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Volumn 45, Issue 49, 2006, Pages 14621-14631

Substrate binding and catalytic mechanism of human choline acetyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CHEMICAL MODIFICATION; NEUROLOGY; SUBSTRATES;

EID: 33845448089     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061536l     Document Type: Article
Times cited : (42)

References (54)
  • 1
    • 0031667995 scopus 로고    scopus 로고
    • The cholinergic deficit in Alzheimer's disease
    • Whitehouse, P. J. (1998) The cholinergic deficit in Alzheimer's disease, J. Clin. Psychiatry 59, 19-22.
    • (1998) J. Clin. Psychiatry , vol.59 , pp. 19-22
    • Whitehouse, P.J.1
  • 2
    • 24044528136 scopus 로고    scopus 로고
    • Reduced density of cholinergic interneurons in the ventral striatum in schizophrenia: An in situ hybridization study
    • Holt, D. J., Bachus, S. E., Hyde, T. M., Wittie, M., Herman, M. M., Vangel, M., Saper, C. B., and Kleinman, J. E. (2005) Reduced density of cholinergic interneurons in the ventral striatum in schizophrenia: an in situ hybridization study, Biol. Psychiatry 58, 408-416.
    • (2005) Biol. Psychiatry , vol.58 , pp. 408-416
    • Holt, D.J.1    Bachus, S.E.2    Hyde, T.M.3    Wittie, M.4    Herman, M.M.5    Vangel, M.6    Saper, C.B.7    Kleinman, J.E.8
  • 4
    • 0037470612 scopus 로고    scopus 로고
    • The lymphocytic cholinergic system and its biological function
    • Kawashima, K., and Fujii, T. (2003) The lymphocytic cholinergic system and its biological function, Life Sci. 72, 2101-2109.
    • (2003) Life Sci. , vol.72 , pp. 2101-2109
    • Kawashima, K.1    Fujii, T.2
  • 5
    • 0018144532 scopus 로고
    • Effect of salts on the physical and kinetic properties of human placental choline acetyltransferase
    • Hersh, L. B., and Peet, M. (1978) Effect of salts on the physical and kinetic properties of human placental choline acetyltransferase, J. Neurochem. 30, 1087-1093.
    • (1978) J. Neurochem. , vol.30 , pp. 1087-1093
    • Hersh, L.B.1    Peet, M.2
  • 6
    • 0037827772 scopus 로고    scopus 로고
    • Identification of a novel nuclear localization signal common to 69- and 82-kDa human choline acetyltransferase
    • Gill, S. K., Bhattacharya, M., Ferguson, S. S., and Rylett, R. J. (2003) Identification of a novel nuclear localization signal common to 69- and 82-kDa human choline acetyltransferase, J. Biol. Chem. 278, 20217-20224.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20217-20224
    • Gill, S.K.1    Bhattacharya, M.2    Ferguson, S.S.3    Rylett, R.J.4
  • 7
    • 0033516560 scopus 로고    scopus 로고
    • Nuclear localization of the 82-kDa form of human choline acetyltransferase
    • Resendes, M. C., Dobransky, T., Ferguson, S. S., and Rylett, R. J. (1999) Nuclear localization of the 82-kDa form of human choline acetyltransferase, J. Biol. Chem. 274, 19417-19421.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19417-19421
    • Resendes, M.C.1    Dobransky, T.2    Ferguson, S.S.3    Rylett, R.J.4
  • 8
    • 26444559465 scopus 로고    scopus 로고
    • Exposure of nuclear antigens in formalin-fixed, paraffin-embedded necropsy human spinal cord tissue: Detection of NeuN
    • Gill, S. K., Ishak, M., and Rylett, R. J. (2005) Exposure of nuclear antigens in formalin-fixed, paraffin-embedded necropsy human spinal cord tissue: detection of NeuN, J. Neurosci. Methods 148, 26-35.
