메뉴 건너뛰기




Volumn 49, Issue 29, 2010, Pages 6219-6227

Redesign of cosubstrate specificity and identification of important residues for substrate binding to hChAT

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL TRANSFERASE; ACETYL-COA; ACTIVE SITE; ACYL-COA; ACYLTRANSFERASES; CARNITINE; CO-SUBSTRATE; PALMITOYLTRANSFERASE; REVERSIBLE FORMATION; SUBSTRATE BINDING; WILD TYPES;

EID: 77954832316     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1007996     Document Type: Article
Times cited : (11)

References (46)
  • 1
    • 0031667995 scopus 로고    scopus 로고
    • The cholinergic deficit in Alzheimers disease
    • Whitehouse, P. J. (1998) The cholinergic deficit in Alzheimers disease J. Clin. Psychiatry 59 (Suppl. 13) 19-22
    • (1998) J. Clin. Psychiatry , vol.59 , Issue.SUPPL. 13 , pp. 19-22
    • Whitehouse, P.J.1
  • 2
    • 0033452570 scopus 로고    scopus 로고
    • Choline acetyltransferase: The structure, distribution and pathologic changes in the central nervous system
    • Oda, Y. (1999) Choline acetyltransferase: The structure, distribution and pathologic changes in the central nervous system Pathol. Int. 49, 921-937
    • (1999) Pathol. Int. , vol.49 , pp. 921-937
    • Oda, Y.1
  • 3
    • 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
    • 55849096212 scopus 로고    scopus 로고
    • The fate of the large striatal interneurons expressing calretinin in Huntingtons disease
    • Massouh, M., Wallman, M. J., Pourcher, E., and Parent, A. (2008) The fate of the large striatal interneurons expressing calretinin in Huntingtons disease Neurosci. Res. 62, 216-224
    • (2008) Neurosci. Res. , vol.62 , pp. 216-224
    • Massouh, M.1    Wallman, M.J.2    Pourcher, E.3    Parent, A.4
  • 5
    • 0033042102 scopus 로고    scopus 로고
    • Reduction in choline acetyltransferase immunoreactivity but not muscarinic-m2 receptor immunoreactivity in the brainstem of SIDS infants
    • Mallard, C., Tolcos, M., Leditschke, J., Campbell, P., and Rees, S. (1999) Reduction in choline acetyltransferase immunoreactivity but not muscarinic-m2 receptor immunoreactivity in the brainstem of SIDS infants J. Neuropathol. Exp. Neurol. 58, 255-264
    • (1999) J. Neuropathol. Exp. Neurol. , vol.58 , pp. 255-264
    • Mallard, C.1    Tolcos, M.2    Leditschke, J.3    Campbell, P.4    Rees, S.5
  • 6
    • 0038182387 scopus 로고    scopus 로고
    • Rett Syndrome: An update
    • Jellinger, K. A. (2003) Rett Syndrome: An update J. Neural Transm. 110, 681-701
    • (2003) J. Neural Transm. , vol.110 , pp. 681-701
    • Jellinger, K.A.1
  • 7
    • 10644256309 scopus 로고    scopus 로고
    • Structure and function of carnitine acyltransferases
    • Jogl, G., Hsiao, Y. S., and Tong, L. (2004) Structure and function of carnitine acyltransferases Ann. N.Y. Acad. Sci. 1033, 17-29
    • (2004) Ann. N.Y. Acad. Sci. , vol.1033 , pp. 17-29
    • Jogl, G.1    Hsiao, Y.S.2    Tong, L.3
  • 8
    • 0029044160 scopus 로고
    • Carnitine, carnitine acetyltransferase, and glutathione in Alzheimer brain
    • Makar, T. K., Cooper, A. J., Tofel-Grehl, B., Thaler, H. T., and Blass, J. P. (1995) Carnitine, carnitine acetyltransferase, and glutathione in Alzheimer brain Neurochem. Res. 20, 705-711
    • (1995) Neurochem. Res. , vol.20 , pp. 705-711
    • Makar, T.K.1    Cooper, A.J.2    Tofel-Grehl, B.3    Thaler, H.T.4    Blass, J.P.5
  • 10
    • 0018637435 scopus 로고
    • Fatal ataxic encephalopathy and carnitine acetyltransferase deficiency: A functional defect of pyruvate oxidation?
