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Volumn 44, Issue 33, 2005, Pages 11295-11306

Catalytic mechanism of hamster arylamine N-acetyltransferase 2

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLATION; AMINES; CARCINOGENS; DRUG DOSAGE; ISOTOPES; METABOLISM; PH EFFECTS; PHYSIOLOGY;

EID: 23944498571     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047564q     Document Type: Article
Times cited : (52)

References (39)
  • 1
    • 0028190698 scopus 로고
    • N-acetyltransferases, O-acetyltransferases, and N,O-acetyltransferases: Enzymology and bioactivation
    • Hanna, P. E. (1994) N-acetyltransferases, O-acetyltransferases, and N,O-acetyltransferases: Enzymology and bioactivation, Adv. Pharmacol. 27, 401-430.
    • (1994) Adv. Pharmacol. , vol.27 , pp. 401-430
    • Hanna, P.E.1
  • 2
    • 0030004042 scopus 로고    scopus 로고
    • Metabolic activation and detoxification of arylamines
    • Hanna, P. E. (1996) Metabolic activation and detoxification of arylamines, Curr. Med. Chem. 3, 195-210.
    • (1996) Curr. Med. Chem. , vol.3 , pp. 195-210
    • Hanna, P.E.1
  • 4
    • 0034037485 scopus 로고    scopus 로고
    • Update on consensus arylamine N-acetyltransferase gene nomenclature
    • Hein, D. W., Grant, D. M., and Sim, E. (2000) Update on consensus arylamine N-acetyltransferase gene nomenclature, Pharmacogenetics 10, 291-292.
    • (2000) Pharmacogenetics , vol.10 , pp. 291-292
    • Hein, D.W.1    Grant, D.M.2    Sim, E.3
  • 5
    • 0025967717 scopus 로고
    • Monomorphic and polymorphic human arylamine N-acetyltransferases: A comparison of liver isozymes and expressed products of two cloned genes
    • Grant, D. M., Blum, M., Beer, M., and Meyer, U. A. (1991) Monomorphic and polymorphic human arylamine N-acetyltransferases: A comparison of liver isozymes and expressed products of two cloned genes, Mol. Pharmacol. 39, 184-191.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 184-191
    • Grant, D.M.1    Blum, M.2    Beer, M.3    Meyer, U.A.4
  • 7
    • 0035282779 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferases of mice, men, and microorganisms
    • Upton, A., Johnson, N., Sandy, J., and Sim, E. (2001) Arylamine N-acetyltransferases of mice, men, and microorganisms, Trends Pharmacol. Sci. 22, 140-146.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 140-146
    • Upton, A.1    Johnson, N.2    Sandy, J.3    Sim, E.4
  • 8
    • 0025237412 scopus 로고
    • Cloning and expression of cDNAs for polymorphic and monomorphic arylamine N-acetyltransferases from human liver
    • Ohsako, S., and Deguchi, T. (1990) Cloning and expression of cDNAs for polymorphic and monomorphic arylamine N-acetyltransferases from human liver, J. Biol. Chem. 265, 4630-4634.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4630-4634
    • Ohsako, S.1    Deguchi, T.2
  • 9
    • 0031742343 scopus 로고    scopus 로고
    • Immunochemical detection of arylamine N-acetyltransferase during mouse embryonic development and in adult mouse brain
    • Stanley, L. A., Copp, A. J., Pope, J., Rolls, S., Smelt, V., Perry, V. H., and Sim, E. (1998) Immunochemical detection of arylamine N-acetyltransferase during mouse embryonic development and in adult mouse brain, Teratology 58, 174-182.
    • (1998) Teratology , vol.58 , pp. 174-182
    • Stanley, L.A.1    Copp, A.J.2    Pope, J.3    Rolls, S.4    Smelt, V.5    Perry, V.H.6    Sim, E.7
  • 11
    • 0022600724 scopus 로고
    • Acetyltransferase in humans: Development and tissue distribution
    • Pacifici, G. M., Bencini, C., and Rane, A. (1986) Acetyltransferase in humans: Development and tissue distribution, Pharmacology 32, 283-291.
    • (1986) Pharmacology , vol.32 , pp. 283-291
    • Pacifici, G.M.1    Bencini, C.2    Rane, A.3
  • 13
    • 0037928462 scopus 로고    scopus 로고
    • Arylamine N-acetyltransferases: A pharmacogenomic approach to drug metabolism and endogenous function
    • Sim, E., Pinter, K., Mushtaq, A., Upton, A., Sandy, J., Bhakta, S., and Noble, M. (2003) Arylamine N-acetyltransferases: A pharmacogenomic approach to drug metabolism and endogenous function, Biochem. Soc. Trans. 31, 615-619.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 615-619
    • Sim, E.1    Pinter, K.2    Mushtaq, A.3    Upton, A.4    Sandy, J.5    Bhakta, S.6    Noble, M.7
  • 15
    • 0028904406 scopus 로고
    • Acetylation of N-aminobenzoylglutamate, a folic acid catabolite, by recombinant human arylamine N-acetyltransferase and U937 cells