    • (2005) J. Neurosci. Methods , vol.148 , pp. 26-35
    • Gill, S.K.1    Ishak, M.2    Rylett, R.J.3
  • 9
    • 0029861246 scopus 로고    scopus 로고
    • Active transport of acetylcholine by the human vesicular acetylcholine transporter
    • Varoqui, H., and Erickson, J. D. (1996) Active transport of acetylcholine by the human vesicular acetylcholine transporter, J. Biol. Chem. 271, 27229-27232.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27229-27232
    • Varoqui, H.1    Erickson, J.D.2
  • 10
    • 0019513449 scopus 로고
    • Choline uptake and acetylcholine synthesis in synaptosomes: Investigations using two different labeled variants of choline
    • Weiler, M. H., Gundersen, C. B., and Jenden, D. J. (1981) Choline uptake and acetylcholine synthesis in synaptosomes: investigations using two different labeled variants of choline, J. Neurochem. 36, 1802-1812.
    • (1981) J. Neurochem. , vol.36 , pp. 1802-1812
    • Weiler, M.H.1    Gundersen, C.B.2    Jenden, D.J.3
  • 11
    • 0034004554 scopus 로고    scopus 로고
    • Identification and characterization of the high-affinity choline transporter
    • Okuda, T., Haga, T., Kanai, Y., Endou, H., Ishihara, T., and Katsura, I. (2000) Identification and characterization of the high-affinity choline transporter, Nat. Neurosci. 3, 120-125.
    • (2000) Nat. Neurosci. , vol.3 , pp. 120-125
    • Okuda, T.1    Haga, T.2    Kanai, Y.3    Endou, H.4    Ishihara, T.5    Katsura, I.6
  • 12
    • 0037375478 scopus 로고    scopus 로고
    • Cytosolic choline acetyltransferase binds specifically to cholinergic plasma membrane of rat brain synaptosomes to generate membrane-bound enzyme
    • Gabrielle, P., Jeana, M., and Lorenza, E. C. (2003) Cytosolic choline acetyltransferase binds specifically to cholinergic plasma membrane of rat brain synaptosomes to generate membrane-bound enzyme, Neurochem. Res. 28, 543-549.
    • (2003) Neurochem. Res. , vol.28 , pp. 543-549
    • Gabrielle, P.1    Jeana, M.2    Lorenza, E.C.3
  • 13
    • 2542528467 scopus 로고    scopus 로고
    • Ultrastructural localization of high-affinity choline transporter in the rat neuromuscular junction: Enrichment on synaptic vesicles
    • Nakata, K., Okuda, T., and Misawa, H. (2004) Ultrastructural localization of high-affinity choline transporter in the rat neuromuscular junction: enrichment on synaptic vesicles, Synapse 53, 53-56.
    • (2004) Synapse , vol.53 , pp. 53-56
    • Nakata, K.1    Okuda, T.2    Misawa, H.3
  • 14
    • 26844474356 scopus 로고    scopus 로고
    • A model for dynamic regulation of choline acetyltransferase by phosphorylation
    • Dobransky, T., and Rylett, R. J. (2005) A model for dynamic regulation of choline acetyltransferase by phosphorylation, J. Neurochem. 95, 305-313.
    • (2005) J. Neurochem. , vol.95 , pp. 305-313
    • Dobransky, T.1    Rylett, R.J.2
  • 15
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures, J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 16
    • 0017647567 scopus 로고
    • Re-evaluation of the kinetic mechanism of the choline acetyltransferase reaction
    • Hersh, L. B., and Peet, M. (1977) Re-evaluation of the kinetic mechanism of the choline acetyltransferase reaction, J. Biol. Chem. 252, 4796-4802.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4796-4802
    • Hersh, L.B.1    Peet, M.2
  • 17
    • 0027156457 scopus 로고
    • Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis
    • Carbini, L. A., and Hersh, L. B. (1993) Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis, J. Neurochem. 61, 247-253.
    • (1993) J. Neurochem. , vol.61 , pp. 247-253
    • Carbini, L.A.1    Hersh, L.B.2
  • 18
    • 0018620004 scopus 로고
    • The reaction of choline acetyltransferase with sulfhydryl reagents. Methoxycarbonyl-CoA disulfide as an active site-directed reagent
    • Hersh, L. B., Nair, R. V., and Smith, D. J. (1979) The reaction of choline acetyltransferase with sulfhydryl reagents. Methoxycarbonyl-CoA disulfide as an active site-directed reagent, J. Biol. Chem. 254, 11988-11992.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11988-11992
    • Hersh, L.B.1    Nair, R.V.2    Smith, D.J.3
  • 19
    • 0025021434 scopus 로고
    • Kinetic and inactivation studies of recombinant Drosophila choline acetyltransferase
    • Carbini, L., Rodriguez, G., and Hersh, L. B. (1990) Kinetic and inactivation studies of recombinant Drosophila choline acetyltransferase, Brain Res. Bull. 24, 119-124.
