메뉴 건너뛰기




Volumn 276, Issue 7, 2009, Pages 2074-2083

Hydrolysis of acetylthiocoline, o-nitroacetanilide and o- nitrotrifluoroacetanilide by fetal bovine serum acetylcholinesterase

Author keywords

Aryl acylamidase; Chemical denaturation; Cholinesterases; Kinetic parameters; Molecular forms

Indexed keywords

2 NITROACETANILIDE; 2 NITROTRIFLUOROACETANILIDE; ACETANILIDE DERIVATIVE; ACETYLCHOLINESTERASE; ACETYLTHIOCOLINE; AMIDASE; ESTERASE; FASCICULIN; GUANIDINE; UNCLASSIFIED DRUG;

EID: 62149086948     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.06942.x     Document Type: Article
Times cited : (17)

References (42)
  • 1
    • 0019768441 scopus 로고
    • The aryl acylamidase and their relationship to cholinesterase in human serum, erythrocyte and liver
    • George ST Balasubramanian AS (1981) The aryl acylamidase and their relationship to cholinesterase 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
  • 2
    • 0027435432 scopus 로고
    • Noncholinergic functions of cholinesterases
    • Balasubramanian AS Bhanumathy CD (1993) Noncholinergic functions of cholinesterases. FASEB J 7, 1354 1358.
    • (1993) FASEB J , vol.7 , pp. 1354-1358
    • Balasubramanian, A.S.1    Bhanumathy, C.D.2
  • 3
    • 42649137543 scopus 로고    scopus 로고
    • Kinetic analysis of effector modulation of butyrylcholinesterase- catalysed hydrolysis of acetanilides and homologous esters
    • Masson P, Froment MT, Gillon E, Nachon F, Lockridge O Schopfer LM (2008) Kinetic analysis of effector modulation of butyrylcholinesterase-catalysed hydrolysis of acetanilides and homologous esters. FEBS J 275, 2617 2631.
    • (2008) FEBS J , vol.275 , pp. 2617-2631
    • Masson, P.1    Froment, M.T.2    Gillon, E.3    Nachon, F.4    Lockridge, O.5    Schopfer, L.M.6
  • 4
    • 28744450290 scopus 로고    scopus 로고
    • Expression of acetylcholinesterase (AChE) and aryl acylamidase (AAA) during early zebrafish embryogenesis
    • Allebrandt KV, Rajesh V, Andermann P Layer PG (2005) Expression of acetylcholinesterase (AChE) and aryl acylamidase (AAA) during early zebrafish embryogenesis. Chem Biol Interact 157-158, 353 355.
    • (2005) Chem Biol Interact , vol.157-158 , pp. 353-355
    • Allebrandt, K.V.1    Rajesh, V.2    Andermann, P.3    Layer, P.G.4
  • 5
    • 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. Protein J 23, 325 333.
    • (2004) Protein J , vol.23 , pp. 325-333
    • Boopathy, R.1    Layer, P.G.2
  • 6
    • 0027475810 scopus 로고
    • Protease inhibitors and indoleamines selectively inhibit cholinesterases in the histopathologic structures of Alzheimer's disease
    • Wright CI, Geula C Mesulam MM (1993) Protease inhibitors and indoleamines selectively inhibit cholinesterases in the histopathologic structures of Alzheimer's disease. Proc Natl Acad Sci USA 90, 683 686.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 683-686
    • Wright, C.I.1    Geula, C.2    Mesulam, M.M.3
  • 7
    • 0036560908 scopus 로고    scopus 로고
    • The origin of the molecular diversity and functional anchoring of cholinesterases
    • Massoulié J (2002) The origin of the molecular diversity and functional anchoring of cholinesterases. Neurosignals 11, 130 143.
    • (2002) Neurosignals , vol.11 , pp. 130-143
    • Massoulié, J.1
  • 11
    • 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 JC 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
  • 13
    • 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
  • 14
    • 33947684265 scopus 로고    scopus 로고
    • Human serum cholinesterase from liver pathological samples exhibit highly elevated aryl acylamidase activity
    • Boopathy R, Rajesh RV, Darvesh S Layer PG (2007) Human serum cholinesterase from liver pathological samples exhibit highly elevated aryl acylamidase activity. Clin Chim Acta 380, 151 156.
    • (2007) Clin Chim Acta , vol.380 , pp. 151-156