    • DiDonato, S., Rimoldi, M., Moise, A., Bertagnoglio, B., and Uziel, G. (1979) Fatal ataxic encephalopathy and carnitine acetyltransferase deficiency: A functional defect of pyruvate oxidation? Neurology 29, 1578-1583
    • (1979) Neurology , vol.29 , pp. 1578-1583
    • Didonato, S.1    Rimoldi, M.2    Moise, A.3    Bertagnoglio, B.4    Uziel, G.5
  • 11
    • 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
  • 13
    • 33845448089 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism of human choline acetyltransferase
    • Kim, A. R., Rylett, R. J., and Shilton, B. H. (2006) Substrate binding and catalytic mechanism of human choline acetyltransferase Biochemistry 45, 14621-14631
    • (2006) Biochemistry , vol.45 , pp. 14621-14631
    • Kim, A.R.1    Rylett, R.J.2    Shilton, B.H.3
  • 14
    • 0038128249 scopus 로고    scopus 로고
    • Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer
    • Wu, D., Govindasamy, L., Lian, W., Gu, Y., Kukar, T., Agbandje-McKenna, M., and McKenna, R. (2003) Structure of human carnitine acetyltransferase. Molecular basis for fatty acyl transfer J. Biol. Chem. 278, 13159-13165
    • (2003) J. Biol. Chem. , vol.278 , pp. 13159-13165
    • Wu, D.1    Govindasamy, L.2    Lian, W.3    Gu, Y.4    Kukar, T.5    Agbandje-Mckenna, M.6    McKenna, R.7
  • 15
    • 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
  • 16
    • 12844251898 scopus 로고    scopus 로고
    • Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity
    • Jogl, G., Hsiao, Y. S., and Tong, L. (2005) Crystal structure of mouse carnitine octanoyltransferase and molecular determinants of substrate selectivity J. Biol. Chem. 280, 738-744
    • (2005) J. Biol. Chem. , vol.280 , pp. 738-744
    • Jogl, G.1    Hsiao, Y.S.2    Tong, L.3
  • 17
    • 3843062433 scopus 로고    scopus 로고
    • Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase
    • Hsiao, Y. S., Jogl, G., and Tong, L. (2004) Structural and biochemical studies of the substrate selectivity of carnitine acetyltransferase J. Biol. Chem. 279, 31584-31589
    • (2004) J. Biol. Chem. , vol.279 , pp. 31584-31589
    • Hsiao, Y.S.1    Jogl, G.2    Tong, L.3
  • 18
    • 33745198879 scopus 로고    scopus 로고
    • Crystal structure of rat carnitine palmitoyltransferase II (CPT-II)
    • Hsiao, Y. S., Jogl, G., Esser, V., and Tong, L. (2006) Crystal structure of rat carnitine palmitoyltransferase II (CPT-II) Biochem. Biophys. Res. Commun. 346, 974-980
    • (2006) Biochem. Biophys. Res. Commun. , vol.346 , pp. 974-980
    • Hsiao, Y.S.1    Jogl, G.2    Esser, V.3    Tong, L.4
  • 19
    • 0028304469 scopus 로고
    • Catalytically important domains of rat carnitine palmitoyltransferase II as determined by site-directed mutagenesis and chemical modification. Evidence for a critical histidine residue
    • Brown, N. F., Anderson, R. C., Caplan, S. L., Foster, D. W., and McGarry, J. D. (1994) Catalytically important domains of rat carnitine palmitoyltransferase II as determined by site-directed mutagenesis and chemical modification. Evidence for a critical histidine residue J. Biol. Chem. 269, 19157-19162
    • (1994) J. Biol. Chem. , vol.269 , pp. 19157-19162
    • Brown, N.F.1    Anderson, R.C.2    Caplan, S.L.3    Foster, D.W.4    McGarry, J.D.5
  • 20
    • 0033985092 scopus 로고    scopus 로고
