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Volumn 18, Issue 11, 2011, Pages 1432-1441

Bisubstrate adenylation inhibitors of biotin protein ligase from mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ENZYME INHIBITOR; LIGASE; TUBERCULOSTATIC AGENT;

EID: 82255186665     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2011.08.013     Document Type: Article
Times cited : (81)

References (52)
  • 2
    • 25144501423 scopus 로고    scopus 로고
    • Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: Structural basis of biotin activation
    • DOI 10.1016/j.jmb.2005.08.032, PII S0022283605009691
    • B. Bagautdinov, C. Kuroishi, M. Sugahara, and N. Kunishima Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation J. Mol. Biol. 353 2005 322 333 (Pubitemid 41356615)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.2 , pp. 322-333
    • Bagautdinov, B.1    Kuroishi, C.2    Sugahara, M.3    Kunishima, N.4
  • 3
    • 0033819143 scopus 로고    scopus 로고
    • The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis
    • M. Braibant, P. Gilot, and J. Content The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis FEMS Microbiol. Rev. 24 2000 449 467
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 449-467
    • Braibant, M.1    Gilot, P.2    Content, J.3
  • 4
    • 57449109136 scopus 로고    scopus 로고
    • Intrinsic nucleofugality scale within the framework of density functional reactivity theory
    • L. Broeckaert, J. Moens, G. Roos, F. De Proft, and P. Geerlings Intrinsic nucleofugality scale within the framework of density functional reactivity theory J. Phys. Chem. A 112 2008 12164 12171
    • (2008) J. Phys. Chem. A , vol.112 , pp. 12164-12171
    • Broeckaert, L.1    Moens, J.2    Roos, G.3    De Proft, F.4    Geerlings, P.5
  • 5
    • 14344255691 scopus 로고    scopus 로고
    • Use of binding enthalpy to drive an allosteric transition
    • DOI 10.1021/bi047792k
    • P.H. Brown, and D. Beckett Use of binding enthalpy to drive an allosteric transition Biochemistry 44 2005 3112 3121 (Pubitemid 40293686)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 3112-3121
    • Brown, P.H.1    Beckett, D.2
  • 6
    • 1642384541 scopus 로고    scopus 로고
    • The biotin repressor: Modulation of allostery by corepressor analogs
    • DOI 10.1016/j.jmb.2004.01.041, PII S0022283604001111
    • P.H. Brown, J.E. Cronan, M. Grøtli, and D. Beckett The biotin repressor: modulation of allostery by corepressor analogs J. Mol. Biol. 337 2004 857 869 (Pubitemid 38368930)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.4 , pp. 857-869
    • Brown, P.H.1    Cronan, J.E.2    Grotli, M.3    Beckett, D.4
  • 7
    • 0035853728 scopus 로고    scopus 로고
    • Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase: Influence of the N-terminus on biotinylation and identification of a minimum functional protein
    • E. Campeau, and R.A. Gravel Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase: influence of the N-terminus on biotinylation and identification of a minimum functional protein J. Biol. Chem. 276 2001 12310 12316
    • (2001) J. Biol. Chem. , vol.276 , pp. 12310-12316
    • Campeau, E.1    Gravel, R.A.2
  • 8
    • 0033199782 scopus 로고    scopus 로고
    • The enzymatic biotinylation of proteins: A post-translational modification of exceptional specificity
    • DOI 10.1016/S0968-0004(99)01438-3, PII S0968000499014383
    • A. Chapman-Smith, and J.E. Cronan Jr. The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity Trends Biochem. Sci. 24 1999 359 363 (Pubitemid 29421812)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 359-363
    • Chapman-Smith, A.1    Cronan Jr., J.E.2
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 14
    • 33344469904 scopus 로고    scopus 로고
    • Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis
    • J.A. Ferreras, J.S. Ryu, F. Di Lello, D.S. Tan, and L.E. Quadri Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis Nat. Chem. Biol. 1 2005 29 32
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 29-32
    • Ferreras, J.A.1    Ryu, J.S.2    Di Lello, F.3    Tan, D.S.4    Quadri, L.E.5
  • 15
    • 30744470169 scopus 로고    scopus 로고
    • Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis
    • DOI 10.1128/JB.188.2.477-486.2006
    • G. Gago, D. Kurth, L. Diacovich, S.C. Tsai, and H. Gramajo Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis J. Bacteriol. 188 2006 477 486 (Pubitemid 43100536)
    • (2006) Journal of Bacteriology , vol.188 , Issue.2 , pp. 477-486
    • Gago, G.1    Kurth, D.2    Diacovich, L.3    Tsai, S.-C.4    Gramajo, H.5
  • 16
    • 77950134712 scopus 로고    scopus 로고
    • Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration
    • V. Gupta, R.K. Gupta, G. Khare, D.M. Salunke, A. Surolia, and A.K. Tyagi Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration PLoS ONE 5 2010 e9222
    • (2010) PLoS ONE , vol.5 , pp. 9222
    • Gupta, V.1    Gupta, R.K.2    Khare, G.3    Salunke, D.M.4    Surolia, A.5    Tyagi, A.K.6
  • 17
    • 28844499031 scopus 로고    scopus 로고
    • Prospects for aminoacyl-tRNA synthetase inhibitors as new antimicrobial agents
    • DOI 10.1128/AAC.49.12.4821-4833.2005
    • J.G. Hurdle, A.J. O'Neill, and I. Chopra Prospects for aminoacyl-tRNA synthetase inhibitors as new antimicrobial agents Antimicrob. Agents Chemother. 49 2005 4821 4833 (Pubitemid 41778891)
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.12 , pp. 4821-4833
    • Hurdle, J.G.1    O'Neill, A.J.2    Chopra, I.3
  • 20
    • 0035980619 scopus 로고    scopus 로고
    • Energy transfer between fluorescent proteins using a co-expression system in Mycobacterium smegmatis
    • DOI 10.1016/S0378-1119(01)00712-0, PII S0378111901007120
    • I. Kaps, S. Ehrt, S. Seeber, D. Schnappinger, C. Martin, L.W. Riley, and M. Niederweis Energy transfer between fluorescent proteins using a co-expression system in Mycobacterium smegmatis Gene 278 2001 115 124 (Pubitemid 33055785)
    • (2001) Gene , vol.278 , Issue.1-2 , pp. 115-124
    • Kaps, I.1    Ehrt, S.2    Seeber, S.3    Schnappinger, D.4    Martin, C.5    Riley, L.W.6    Niederweis, M.7
  • 21
    • 0037844668 scopus 로고    scopus 로고
    • Aminoacyl-tRNA synthetases and their inhibitors as a novel family of antibiotics
    • S. Kim, S.W. Lee, E.C. Choi, and S.Y. Choi Aminoacyl-tRNA synthetases and their inhibitors as a novel family of antibiotics Appl. Microbiol. Biotechnol. 61 2003 278 288 (Pubitemid 36683523)
    • (2003) Applied Microbiology and Biotechnology , vol.61 , Issue.4 , pp. 278-288
    • Kim, S.1    Lee, S.W.2    Choi, E.-C.3    Choi, S.Y.4
  • 24
    • 0035442411 scopus 로고    scopus 로고
    • Direct measurement of protein binding energetics by isothermal titration calorimetry
    • DOI 10.1016/S0959-440X(00)00248-7
    • S. Leavitt, and E. Freire Direct measurement of protein binding energetics by isothermal titration calorimetry Curr. Opin. Struct. Biol. 11 2001 560 566 (Pubitemid 32972017)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.5 , pp. 560-566
    • Leavitt, S.1    Freire, E.2
  • 25
    • 54549127323 scopus 로고    scopus 로고
    • Alpha,beta-methylene-2′-deoxynucleoside 5′-triphosphates as noncleavable substrates for DNA polymerases: Isolation, characterization, and stability studies of novel 2′-deoxycyclonucleosides, 3,5′-cyclo-dG, and 2,5′-cyclo-dT
    • F. Liang, N. Jain, T. Hutchens, D.D. Shock, W.A. Beard, S.H. Wilson, M.P. Chiarelli, and B.P. Cho Alpha,beta-methylene-2′-deoxynucleoside 5′-triphosphates as noncleavable substrates for DNA polymerases: isolation, characterization, and stability studies of novel 2′- deoxycyclonucleosides, 3,5′-cyclo-dG, and 2,5′-cyclo-dT J. Med. Chem. 51 2008 6460 6470
    • (2008) J. Med. Chem. , vol.51 , pp. 6460-6470
    • Liang, F.1    Jain, N.2    Hutchens, T.3    Shock, D.D.4    Beard, W.A.5    Wilson, S.H.6    Chiarelli, M.P.7    Cho, B.P.8
  • 26
    • 55249100482 scopus 로고    scopus 로고
    • Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis
    • X. Lu, H. Zhang, P.J. Tonge, and D.S. Tan Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis Bioorg. Med. Chem. Lett. 18 2008 5963 5966
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 5963-5966
    • Lu, X.1    Zhang, H.2    Tonge, P.J.3    Tan, D.S.4
  • 27
    • 84859477210 scopus 로고    scopus 로고
    • Accessed July 28, 2011
    • Ma, Q., and Wilmanns, M. (2007). Protein Data Bank code 2CGH. http://www.rcsb.org/pdb/explore/explore.do?structureId=2CGH. Accessed July 28, 2011.