    • Minchin, R. F. (1995) Acetylation of N-aminobenzoylglutamate, a folic acid catabolite, by recombinant human arylamine N-acetyltransferase and U937 cells, Biochem. J. 307 (part 1), 1-3.
    • (1995) Biochem. J. , vol.307 , Issue.PART 1 , pp. 1-3
    • Minchin, R.F.1
  • 16
    • 0026496458 scopus 로고
    • The quantitative analysis of endogenous folate catabolites in human urine
    • McPartlin, J., Courtney, G., McNulty, H., Weir, D., and Scott, J. (1992) The quantitative analysis of endogenous folate catabolites in human urine, Anal. Biochem. 206, 256-261.
    • (1992) Anal. Biochem. , vol.206 , pp. 256-261
    • McPartlin, J.1    Courtney, G.2    McNulty, H.3    Weir, D.4    Scott, J.5
  • 18
    • 0029033697 scopus 로고
    • Molecular mechanisms of polymorphism in acetylating enzymes for arylamines and N-hydroxyarylamines in hamster liver
    • Kato, R., and Yamazoe, Y. (1995) Molecular mechanisms of polymorphism in acetylating enzymes for arylamines and N-hydroxyarylamines in hamster liver, Drug Metab. Rev. 27, 241-256.
    • (1995) Drug Metab. Rev. , vol.27 , pp. 241-256
    • Kato, R.1    Yamazoe, Y.2
  • 20
    • 3042513718 scopus 로고    scopus 로고
    • Probing the mechanism of hamster arylamine N-acetyltransferase 2 acetylation by active site modification, site-directed mutagenesis, and pre-steady state and steady-state kinetic studies
    • Wang, H., Vath, G. M., Gleason, K. J., Hanna, P. E., and Wagner, C. R. (2004) Probing the mechanism of hamster arylamine N-acetyltransferase 2 acetylation by active site modification, site-directed mutagenesis, and pre-steady state and steady-state kinetic studies, Biochemistry 43, 8234-8246.
    • (2004) Biochemistry , vol.43 , pp. 8234-8246
    • Wang, H.1    Vath, G.M.2    Gleason, K.J.3    Hanna, P.E.4    Wagner, C.R.5
  • 21
    • 0033938882 scopus 로고    scopus 로고
    • Structure of arylamine N-acetyltransferase reveals a catalytic triad
    • Sinclair, J. C., Sandy, J., Delgoda, R., Sim, E., and Noble, M. E. (2000) Structure of arylamine N-acetyltransferase reveals a catalytic triad, Nat. Struct. Biol. 7, 560-564.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 560-564
    • Sinclair, J.C.1    Sandy, J.2    Delgoda, R.3    Sim, E.4    Noble, M.E.5
  • 22
    • 0036085411 scopus 로고    scopus 로고
    • 3D model of human arylamine N-acetyltransferase 2: Structural basis of the slow acetylator phenotype of the R64Q variant and analysis of the active-site loop
    • Rodrigues-Lima, F., and Dupret, J. M. (2002) 3D model of human arylamine N-acetyltransferase 2: Structural basis of the slow acetylator phenotype of the R64Q variant and analysis of the active-site loop, Biochem. Biophys. Res. Commun. 291, 116-123.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , pp. 116-123
    • Rodrigues-Lima, F.1    Dupret, J.M.2
  • 23
    • 0035365879 scopus 로고    scopus 로고
    • Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: Evidence for the conservation of a cysteine protease catalytic domain and an active-site loop
    • Rodrigues-Lima, F., Delomenie, C., Goodfellow, G. H., Grant, D. M., and Dupret, J. M. (2001) Homology modelling and structural analysis of human arylamine N-acetyltransferase NAT1: Evidence for the conservation of a cysteine protease catalytic domain and an active-site loop, Biochem. J. 356, 327-334.
    • (2001) Biochem. J. , vol.356 , pp. 327-334
    • Rodrigues-Lima, F.1    Delomenie, C.2    Goodfellow, G.H.3    Grant, D.M.4    Dupret, J.M.5
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0031172320 scopus 로고    scopus 로고
    • Overexpression and large-scale purification of recombinant hamster polymorphic arylamine N-acetyltransferase as a dihydrofolate reductase fusion protein
    • Sticha, K. R., Sieg, C. A., Bergstrom, C. P., Hanna, P. E., and Wagner, C. R. (1997) Overexpression and large-scale purification of recombinant hamster polymorphic arylamine N-acetyltransferase as a dihydrofolate reductase fusion protein, Protein. Expression Purif. 10, 141-153.
    • (1997) Protein. Expression Purif. , vol.10 , pp. 141-153
    • Sticha, K.R.1    Sieg, C.A.2    Bergstrom, C.P.3    Hanna, P.E.4    Wagner, C.R.5
  • 26
    • 0026674776 scopus 로고
    • Arylamine N-acetyltransferase in human red blood cells
    • Ward, A., Hickman, D., Gordon, J. W., and Sim, E. (1992) Arylamine N-acetyltransferase in human red blood cells, Biochem. Pharmacol. 44, 1099-1104.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 1099-1104
