메뉴 건너뛰기




Volumn 58, Issue 10, 2014, Pages 6122-6132

Structure, activity, and inhibition of the carboxyltransferase β-Subunit of acetyl coenzyme a carboxylase (AccD6) from mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; HALOXYFOP; HERBICIDE; LIGASE INHIBITOR; MALONYL COENZYME A; TUBERCULOSTATIC AGENT; BACTERIAL PROTEIN; PROTEIN BINDING; PYRIDINE DERIVATIVE; TRANSFERASE;

EID: 84907916561     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02574-13     Document Type: Article
Times cited : (19)

References (44)
  • 1
    • 0020643469 scopus 로고
    • Fatty acid synthesis and its regulation
    • Wakil SJ, Stoops JK, Joshi VC. 1983. Fatty acid synthesis and its regulation. Annu. Rev. Biochem. 52:537-579. http://dx.doi.org/10.1146/annurev.bi.52 .070183.002541.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 537-579
    • Wakil, S.J.1    Stoops, J.K.2    Joshi, V.C.3
  • 2
    • 0036018143 scopus 로고    scopus 로고
    • Multi-subunit acetyl-CoA carboxylases
    • Cronan JE, Jr, Waldrop GL. 2002. Multi-subunit acetyl-CoA carboxylases. Prog. Lipid Res. 41:407-435. http://dx.doi.org/10.1016/S0163-7827 (02)00007-3.
    • (2002) Prog. Lipid Res. , vol.41 , pp. 407-435
    • Cronan, J.E.1    Waldrop, G.L.2
  • 3
    • 0016830820 scopus 로고
    • Acetyl-coenzyme-A carboxylase from rat liver. Subunit structure and proteolytic modification
    • Tanabe T, Wada K, Okazaki T, Numa S. 1975. Acetyl-coenzyme-A carboxylase from rat liver. Subunit structure and proteolytic modification. Eur. J. Biochem. 57:15-24.
    • (1975) Eur. J. Biochem. , vol.57 , pp. 15-24
    • Tanabe, T.1    Wada, K.2    Okazaki, T.3    Numa, S.4
  • 6
    • 0035940515 scopus 로고    scopus 로고
    • Comprehensive identification of conditionally essential genes in mycobacteria
    • Sassetti CM, Boyd DH, Rubin EJ. 2001. Comprehensive identification of conditionally essential genes in mycobacteria. Proc. Natl. Acad. Sci. U. S. A. 98:12712-12717. http://dx.doi.org/10.1073/pnas.231275498.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 12712-12717
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 7
    • 12844278679 scopus 로고    scopus 로고
    • Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis
    • Takayama K, Wang C, Besra GS. 2005. Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis. Clin. Microbiol. Rev. 18:81-10. http://dx.doi.org/10.1128/CMR.18.1.81-101.2005.
    • (2005) Clin. Microbiol. Rev. , vol.18 , pp. 81-10
    • Takayama, K.1    Wang, C.2    Besra, G.S.3
  • 8
    • 33845415806 scopus 로고    scopus 로고
    • Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis
    • Holton SJ, King-Scott S, Nasser-Eddine A, Kaufmann SH, Wilmanns M. 2006. Structural diversity in the six-fold redundant set of acyl-CoA carboxyltransferases in Mycobacterium tuberculosis. FEBS Lett. 580:6898-6902. http://dx.doi.org/10.1016/j.febslet.2006.11.054.
    • (2006) FEBS Lett. , vol.580 , pp. 6898-6902
    • Holton, S.J.1    King-Scott, S.2    Nasser-Eddine, A.3    Kaufmann, S.H.4    Wilmanns, M.5
  • 9
    • 0036160305 scopus 로고    scopus 로고
    • Genomic analyses of microbial virulence
    • Sassetti C, Rubin EJ. 2002. Genomic analyses of microbial virulence. Curr. Opin. Microbiol. 5:27-32. http://dx.doi.org/10.1016/S1369-5274 (02)00281-3.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 27-32
    • Sassetti, C.1    Rubin, E.J.2
  • 10
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • Sassetti CM, Boyd DH, Rubin EJ. 2003. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 48:77-84. http://dx.doi.org/10.1046/j.1365-2958.2003.03425.x.