    • Boopathy, R.1    Rajesh, R.V.2    Darvesh, S.3    Layer, P.G.4
  • 15
    • 0016790041 scopus 로고
    • Acetylcholinesterase-catalyzed hydrolysis of an amide
    • Moore DH Hess GP (1975) Acetylcholinesterase-catalyzed hydrolysis of an amide. Biochemistry 14, 2386 2389.
    • (1975) Biochemistry , vol.14 , pp. 2386-2389
    • Moore, D.H.1    Hess, G.P.2
  • 16
    • 0018749692 scopus 로고
    • The association of the serotonin-sensitive aryl acylamidase with acetylcholinesterase in the monkey brain
    • Oommen A Balasubramanian AS (1979) The association of the serotonin-sensitive aryl acylamidase with acetylcholinesterase in the monkey brain. Eur J Biochem 94, 135 143.
    • (1979) Eur J Biochem , vol.94 , pp. 135-143
    • Oommen, A.1    Balasubramanian, A.S.2
  • 18
    • 0016311626 scopus 로고
    • A simple method for purification of acetylcholinesterase from human erythrocyte membranes
    • Sihotang K (1974) A simple method for purification of acetylcholinesterase from human erythrocyte membranes. Biochim Biophys Acta 370, 468 476.
    • (1974) Biochim Biophys Acta , vol.370 , pp. 468-476
    • Sihotang, K.1
  • 19
    • 0017089228 scopus 로고
    • Affinity chromatography of acetylcholinesterase. the importance of hydrophobic interations
    • Massoulié J Bon S (1976) Affinity chromatography of acetylcholinesterase. The importance of hydrophobic interations. Eur J Biochem 68, 531 539.
    • (1976) Eur J Biochem , vol.68 , pp. 531-539
    • Massoulié, J.1    Bon, S.2
  • 21
    • 0026011253 scopus 로고
    • Species specificity in the chemical mechanisms of organophosphorous anticholinesterase activity
    • Wallace KB Kemp JR (1991) Species specificity in the chemical mechanisms of organophosphorous anticholinesterase activity. Chem Res Toxicol 4, 41 49.
    • (1991) Chem Res Toxicol , vol.4 , pp. 41-49
    • Wallace, K.B.1    Kemp, J.R.2
  • 22
    • 0021355165 scopus 로고
    • Interactions with lectins indicate differences in the carbohydrate composition of the membrane-bound enzymes acetylcholinesterase and 5′-nucleotidase in different cell types
    • Meflah K, Bernard S Massoulie J (1984) Interactions with lectins indicate differences in the carbohydrate composition of the membrane-bound enzymes acetylcholinesterase and 5′-nucleotidase in different cell types. Biochimie 66, 59 69.
    • (1984) Biochimie , vol.66 , pp. 59-69
    • Meflah, K.1    Bernard, S.2    Massoulie, J.3
  • 23
    • 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 1777.
    • (1998) Biochem Pharmacol , vol.55 , pp. 1733-1777
    • Costagli, C.1    Galli, A.2
  • 24
    • 0037413712 scopus 로고    scopus 로고
    • Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
    • Bourne Y, Taylor P, Radic Z Marchot P (2003) Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 22, 1 12.
    • (2003) EMBO J , vol.22 , pp. 1-12
    • Bourne, Y.1    Taylor, P.2    Radic, Z.3    Marchot, P.4
  • 25
    • 0033524414 scopus 로고    scopus 로고
    • Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect
    • Szegletes T, Mallender WD, Thomas PJ Rosenberry TL (1999) Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 38, 122 133.
    • (1999) Biochemistry , vol.38 , pp. 122-133
    • Szegletes, T.1    Mallender, W.D.2    Thomas, P.J.3    Rosenberry, T.L.4
  • 27
    • 0028116312 scopus 로고
    • Fasciculin inhibition of acetylcholinesterase is prevented by chemical modification of the enzyme at the peripheral site
    • Durán R, Cerveñansky C, Dajas F Tipton KF (1994) Fasciculin inhibition of acetylcholinesterase is prevented by chemical modification of the enzyme at the peripheral site. Biochim Biophys Acta 1201, 381 388.
    • (1994) Biochim Biophys Acta , vol.1201 , pp. 381-388
    • Durán, R.1    Cerveñansky, C.2    Dajas, F.3    Tipton, K.F.4
  • 28
    • 29444441881 scopus 로고    scopus 로고
    • Modeling effects of oxyanion hole on the ester hydrolysis catalyzed by human cholinesterases