    • Identification of the two histidine residues responsible for the inhibition by malonyl-CoA in peroxisomal carnitine octanoyltransferase from rat liver
    • Morillas, M., Clotet, J., Rubi, B., Serra, D., Asins, G., Arino, J., and Hegardt, F. G. (2000) Identification of the two histidine residues responsible for the inhibition by malonyl-CoA in peroxisomal carnitine octanoyltransferase from rat liver FEBS Lett. 466, 183-186
    • (2000) FEBS Lett. , vol.466 , pp. 183-186
    • Morillas, M.1    Clotet, J.2    Rubi, B.3    Serra, D.4    Asins, G.5    Arino, J.6    Hegardt, F.G.7
  • 21
    • 0035976911 scopus 로고    scopus 로고
    • Structural model of the catalytic core of carnitine palmitoyltransferase i and carnitine octanoyltransferase (COT): Mutation of CPT i histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity
    • Morillas, M., Gomez-Puertas, P., Roca, R., Serra, D., Asins, G., Valencia, A., and Hegardt, F. G. (2001) Structural model of the catalytic core of carnitine palmitoyltransferase I and carnitine octanoyltransferase (COT): Mutation of CPT I histidine 473 and alanine 381 and COT alanine 238 impairs the catalytic activity J. Biol. Chem. 276, 45001-45008
    • (2001) J. Biol. Chem. , vol.276 , pp. 45001-45008
    • Morillas, M.1    Gomez-Puertas, P.2    Roca, R.3    Serra, D.4    Asins, G.5    Valencia, A.6    Hegardt, F.G.7
  • 22
  • 24
    • 33646592906 scopus 로고    scopus 로고
    • Mutagenesis of specific amino acids converts carnitine acetyltransferase into carnitine palmitoyltransferase
    • Cordente, A. G., Lopez-Vinas, E., Vazquez, M. I., Gomez-Puertas, P., Asins, G., Serra, D., and Hegardt, F. G. (2006) Mutagenesis of specific amino acids converts carnitine acetyltransferase into carnitine palmitoyltransferase Biochemistry 45, 6133-6141
    • (2006) Biochemistry , vol.45 , pp. 6133-6141
    • Cordente, A.G.1    Lopez-Vinas, E.2    Vazquez, M.I.3    Gomez-Puertas, P.4    Asins, G.5    Serra, D.6    Hegardt, F.G.7
  • 25
    • 0032544596 scopus 로고    scopus 로고
    • Redesign of choline acetyltransferase specificity by protein engineering
    • Cronin, C. N. (1998) Redesign of choline acetyltransferase specificity by protein engineering J. Biol. Chem. 273, 24465-24469
    • (1998) J. Biol. Chem. , vol.273 , pp. 24465-24469
    • Cronin, C.N.1
  • 26
    • 70349405978 scopus 로고    scopus 로고
    • HChAT: A tool for the chemoenzymatic generation of potential acetyl/butyrylcholinesterase inhibitors
    • Green, K. D., Fridman, M., and Garneau-Tsodikova, S. (2009) hChAT: A tool for the chemoenzymatic generation of potential acetyl/butyrylcholinesterase inhibitors ChemBioChem 10, 2191-2194
    • (2009) ChemBioChem , vol.10 , pp. 2191-2194
    • Green, K.D.1    Fridman, M.2    Garneau-Tsodikova, S.3
  • 27
    • 44349172245 scopus 로고    scopus 로고
    • Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase
    • Biswas, T. and Tsodikov, O. V. (2008) Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase FEBS J. 275, 3064-3071
    • (2008) FEBS J. , vol.275 , pp. 3064-3071
    • Biswas, T.1    Tsodikov, O.V.2
  • 28
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77, 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 29
    • 28944432885 scopus 로고    scopus 로고
    • The kinetic mechanism of AAC3-IV aminoglycoside acetyltransferase from Escherichia coli