    • (1990) Brain Res. Bull. , vol.24 , pp. 119-124
    • Carbini, L.1    Rodriguez, G.2    Hersh, L.B.3
  • 20
    • 0028883982 scopus 로고
    • Identification of an active site arginine in rat choline acetyltransferase by alanine scanning mutagenesis
    • Wu, D., and Hersh, L. B. (1995) Identification of an active site arginine in rat choline acetyltransferase by alanine scanning mutagenesis, J. Biol. Chem. 270, 29111-29116.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29111-29116
    • Wu, D.1    Hersh, L.B.2
  • 21
    • 0018340608 scopus 로고
    • The lack of specificity towards salts in the activation of choline acetyltransferase from human placenta
    • Hersh, L. B. (1979) The lack of specificity towards salts in the activation of choline acetyltransferase from human placenta, J. Neurochem. 32, 991-996.
    • (1979) J. Neurochem. , vol.32 , pp. 991-996
    • Hersh, L.B.1
  • 22
    • 0017871623 scopus 로고
    • Effect of sodium chloride on changing the rate-limiting step in the human placental choline acetyltransferase reaction
    • Hersh, L. B., Barker, L. A., and Rush, B. (1978) Effect of sodium chloride on changing the rate-limiting step in the human placental choline acetyltransferase reaction, J. Biol. Chem. 253, 4966-4970.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4966-4970
    • Hersh, L.B.1    Barker, L.A.2    Rush, B.3
  • 23
    • 2942597469 scopus 로고    scopus 로고
    • Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders
    • Cai, Y., Cronin, C. N., Engel, A. G., Ohno, K., Hersh, L. B., and Rodgers, D. W. (2004) Choline acetyltransferase structure reveals distribution of mutations that cause motor disorders, EMBO J. 23, 2047-2058.
    • (2004) EMBO J. , vol.23 , pp. 2047-2058
    • Cai, Y.1    Cronin, C.N.2    Engel, A.G.3    Ohno, K.4    Hersh, L.B.5    Rodgers, D.W.6
  • 25
    • 32944458303 scopus 로고    scopus 로고
    • Surface-entropy reduction used in the crystallization of human choline acetyltransferase
    • Kim, A. R., Dobransky, T., Rylett, R. J., and Shilton, B. H. (2005) Surface-entropy reduction used in the crystallization of human choline acetyltransferase, Acta Crystallogr., Sect. D 61, 1306-1310.
    • (2005) Acta Crystallogr., Sect. D , vol.61 , pp. 1306-1310
    • Kim, A.R.1    Dobransky, T.2    Rylett, R.J.3    Shilton, B.H.4
  • 26
    • 0037428082 scopus 로고    scopus 로고
    • Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport
    • Jogl, G., and Tong, L. (2003) Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport, Cell 112, 113-122.
    • (2003) Cell , vol.112 , pp. 113-122
    • Jogl, G.1    Tong, L.2
  • 27
    • 13844254069 scopus 로고    scopus 로고
    • Two methods for large-scale purification of recombinant human choline acetyltransferase
    • Kim, A. R., Doherty-Kirby, A., Lajoie, G., Rylett, R. J., and Shilton, B. H. (2005) Two methods for large-scale purification of recombinant human choline acetyltransferase, Protein Expression Purif. 40, 107-117.
    • (2005) Protein Expression Purif. , vol.40 , pp. 107-117
    • Kim, A.R.1    Doherty-Kirby, A.2    Lajoie, G.3    Rylett, R.J.4    Shilton, B.H.5
  • 28
    • 0016415191 scopus 로고
    • Comparative studies of substrates and inhibitors of choline transport and choline acetyltransferase
    • Barker, L. A., and Mittag, T. W. (1975) Comparative studies of substrates and inhibitors of choline transport and choline acetyltransferase, J. Pharmacol. Exp. Ther. 192, 86-94.