    • Ward, A.1    Hickman, D.2    Gordon, J.W.3    Sim, E.4
  • 27
    • 0020346954 scopus 로고
    • Solvent isotope effects of enzyme systems
    • Schowen, K. B., and Schowen, R. L. (1982) Solvent isotope effects of enzyme systems, Methods Enzymol. 87, 551-606.
    • (1982) Methods Enzymol. , vol.87 , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 28
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis, K. J., and Morrison, J. F. (1982) Buffers of constant ionic strength for studying pH-dependent processes, Methods Enzymol. 87, 405-426.
    • (1982) Methods Enzymol. , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 32
    • 3042904467 scopus 로고
    • Separation of acetyl transfer enzymes in pigeon liver extract
    • Chou, T. C., and Lipmann, F. (1952) Separation of acetyl transfer enzymes in pigeon liver extract, J. Biol. Chem. 196, 89-103.
    • (1952) J. Biol. Chem. , vol.196 , pp. 89-103
    • Chou, T.C.1    Lipmann, F.2
  • 33
    • 0036042103 scopus 로고    scopus 로고
    • The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis - An enzyme which inactivates the anti-tubercular drug, isoniazid
    • Sandy, J., Mushtaq, A., Kawamura, A., Sinclair, J., Sim, E., and Noble, M. (2002) The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis - An enzyme which inactivates the anti-tubercular drug, isoniazid, J. Mol. Biol. 318, 1071-1083.
    • (2002) J. Mol. Biol. , vol.318 , pp. 1071-1083
    • Sandy, J.1    Mushtaq, A.2    Kawamura, A.3    Sinclair, J.4    Sim, E.5    Noble, M.6
  • 34
    • 0034658314 scopus 로고    scopus 로고
    • Identification of amino acids imparting acceptor substrate selectivity to human arylamine acetyltransferases NAT1 and NAT2
    • Goodfellow, G. H., Dupret, J. M., and Grant, D. M. (2000) Identification of amino acids imparting acceptor substrate selectivity to human arylamine acetyltransferases NAT1 and NAT2, Biochem. J. 348 (part 1), 159-166.
    • (2000) Biochem. J. , vol.348 , Issue.PART 1 , pp. 159-166
    • Goodfellow, G.H.1    Dupret, J.M.2    Grant, D.M.3
  • 35
    • 0015239531 scopus 로고
    • Acetyl-coenzyme A: Arylamine N-acetyltransferase. Role of the acetyl-enzyme intermediate and the effects of substituents on the rate
    • Riddle, B., and Jencks, W. P. (1971) Acetyl-coenzyme A: Arylamine N-acetyltransferase. Role of the acetyl-enzyme intermediate and the effects of substituents on the rate, J. Biol. Chem. 246, 3250-3258.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3250-3258
    • Riddle, B.1    Jencks, W.P.2
  • 36
    • 0014082823 scopus 로고
    • N-Acetylation of drugs: Isolation and properties of an N-acetyltransferase from rabbit liver
    • Weber, W. W., and Cohen, S. N. (1967) N-Acetylation of drugs: Isolation and properties of an N-acetyltransferase from rabbit liver, Mol. Pharmacol. 3, 266-273.
    • (1967) Mol. Pharmacol. , vol.3 , pp. 266-273
    • Weber, W.W.1    Cohen, S.N.2
  • 37
    • 0035902435 scopus 로고    scopus 로고
    • Kinetic studies of guinea pig liver transglutaminase reveal a general-base-catalyzed deacylation mechanism
    • Leblanc, A., Gravel, C., Labelle, J., and Keillor, J. W. (2001) Kinetic studies of guinea pig liver transglutaminase reveal a general-base-catalyzed deacylation mechanism, Biochemistry 40, 8335-8342.
    • (2001) Biochemistry , vol.40 , pp. 8335-8342
    • Leblanc, A.1    Gravel, C.2    Labelle, J.3    Keillor, J.W.4
  • 38
    • 33845184117 scopus 로고
    • Structural-reactivity correlation in the aminolysis of phenyl and p-nitrophenyl thiolacetates
    • Castro, E. A., and Ureta, C. (1989) Structural-reactivity correlation in the aminolysis of phenyl and p-nitrophenyl thiolacetates, J. Org. Chem. 54, 2153-2159.
    • (1989) J. Org. Chem. , vol.54 , pp. 2153-2159
    • Castro, E.A.1    Ureta, C.2
  • 39
    • 13844289459 scopus 로고    scopus 로고
    • Irreversible interaction of arylamine N-acetyltransferases in the presence of N-hydroxy-4-acetylaminobiphenyl: A comparison of human and hamster enzymes
    • Wang, H., Wagner, C. R., and Hanna, P. E. (2005) Irreversible interaction of arylamine N-acetyltransferases in the presence of N-hydroxy-4- acetylaminobiphenyl: A comparison of human and hamster enzymes, Chem. Res. Toxicol. 18, 183-197.
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 183-197
    • Wang, H.1    Wagner, C.R.2    Hanna, P.E.3


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