    • Magalhaes, M. L. and Blanchard, J. S. (2005) The kinetic mechanism of AAC3-IV aminoglycoside acetyltransferase from Escherichia coli Biochemistry 44, 16275-16283
    • (2005) Biochemistry , vol.44 , pp. 16275-16283
    • Magalhaes, M.L.1    Blanchard, J.S.2
  • 30
    • 34447545711 scopus 로고    scopus 로고
    • Chemoenzymatic formation of novel aminocoumarin antibiotics by the enzymes CouN1 and CouN7
    • Fridman, M., Balibar, C. J., Lupoli, T., Kahne, D., Walsh, C. T., and Garneau-Tsodikova, S. (2007) Chemoenzymatic formation of novel aminocoumarin antibiotics by the enzymes CouN1 and CouN7 Biochemistry 46, 8462-8471
    • (2007) Biochemistry , vol.46 , pp. 8462-8471
    • Fridman, M.1    Balibar, C.J.2    Lupoli, T.3    Kahne, D.4    Walsh, C.T.5    Garneau-Tsodikova, S.6
  • 31
    • 9744235772 scopus 로고    scopus 로고
    • Assembly of dimeric variants of coumermycins by tandem action of the four biosynthetic enzymes CouL, CouM, CouP, and NovN
    • Freel Meyers, C. L., Oberthur, M., Heide, L., Kahne, D., and Walsh, C. T. (2004) Assembly of dimeric variants of coumermycins by tandem action of the four biosynthetic enzymes CouL, CouM, CouP, and NovN Biochemistry 43, 15022-15036
    • (2004) Biochemistry , vol.43 , pp. 15022-15036
    • Freel Meyers, C.L.1    Oberthur, M.2    Heide, L.3    Kahne, D.4    Walsh, C.T.5
  • 32
    • 67349244074 scopus 로고    scopus 로고
    • Increasing structure diversity of prenylated diketopiperazine derivatives by using a 4-dimethylallyltryptophan synthase
    • Steffan, N. and Li, S. M. (2009) Increasing structure diversity of prenylated diketopiperazine derivatives by using a 4-dimethylallyltryptophan synthase Arch. Microbiol. 191, 461-466
    • (2009) Arch. Microbiol. , vol.191 , pp. 461-466
    • Steffan, N.1    Li, S.M.2
  • 33
    • 72749089599 scopus 로고    scopus 로고
    • Characterization of cyclo-acetoacetyl- l -tryptophan dimethylallyltransferase in cyclopiazonic acid biosynthesis: Substrate promiscuity and site directed mutagenesis studies
    • Liu, X. and Walsh, C. T. (2009) Characterization of cyclo-acetoacetyl- l -tryptophan dimethylallyltransferase in cyclopiazonic acid biosynthesis: Substrate promiscuity and site directed mutagenesis studies Biochemistry 48, 11032-11044
    • (2009) Biochemistry , vol.48 , pp. 11032-11044
    • Liu, X.1    Walsh, C.T.2
  • 34
    • 77952899716 scopus 로고    scopus 로고
    • Transglucosidases as efficient tools for oligosaccharide and glucoconjugate synthesis
    • Monsan, P., Remaud-Simeon, M., and Andre, I. (2010) Transglucosidases as efficient tools for oligosaccharide and glucoconjugate synthesis Curr. Opin. Microbiol. 13, 293-300
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 293-300
    • Monsan, P.1    Remaud-Simeon, M.2    Andre, I.3
  • 35
    • 75649101296 scopus 로고    scopus 로고
    • Exploring the substrate promiscuity of drug-modifying enzymes for the chemoenzymatic generation of N-acylated aminoglycosides
    • Green, K. D., Chen, W., Houghton, J. L., Fridman, M., and Garneau-Tsodikova, S. (2010) Exploring the substrate promiscuity of drug-modifying enzymes for the chemoenzymatic generation of N-acylated aminoglycosides ChemBioChem 11, 119-126
    • (2010) ChemBioChem , vol.11 , pp. 119-126