    • (1975) J. Pharmacol. Exp. Ther. , vol.192 , pp. 86-94
    • Barker, L.A.1    Mittag, T.W.2
  • 29
    • 0019363880 scopus 로고
    • Acetylation of choline and homocholine by membrane-bound choline-O-acetyltransferase in mouse forebrain nerve endings
    • Benishin, C. G., and Carroll, P. T. (1981) Acetylation of choline and homocholine by membrane-bound choline-O-acetyltransferase in mouse forebrain nerve endings, J. Neurochem. 36, 732-740.
    • (1981) J. Neurochem. , vol.36 , pp. 732-740
    • Benishin, C.G.1    Carroll, P.T.2
  • 30
    • 0021289358 scopus 로고
    • Pharmacological actions of some cyclic analogues of choline
    • Hemsworth, B. A., Shreeve, S. M., and Veitch, G. B. (1984) Pharmacological actions of some cyclic analogues of choline, Br. J. Pharmacol. 81, 685-692.
    • (1984) Br. J. Pharmacol. , vol.81 , pp. 685-692
    • Hemsworth, B.A.1    Shreeve, S.M.2    Veitch, G.B.3
  • 31
    • 0021162086 scopus 로고
    • Uptake, metabolism, and releasability of ethyl analogues of homocholine by rat brain
    • Welner, S. A., and Collier, B. (1984) Uptake, metabolism, and releasability of ethyl analogues of homocholine by rat brain, J. Neurochem. 43, 1143-1151.
    • (1984) J. Neurochem. , vol.43 , pp. 1143-1151
    • Welner, S.A.1    Collier, B.2
  • 32
    • 0021239055 scopus 로고
    • Acetylation of some novel hemicholinium compounds by soluble choline acetyltransferase: Structure-activity relationships
    • Shreeve, S. M., Veitch, G. B., and Hemsworth, B. A. (1984) Acetylation of some novel hemicholinium compounds by soluble choline acetyltransferase: structure-activity relationships, J. Med. Chem. 27, 754-757.
    • (1984) J. Med. Chem. , vol.27 , pp. 754-757
    • Shreeve, S.M.1    Veitch, G.B.2    Hemsworth, B.A.3
  • 33
    • 0037880480 scopus 로고    scopus 로고
    • Close pairs of carboxylates: A possibility of multicenter hydrogen bonds in proteins
    • Torshin, I. Y., Harrison, R. W., and Weber, I. T. (2003) Close pairs of carboxylates: a possibility of multicenter hydrogen bonds in proteins, Protein Eng. 16, 201-207.
    • (2003) Protein Eng. , vol.16 , pp. 201-207
    • Torshin, I.Y.1    Harrison, R.W.2    Weber, I.T.3
  • 34
    • 0028972337 scopus 로고
    • Strange bedfellows: Interactions between acidic side-chains in proteins
    • Flocco, M. M., and Mowbray, S. L. (1995) Strange bedfellows: interactions between acidic side-chains in proteins, J. Mol. Biol. 254, 96-105.
    • (1995) J. Mol. Biol. , vol.254 , pp. 96-105
    • Flocco, M.M.1    Mowbray, S.L.2
  • 35
    • 0016291686 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution
    • Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J., and Steigemann, W. (1974) Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution, J. Mol. Biol. 89, 73-101.
    • (1974) J. Mol. Biol. , vol.89 , pp. 73-101
    • Huber, R.1    Kukla, D.2    Bode, W.3    Schwager, P.4    Bartels, K.5    Deisenhofer, J.6    Steigemann, W.7
  • 36
    • 0007715651 scopus 로고
    • Structure of chloramphenicol acetyltransferase at 1.75-A resolution
    • Leslie, A. G., Moody, P. C., and Shaw, W. V. (1988) Structure of chloramphenicol acetyltransferase at 1.75-A resolution, Proc. Natl. Acad. Sci. U.S.A. 85, 4133-4137.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 4133-4137
    • Leslie, A.G.1    Moody, P.C.2    Shaw, W.V.3
  • 37
    • 0027285476 scopus 로고
    • Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p)
    • Mattevi, A., Obmolova, G., Kalk, K. H., Teplyakov, A., and Hol, W. G. (1993) Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p), Biochemistry 32, 3887-3901.