    • (2007) Protein Data Bank Code 2CGH
    • Ma, Q.1    Wilmanns, M.2
  • 28
    • 0034903883 scopus 로고    scopus 로고
    • E: Role in global gene expression and survival in macrophages
    • DOI 10.1046/j.1365-2958.2001.02525.x
    • R. Manganelli, M.I. Voskuil, G.K. Schoolnik, and I. Smith The Mycobacterium tuberculosis ECF sigma factor sigmaE: role in global gene expression and survival in macrophages Mol. Microbiol. 41 2001 423 437 (Pubitemid 32730541)
    • (2001) Molecular Microbiology , vol.41 , Issue.2 , pp. 423-437
    • Manganelli, R.1    Voskuil, M.I.2    Schoolnik, G.K.3    Smith, I.4
  • 29
    • 77953105101 scopus 로고    scopus 로고
    • Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection
    • J. Marrero, K.Y. Rhee, D. Schnappinger, K. Pethe, and S. Ehrt Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection Proc. Natl. Acad. Sci. USA 107 2010 9819 9824
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 9819-9824
    • Marrero, J.1    Rhee, K.Y.2    Schnappinger, D.3    Pethe, K.4    Ehrt, S.5
  • 32
    • 51849155973 scopus 로고    scopus 로고
    • Inhibition of siderophore biosynthesis in Mycobacterium tuberculosis with nucleoside bisubstrate analogues: Structure-activity relationships of the nucleobase domain of 5′-O-[N-(salicyl)sulfamoyl]adenosine
    • J. Neres, N.P. Labello, R.V. Somu, H.I. Boshoff, D.J. Wilson, J. Vannada, L. Chen, C.E. Barry 3rd, E.M. Bennett, and C.C. Aldrich Inhibition of siderophore biosynthesis in Mycobacterium tuberculosis with nucleoside bisubstrate analogues: structure-activity relationships of the nucleobase domain of 5′-O-[N-(salicyl)sulfamoyl]adenosine J. Med. Chem. 51 2008 5349 5370
    • (2008) J. Med. Chem. , vol.51 , pp. 5349-5370
    • Neres, J.1    Labello, N.P.2    Somu, R.V.3    Boshoff, H.I.4    Wilson, D.J.5    Vannada, J.6    Chen, L.7    Barry III, C.E.8    Bennett, E.M.9    Aldrich, C.C.10
  • 33
    • 0348110537 scopus 로고    scopus 로고
    • Efficient switching of mycobacteriophage L5-based integrating plasmids in Mycobacterium tuberculosis
    • DOI 10.1016/S0378-1097(03)00823-1
    • C.A. Pashley, and T. Parish Efficient switching of mycobacteriophage L5-based integrating plasmids in Mycobacterium tuberculosis FEMS Microbiol. Lett. 229 2003 211 215 (Pubitemid 37532872)
    • (2003) FEMS Microbiology Letters , vol.229 , Issue.2 , pp. 211-215
    • Pashley, C.A.1    Parish, T.2
  • 35
    • 9144263033 scopus 로고    scopus 로고
    • New aminoacyl-tRNA synthetase inhibitors as antibacterial agents
    • DOI 10.2174/1568005043340515
    • J. Pohlmann, and H. Brötz-Oesterhelt New aminoacyl-tRNA synthetase inhibitors as antibacterial agents Curr. Drug Targets Infect. Disord. 4 2004 261 272 (Pubitemid 39539181)
    • (2004) Current Drug Targets - Infectious Disorders , vol.4 , Issue.4 , pp. 261-272
    • Pohlmann, J.1    Brotz-Oesterhelt, H.2
  • 36
    • 15744389881 scopus 로고    scopus 로고
    • The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: Identification of the carboxylation product and determination of the acyl-CoA carboxylase components
    • DOI 10.1074/jbc.M408578200