    • Gao D Zhan CG (2005) Modeling effects of oxyanion hole on the ester hydrolysis catalyzed by human cholinesterases. J Phys Chem B 109, 23070 23076.
    • (2005) J Phys Chem B , vol.109 , pp. 23070-23076
    • Gao, D.1    Zhan, C.G.2
  • 31
    • 0030050221 scopus 로고    scopus 로고
    • Interaction of partially unfolded forms of Torpedo acetylcholinesterase with liposomes
    • Shin I, Silman I Weiner LM (1996) Interaction of partially unfolded forms of Torpedo acetylcholinesterase with liposomes. Protein Sci 5, 42 51.
    • (1996) Protein Sci , vol.5 , pp. 42-51
    • Shin, I.1    Silman, I.2    Weiner, L.M.3
  • 32
    • 2942720656 scopus 로고    scopus 로고
    • Nanosecond dynamics of acetylcholinesterase near the active center gorge
    • Boyd AE, Dunlop CS, Wong L, Radic Z, Taylor P Johnson DA (2004) Nanosecond dynamics of acetylcholinesterase near the active center gorge. J Biol Chem 279, 26612 26618.
    • (2004) J Biol Chem , vol.279 , pp. 26612-26618
    • Boyd, A.E.1    Dunlop, C.S.2    Wong, L.3    Radic, Z.4    Taylor, P.5    Johnson, D.A.6
  • 33
    • 0032741498 scopus 로고    scopus 로고
    • Conformational flexibility of the acetylcholinesterase tetramer suggested by X-ray crystallography
    • Bourne Y, Grassi J, Bougis PE Marchot P (1999) Conformational flexibility of the acetylcholinesterase tetramer suggested by X-ray crystallography. J Biol Chem 274, 30370 30376.
    • (1999) J Biol Chem , vol.274 , pp. 30370-30376
    • Bourne, Y.1    Grassi, J.2    Bougis, P.E.3    Marchot, P.4
  • 34
    • 0141523253 scopus 로고    scopus 로고
    • Stabilization of a metastable state of Torpedo californica acetylcholinesterase by chemical chaperones
    • Millard CB, Shnyrov VL, Newstead S, Shin I, Roth E, Silman I Weiner L (2003) Stabilization of a metastable state of Torpedo californica acetylcholinesterase by chemical chaperones. Protein Sci 12, 2337 2347.
    • (2003) Protein Sci , vol.12 , pp. 2337-2347
    • Millard, C.B.1    Shnyrov, V.L.2    Newstead, S.3    Shin, I.4    Roth, E.5    Silman, I.6    Weiner, L.7
  • 36
    • 0030833450 scopus 로고    scopus 로고
    • Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2dy mouse muscle
    • Cabezas-Herrera J, Moral-Naranjo MT, Campoy FJ Vidal CJ (1997) Glycosylation of acetylcholinesterase forms in microsomal membranes from normal and dystrophic Lama2dy mouse muscle. J Neurochem 69, 1964 1974.
    • (1997) J Neurochem , vol.69 , pp. 1964-1974
    • Cabezas-Herrera, J.1    Moral-Naranjo, M.T.2    Campoy, F.J.3    Vidal, C.J.4
  • 37
    • 0032838527 scopus 로고    scopus 로고
    • Increased butyrylcholinesterase levels in microsomal membranes of dystrophic Lama2dy mouse muscle
    • Moral-Naranjo MT, Campoy FJ, Cabezas-Herrera J Vidal CJ (1999) Increased butyrylcholinesterase levels in microsomal membranes of dystrophic Lama2dy mouse muscle. J Neurochem 73, 1138 1144.
    • (1999) J Neurochem , vol.73 , pp. 1138-1144
    • Moral-Naranjo, M.T.1    Campoy, F.J.2    Cabezas-Herrera, J.3    Vidal, C.J.4
  • 38
    • 27544478172 scopus 로고    scopus 로고
    • Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
    • Li B, Sedlacek M, Manoharan 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    Manoharan, I.3    Boopathy, R.4    Duysen, E.G.5    Masson, P.6    Lockridge, O.7
  • 39
    • 34547814760 scopus 로고    scopus 로고
    • Aryl acylamidase activity of human serum albumin with o-nitrotrifluoroacetanilide as the substrate
    • Masson P, Froment MT, Darvesh S, Schopfer LM Lockridge O (2007) Aryl acylamidase activity of human serum albumin with o-nitrotrifluoroacetanilide as the substrate. J Enzyme Inhib Med Chem 22, 463 469.
    • (2007) J Enzyme 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
  • 42
    • 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 MT, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.