    • (1993) Biochemistry , vol.32 , pp. 3887-3901
    • Mattevi, A.1    Obmolova, G.2    Kalk, K.H.3    Teplyakov, A.4    Hol, W.G.5
  • 39
    • 0032777703 scopus 로고    scopus 로고
    • Carnitine acyltransferases: Functional significance of subcellular distribution and membrane topology
    • Zammit, V. A. (1999) Carnitine acyltransferases: functional significance of subcellular distribution and membrane topology, Prog. Lipid Res. 38, 199-224.
    • (1999) Prog. Lipid Res. , vol.38 , pp. 199-224
    • Zammit, V.A.1
  • 41
    • 0035933779 scopus 로고    scopus 로고
    • Functional characterization of phosphorylation of 69-kDa human choline acetyltransferase at serine 440 by protein kinase C
    • Dobransky, T., Davis, W. L., and Rylett, R. J. (2001) Functional characterization of phosphorylation of 69-kDa human choline acetyltransferase at serine 440 by protein kinase C, J. Biol. Chem. 276, 22244-22250.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22244-22250
    • Dobransky, T.1    Davis, W.L.2    Rylett, R.J.3
  • 42
    • 0034234806 scopus 로고    scopus 로고
    • Expression, purification and characterization of recombinant human choline acetyltransferase: Phosphorylation of the enzyme regulates catalytic activity
    • Dobransky, T., Davis, W. L., Xiao, G. H., and Rylett, R. J. (2000) Expression, purification and characterization of recombinant human choline acetyltransferase: phosphorylation of the enzyme regulates catalytic activity, Biochem. J. 349, 141-151.
    • (2000) Biochem. J. , vol.349 , pp. 141-151
    • Dobransky, T.1    Davis, W.L.2    Xiao, G.H.3    Rylett, R.J.4
  • 43
    • 0037458638 scopus 로고    scopus 로고
    • Phosphorylation of 69-kDa choline acetyltransferase at threonine 456 in response to amyloid-beta peptide 1-42
    • Dobransky, T., Brewer, D., Lajoie, G., and Rylett, R. J. (2003) Phosphorylation of 69-kDa choline acetyltransferase at threonine 456 in response to amyloid-beta peptide 1-42, J. Biol. Chem. 278, 5883-5893.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5883-5893
    • Dobransky, T.1    Brewer, D.2    Lajoie, G.3    Rylett, R.J.4
  • 44
    • 10644249760 scopus 로고    scopus 로고
    • Protein kinase-C isoforms differentially phosphorylate human choline acetyltransferase regulating its catalytic activity
    • Dobransky, T., Doherty-Kirby, A., Kim, A. R., Brewer, D., Lajoie, G., and Rylett, R. J. (2004) Protein kinase-C isoforms differentially phosphorylate human choline acetyltransferase regulating its catalytic activity, J. Biol. Chem. 279, 52059-52068.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52059-52068
    • Dobransky, T.1    Doherty-Kirby, A.2    Kim, A.R.3    Brewer, D.4    Lajoie, G.5    Rylett, R.J.6
  • 45
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • Derewenda, Z. S. (2004) Rational protein crystallization by mutational surface engineering, Structure 12, 529-535.
    • (2004) Structure , vol.12 , pp. 529-535
    • Derewenda, Z.S.1
  • 46
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 47
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994) AMoRe: an automated package for molecular replacement, Acta Crystallogr. Sect. A 50, 157-163.
    • (1994) Acta Crystallogr. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 50
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 52
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • Li, H., Robertson, A. D., and Jensen, J. H. (2005) Very fast empirical prediction and rationalization of protein pKa values, Proteins 61, 704-721.
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 53
    • 0027489966 scopus 로고
    • Regulation of expression of cholinergic neuronal phenotypic markers in neuroblastoma LA-N-2
    • Rylett, R. J., Goddard, S., and Lambros, A. (1993) Regulation of expression of cholinergic neuronal phenotypic markers in neuroblastoma LA-N-2, J. Neurochem. 61, 1388-1397.
    • (1993) J. Neurochem. , vol.61 , pp. 1388-1397
    • Rylett, R.J.1    Goddard, S.2    Lambros, A.3
  • 54
    • 0016468979 scopus 로고
    • A rapid radiochemical method for the determination of choline acetyltransferase
    • Fonnum, F. (1975) A rapid radiochemical method for the determination of choline acetyltransferase, J. Neurochem. 24, 407-409.
    • (1975) J. Neurochem. , vol.24 , pp. 407-409
    • Fonnum, F.1


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