex with organophosphorus compounds suggest that the acyl pocket modulates the aging reaction by precluding the formation of the trigonal bipyramidal transition state
    • Hörnberg H, Tunemalm AK Ekström F (2007) Crystal structures of acetylcholinesterase in complex with organophosphorus compounds suggest that the acyl pocket modulates the aging reaction by precluding the formation of the trigonal bipyramidal transition state. Biochemistry 46, 4815 4825.
    • (2007) Biochemistry , vol.46 , pp. 4815-4825
    • Hörnberg, H.1    Tunemalm, A.K.2    Ekström, F.3
  • 62
    • 0033789253 scopus 로고    scopus 로고
    • High plasma serotonin concentration levels in primary pulmonary hypertension: Effect of long-term epoprostenol (prostacyclin) therapy
    • Kereveur A, Callebert J, Humbert M, Herve P, Simonneau G, Launay JM Drouet L (2000) High plasma serotonin concentration levels in primary pulmonary hypertension: effect of long-term epoprostenol (prostacyclin) therapy. Arterioscler Thromb Vasc Biol 20, 2233 2239.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 2233-2239
    • Kereveur, A.1    Callebert, J.2    Humbert, M.3    Herve, P.4    Simonneau, G.5    Launay, J.M.6    Drouet, L.7
  • 65
    • 27544478172 scopus 로고    scopus 로고
    • Butyrylcholinesterase, paraoxonase, and albumin esterase but not carboxylesterase, are present in human plasma
    • Li B, Sedlacek M, Manoharam I, Boopathy R, Duysen EG, Masson P Lockridge O (2005) Butyrylcholinesterase, paraoxonase, and albumin esterase but not carboxylesterase, are present in human plasma. Biochem Pharmacol 70, 1673 1684.
    • (2005) Biochem Pharmacol , vol.70 , pp. 1673-1684
    • Li, B.1    Sedlacek, M.2    Manoharam, I.3    Boopathy, R.4    Duysen, E.G.5    Masson, P.6    Lockridge, O.7
  • 66
    • 33748744628 scopus 로고    scopus 로고
    • Structure, function and regulation of carboxylesterases
    • Satoh T Hosokawa M (2006) Structure, function and regulation of carboxylesterases. Chem-Biol Interact 162, 195 211.
    • (2006) Chem-Biol Interact , vol.162 , pp. 195-211
    • Satoh, T.1    Hosokawa, M.2
  • 67
    • 27544478065 scopus 로고    scopus 로고
    • 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
    • doi:.
    • Lockridge O, Schopfer LM, Winger G Woods JH (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 Chem Biol Radiol Def 3, doi :.
    • (2005) J Med Chem Biol Radiol Def , vol.3
    • Lockridge, O.1    Schopfer, L.M.2    Winger, G.3    Woods, J.H.4
  • 68
    • 3142543643 scopus 로고    scopus 로고
    • A direct method to visualise the arylacylamidase activity on cholinesterases in polyacrylamide gels
    • doi:.
    • Jaganathan L Boopathy R (2000) A direct method to visualise the arylacylamidase activity on cholinesterases in polyacrylamide gels. BMC Biochem doi :.
    • (2000) BMC Biochem
    • Jaganathan, L.1    Boopathy, R.2
  • 69
    • 0038219567 scopus 로고    scopus 로고
    • Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate
    • Johnson JL, Cusack B, Davies MP, Fauq A Rosenberry TL (2003) Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate. Biochemistry 42, 5438 5452.
    • (2003) Biochemistry , vol.42 , pp. 5438-5452
    • Johnson, J.L.1    Cusack, B.2    Davies, M.P.3    Fauq, A.4    Rosenberry, T.L.5
  • 70
    • 33845388436 scopus 로고    scopus 로고
    • N-acetylanthranilate amidase from Arthrobacter nitroguajacolicus Rü61a, an α/β-hydrolase-fold protein active towards aryl-acylamides and esters, and properties of its cysteine-deficient variant
    • Kolkenbrock S, Parschat K, Beermann B, Hinz HJ Fetzner S (2006) N-acetylanthranilate amidase from Arthrobacter nitroguajacolicus Rü61a, an α/β-hydrolase-fold protein active towards aryl-acylamides and esters, and properties of its cysteine-deficient variant. J Bacteriol 188, 8430 8440.
    • (2006) J Bacteriol , vol.188 , pp. 8430-8440
    • Kolkenbrock, S.1    Parschat, K.2    Beermann, B.3    Hinz, H.J.4    Fetzner, S.5
  • 71
    • 0015247334 scopus 로고
    • Nitroacetanilides as chromogenic substrate for assaying de-acetylating activity: The isolation and partial purification of aryl acylamidases from erepsin and tulip
    • Hoagland RE Graf G (1971) Nitroacetanilides as chromogenic substrate for assaying de-acetylating activity: the isolation and partial purification of aryl acylamidases from erepsin and tulip. Enzymologia 41, 313 319.
    • (1971) Enzymologia , vol.41 , pp. 313-319
    • Hoagland, R.E.1    Graf, G.2
  • 73
    • 0031713093 scopus 로고    scopus 로고
    • Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon
    • Amitai G, Moorad D, Adani R Doctor BP (1998) Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon. Biochem Pharmacol 56, 293 299.
    • (1998) Biochem Pharmacol , vol.56 , pp. 293-299
    • Amitai, G.1    Moorad, D.2    Adani, R.3    Doctor, B.P.4
  • 74
    • 0015972948 scopus 로고
    • A graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden A (1974) A graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem J 137, 143 144.
    • (1974) Biochem J , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.