    • (2003) Mol. Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 11
    • 33846632320 scopus 로고    scopus 로고
    • AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acylcoenzyme A carboxylase in Mycobacterium tuberculosis
    • Daniel J, Oh TJ, Lee CM, Kolattukudy PE. 2007. AccD6, a member of the Fas II locus, is a functional carboxyltransferase subunit of the acylcoenzyme A carboxylase in Mycobacterium tuberculosis. J. Bacteriol. 189: 911-917. http://dx.doi.org/10.1128/JB.01019-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 911-917
    • Daniel, J.1    Oh, T.J.2    Lee, C.M.3    Kolattukudy, P.E.4
  • 12
    • 33645239314 scopus 로고    scopus 로고
    • Identification and characterization of Rv3281 as a novel subunit of a biotindependent acyl-CoA carboxylase in Mycobacterium tuberculosis
    • Oh TJ, Daniel J, Kim HJ, Sirakova TD, Kolattukudy PE. 2006. Identification and characterization of Rv3281 as a novel subunit of a biotindependent acyl-CoA carboxylase in Mycobacterium tuberculosis. J. Biol. Chem. 281:3899-3908. http://dx.doi.org/10.1074/jbc.M511761200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3899-3908
    • Oh, T.J.1    Daniel, J.2    Kim, H.J.3    Sirakova, T.D.4    Kolattukudy, P.E.5
  • 13
    • 0346726282 scopus 로고    scopus 로고
    • Herbicide safety relative to common targets in plants and mammals
    • Shaner DL. 2004. Herbicide safety relative to common targets in plants and mammals. Pest Manag. Sci. 60:17-24. http://dx.doi.org/10.1002/ps .782.
    • (2004) Pest Manag. Sci. , vol.60 , pp. 17-24
    • Shaner, D.L.1
  • 14
    • 0027955944 scopus 로고
    • Herbicides inhibiting acetyl-CoA carboxylase
    • Gronwald JW. 1994. Herbicides inhibiting acetyl-CoA carboxylase. Biochem. Soc. Trans. 22:616-621.
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 616-621
    • Gronwald, J.W.1
  • 16
    • 0033539685 scopus 로고    scopus 로고
    • Growth of Toxoplasma gondii is inhibited by aryloxyphenoxypropionate herbicides targeting acetyl-CoA carboxylase
    • Zuther E, Johnson JJ, Haselkorn R, McLeod R, Gornicki P. 1999. Growth of Toxoplasma gondii is inhibited by aryloxyphenoxypropionate herbicides targeting acetyl-CoA carboxylase. Proc. Natl. Acad. Sci. U. S. A. 96:13387-13392. http://dx.doi.org/10.1073/pnas.96.23.13387.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13387-13392
    • Zuther, E.1    Johnson, J.J.2    Haselkorn, R.3    Mc Leod, R.4    Gornicki, P.5
  • 17
    • 0033431683 scopus 로고    scopus 로고
    • Herbicide sensitivity determinant of wheat plastid acetyl-CoA carboxylase is located in a 400-amino acid fragment of the carboxyltransferase domain
    • Nikolskaya T, Zagnitko O, Tevzadze G, Haselkorn R, Gornicki P. 1999. Herbicide sensitivity determinant of wheat plastid acetyl-CoA carboxylase is located in a 400-amino acid fragment of the carboxyltransferase domain. Proc. Natl. Acad. Sci. U. S. A. 96:14647-14651. http://dx.doi.org/10 .1073/pnas.96.25.14647.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 14647-14651
    • Nikolskaya, T.1    Zagnitko, O.2    Tevzadze, G.3    Haselkorn, R.4    Gornicki, P.5
  • 18
    • 0027619184 scopus 로고
    • Wheat acetyl-CoA carboxylase
    • Gornicki P, Haselkorn R. 1993. Wheat acetyl-CoA carboxylase. Plant Mol. Biol. 22:547-552. http://dx.doi.org/10.1007/BF00015984.