    • D. Portevin, C. de Sousa-D'Auria, H. Montrozier, C. Houssin, A. Stella, M.A. Lanéelle, F. Bardou, C. Guilhot, and M. Daffé The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase are required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components J. Biol. Chem. 280 2005 8862 8874 (Pubitemid 40409576)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 8862-8874
    • Portevin, D.1    De Sousa-D'Auria, C.2    Montrozier, H.3    Houssin, C.4    Stella, A.5    Laneelle, M.-A.6    Bardou, F.7    Guilhot, C.8    Daffe, M.9
  • 37
    • 48449094348 scopus 로고    scopus 로고
    • Ligand specificity of group i biotin protein ligase of Mycobacterium tuberculosis
    • S. Purushothaman, G. Gupta, R. Srivastava, V.G. Ramu, and A. Surolia Ligand specificity of group I biotin protein ligase of Mycobacterium tuberculosis PLoS ONE 3 2008 e2320
    • (2008) PLoS ONE , vol.3 , pp. 2320
    • Purushothaman, S.1    Gupta, G.2    Srivastava, R.3    Ramu, V.G.4    Surolia, A.5
  • 39
    • 0034650726 scopus 로고    scopus 로고
    • Exact analysis of competition ligand binding by displacement isothermal titration calorimetry
    • DOI 10.1006/abio.1999.4402
    • B.W. Sigurskjold Exact analysis of competition ligand binding by displacement isothermal titration calorimetry Anal. Biochem. 277 2000 260 266 (Pubitemid 30055877)
    • (2000) Analytical Biochemistry , vol.277 , Issue.2 , pp. 260-266
    • Sigurskjold, B.W.1
  • 40
    • 77951680623 scopus 로고    scopus 로고
    • Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from Escherichia coli
    • A.L. Sikora, D.J. Wilson, C.C. Aldrich, and J.S. Blanchard Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from Escherichia coli Biochemistry 49 2010 3648 3657
    • (2010) Biochemistry , vol.49 , pp. 3648-3657
    • Sikora, A.L.1    Wilson, D.J.2    Aldrich, C.C.3    Blanchard, J.S.4
  • 41
    • 0033709606 scopus 로고    scopus 로고
    • Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis
    • R.A. Slayden, R.E. Lee, and C.E. Barry 3rd Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis Mol. Microbiol. 38 2000 514 525
    • (2000) Mol. Microbiol. , vol.38 , pp. 514-525
    • Slayden, R.A.1    Lee, R.E.2    Barry III, C.E.3
  • 42
    • 30444445995 scopus 로고    scopus 로고
    • Rationally-designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis
    • DOI 10.1021/jm051060o
    • R.V. Somu, H. Boshoff, C. Qiao, E.M. Bennett, C.E. Barry 3rd, and C.C. Aldrich Rationally designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis J. Med. Chem. 49 2006 31 34 (Pubitemid 43077318)
    • (2006) Journal of Medicinal Chemistry , vol.49 , Issue.1 , pp. 31-34
    • Somu, R.V.1    Boshoff, H.2    Qiao, C.3    Bennett, E.M.4    Barry III, C.E.5    Aldrich, C.C.6
  • 44
    • 61449218735 scopus 로고    scopus 로고
    • Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity
    • C.M. Tron, I.W. McNae, M. Nutley, D.J. Clarke, A. Cooper, M.D. Walkinshaw, R.L. Baxter, and D.J. Campopiano Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity J. Mol. Biol. 387 2009 129 146
    • (2009) J. Mol. Biol. , vol.387 , pp. 129-146
    • Tron, C.M.1    McNae, I.W.2    Nutley, M.3    Clarke, D.J.4    Cooper, A.5    Walkinshaw, M.D.6    Baxter, R.L.7    Campopiano, D.J.8
  • 45
    • 0032922193 scopus 로고    scopus 로고
    • SFCHECK: A unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model
    • A.A. Vaguine, J. Richelle, and S.J. Wodak SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model Acta Crystallogr. D Biol. Crystallogr. 55 1999 191 205 (Pubitemid 29053816)