    • Green, K.D.1    Chen, W.2    Houghton, J.L.3    Fridman, M.4    Garneau-Tsodikova, S.5
  • 37
    • 0035031853 scopus 로고    scopus 로고
    • Mechanistic studies on the alkyltransferase activity of serotonin N-acetyltransferase
    • Zheng, W., Scheibner, K. A., Ho, A. K., and Cole, P. A. (2001) Mechanistic studies on the alkyltransferase activity of serotonin N-acetyltransferase Chem. Biol. 8, 379-389
    • (2001) Chem. Biol. , vol.8 , pp. 379-389
    • Zheng, W.1    Scheibner, K.A.2    Ho, A.K.3    Cole, P.A.4
  • 38
    • 70349906430 scopus 로고    scopus 로고
    • Revealing substrate promiscuity of 1-deoxy- d -xylulose 5-phosphate synthase
    • Brammer, L. A. and Meyers, C. F. (2009) Revealing substrate promiscuity of 1-deoxy- d -xylulose 5-phosphate synthase Org. Lett. 11, 4748-4751
    • (2009) Org. Lett. , vol.11 , pp. 4748-4751
    • Brammer, L.A.1    Meyers, C.F.2
  • 39
    • 64249150641 scopus 로고    scopus 로고
    • Chapter 12. The power of glycosyltransferases to generate bioactive natural compounds
    • Harle, J. and Bechthold, A. (2009) Chapter 12. The power of glycosyltransferases to generate bioactive natural compounds Methods Enzymol. 458, 309-333
    • (2009) Methods Enzymol. , vol.458 , pp. 309-333
    • Harle, J.1    Bechthold, A.2
  • 40
    • 41949101106 scopus 로고    scopus 로고
    • Optimizing glycosyltransferase specificity via hot spot saturation mutagenesis presents a catalyst for novobiocin glycorandomization
    • Williams, G. J., Goff, R. D., Zhang, C., and Thorson, J. S. (2008) Optimizing glycosyltransferase specificity via hot spot saturation mutagenesis presents a catalyst for novobiocin glycorandomization Chem. Biol. 15, 393-401
    • (2008) Chem. Biol. , vol.15 , pp. 393-401
    • Williams, G.J.1    Goff, R.D.2    Zhang, C.3    Thorson, J.S.4
  • 42
    • 58049214870 scopus 로고    scopus 로고
    • Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation
    • Faridmoayer, A., Fentabil, M. A., Haurat, M. F., Yi, W., Woodward, R., Wang, P. G., and Feldman, M. F. (2008) Extreme substrate promiscuity of the Neisseria oligosaccharyl transferase involved in protein O-glycosylation J. Biol. Chem. 283, 34596-34604
    • (2008) J. Biol. Chem. , vol.283 , pp. 34596-34604
    • Faridmoayer, A.1    Fentabil, M.A.2    Haurat, M.F.3    Yi, W.4    Woodward, R.5    Wang, P.G.6    Feldman, M.F.7
  • 43
    • 23044507077 scopus 로고    scopus 로고
    • A systematic investigation of the synthetic utility of glycopeptide glycosyltransferases
    • Oberthur, M., Leimkuhler, C., Kruger, R. G., Lu, W., Walsh, C. T., and Kahne, D. (2005) A systematic investigation of the synthetic utility of glycopeptide glycosyltransferases J. Am. Chem. Soc. 127, 10747-10752
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 10747-10752
    • Oberthur, M.1    Leimkuhler, C.2    Kruger, R.G.3    Lu, W.4    Walsh, C.T.5    Kahne, D.6
  • 44
    • 34548685673 scopus 로고    scopus 로고
    • Expanding the promiscuity of a natural-product glycosyltransferase by directed evolution
    • Williams, G. J., Zhang, C., and Thorson, J. S. (2007) Expanding the promiscuity of a natural-product glycosyltransferase by directed evolution Nat. Chem. Biol. 3, 657-662
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 657-662
    • Williams, G.J.1    Zhang, C.2    Thorson, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.