    • (1999) Acta Crystallographica Section D: Biological Crystallography , vol.55 , Issue.1 , pp. 191-205
    • Vaguine, A.A.1    Richelle, J.2    Wodak, S.J.3
  • 46
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • A. Velazquez-Campoy, and E. Freire Isothermal titration calorimetry to determine association constants for high-affinity ligands Nat. Protoc. 1 2006 186 191
    • (2006) Nat. Protoc. , vol.1 , pp. 186-191
    • Velazquez-Campoy, A.1    Freire, E.2
  • 47
    • 0035876257 scopus 로고    scopus 로고
    • The binding energetics of first- and second-generation HIV-1 protease inhibitors: Implications for drug design
    • DOI 10.1006/abbi.2001.2333
    • A. Velazquez-Campoy, Y. Kiso, and E. Freire The binding energetics of first- and second-generation HIV-1 protease inhibitors: implications for drug design Arch. Biochem. Biophys. 390 2001 169 175 (Pubitemid 32568478)
    • (2001) Archives of Biochemistry and Biophysics , vol.390 , Issue.2 , pp. 169-175
    • Velazquez-Campoy, A.1    Kiso, Y.2    Freire, E.3
  • 48
    • 77954086090 scopus 로고    scopus 로고
    • A continuous kinetic assay for adenylation enzyme activity and inhibition
    • D.J. Wilson, and C.C. Aldrich A continuous kinetic assay for adenylation enzyme activity and inhibition Anal. Biochem. 404 2010 56 63
    • (2010) Anal. Biochem. , vol.404 , pp. 56-63
    • Wilson, D.J.1    Aldrich, C.C.2
  • 49
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • DOI 10.1016/0003-2697(89)90213-3
    • T. Wiseman, S. Williston, J.F. Brandts, and L.N. Lin Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179 1989 131 137 (Pubitemid 19149635)
    • (1989) Analytical Biochemistry , vol.179 , Issue.1 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 50
    • 33344466006 scopus 로고    scopus 로고
    • Co-repressor induced order and biotin repressor dimerization: A case for divergent followed by convergent evolution
    • DOI 10.1016/j.jmb.2005.12.066, PII S0022283605016426
    • Z.A. Wood, L.H. Weaver, P.H. Brown, D. Beckett, and B.W. Matthews Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution J. Mol. Biol. 357 2006 509 523 (Pubitemid 43290751)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.2 , pp. 509-523
    • Wood, Z.A.1    Weaver, L.H.2    Brown, P.H.3    Beckett, D.4    Matthews, B.W.5
  • 51
    • 0028034484 scopus 로고
    • Amino-imino tautomerization of N2-(4-n-butylphenyl)-2′-deoxy-3, 5′-cycloguanosine
    • I.B. Yanachkov, and G.E. Wright Amino-imino tautomerization of N2-(4-n-butylphenyl)-2′-deoxy-3,5′-cycloguanosine J. Org. Chem. 59 1994 6739 6743
    • (1994) J. Org. Chem. , vol.59 , pp. 6739-6743
    • Yanachkov, I.B.1    Wright, G.E.2
  • 52
    • 33845390581 scopus 로고    scopus 로고
    • Bisubstrate inhibition: Theory and application to N-acetyltransferases
    • DOI 10.1021/bi061621t
    • M. Yu, M.L. Magalhães, P.F. Cook, and J.S. Blanchard Bisubstrate inhibition: theory and application to N-acetyltransferases Biochemistry 45 2006 14788 14794 (Pubitemid 44906995)
    • (2006) Biochemistry , vol.45 , Issue.49 , pp. 14788-14794
    • Yu, M.1    Magalhaes, M.L.B.2    Cook, P.F.3    Blanchard, J.S.4


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