    • (1993) Plant Mol. Biol. , vol.22 , pp. 547-552
    • Gornicki, P.1    Haselkorn, R.2
  • 19
    • 1942533548 scopus 로고    scopus 로고
    • Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop
    • Zhang H, Tweel B, Tong L. 2004. Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop. Proc. Natl. Acad. Sci. U. S. A. 101:5910-5915. http://dx .doi.org/10.1073/pnas.0400891101.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 5910-5915
    • Zhang, H.1    Tweel, B.2    Tong, L.3
  • 20
    • 73949136846 scopus 로고    scopus 로고
    • A different mechanism for the inhibition of the carboxyltransferase domain of acetylcoenzyme A carboxylase by tepraloxydim
    • Xiang S, Callaghan MM, Watson KG, Tong L. 2009. A different mechanism for the inhibition of the carboxyltransferase domain of acetylcoenzyme A carboxylase by tepraloxydim. Proc. Natl. Acad. Sci. U. S. A. 106:20723-20727. http://dx.doi.org/10.1073/pnas.0908431106.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20723-20727
    • Xiang, S.1    Callaghan, M.M.2    Watson, K.G.3    Tong, L.4
  • 21
    • 78650638635 scopus 로고    scopus 로고
    • Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden
    • Yu LP, Kim YS, Tong L. 2010. Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden. Proc. Natl. Acad. Sci. U. S. A. 107:22072-22077. http://dx.doi.org/10 .1073/pnas.1012039107.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , Issue.107 , pp. 22072-22077
    • Yu, L.P.1    Kim, Y.S.2    Tong, L.3
  • 22
    • 0016285541 scopus 로고
    • Acetyl coenzyme-A carboxylase system of Escherichia coli-purification and properties of biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components
    • Guchhait RB, Polakis SE, Dimroth P, Stoll E, Moss J, Lane MD. 1974. Acetyl coenzyme-A carboxylase system of Escherichia coli-purification and properties of biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components. J. Biol. Chem. 249:6633-6645.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6633-6645
    • Guchhait, R.B.1    Polakis, S.E.2    Dimroth, P.3    Stoll, E.4    Moss, J.5    Lane, M.D.6
  • 23
    • 0000810256 scopus 로고
    • Inhibition of acetyl-coenzyme-A carboxylase by 2 classes of grass-selective herbicides
    • Rendina AR, Craigkennard AC, Beaudoin JD, Breen MK. 1990. Inhibition of acetyl-coenzyme-A carboxylase by 2 classes of grass-selective herbicides. J. Agric. Food Chem. 38:1282-1287. http://dx.doi.org/10.1021/jf00095a029.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1282-1287
    • Rendina, A.R.1    Craigkennard, A.C.2    Beaudoin, J.D.3    Breen, M.K.4
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol. 276:307-326. http://dx .doi.org/10.1016/S0076-6879(97)76066-X.
    • (1997) Method Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong M, Sawaya MR, Wang SS, Phillips M, Cascio D, Eisenberg D. 2006. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 103:8060-8065. http://dx.doi.org/10.1073/pnas .0602606103.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 27
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60:2126-2132. http://dx .doi.org/10.1107/S0907444904019158.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 29
    • 33747593473 scopus 로고    scopus 로고
    • Use of PYMOL as a communications tool for molecular science
    • DeLano WL. 2004. Use of PYMOL as a communications tool for molecular science. Abstr. Pap. Am. Chem. Soc. 228:U313-U314.
    • (2004) Abstr. Pap. Am. Chem. Soc. , vol.228 , pp. U313-U314
    • De Lano, W.L.1
  • 30
    • 0036296417 scopus 로고    scopus 로고
    • A bisubstrate analog inhibitor of the carboxyltransferase component of acetyl-CoA carboxylase
    • Levert KL, Waldrop GL. 2002. A bisubstrate analog inhibitor of the carboxyltransferase component of acetyl-CoA carboxylase. Biochem. Biophys. Res. Co. 291:1213-1217. http://dx.doi.org/10.1006/bbrc.2002.6576.
    • (2002) Biochem. Biophys. Res. Co. , vol.291 , pp. 1213-1217
    • Levert, K.L.1    Waldrop, G.L.2
  • 31
    • 0002314426 scopus 로고
    • Inhibition of acetyl-CoA carboxylase activity by haloxyfop and tralkoxydim
    • Secor J, Cseke C. 1988. Inhibition of acetyl-CoA carboxylase activity by haloxyfop and tralkoxydim. Plant Physiol. 86:10-12. http://dx.doi.org/10 .1104/pp.86.1.10.
    • (1988) Plant Physiol. , vol.86 , pp. 10-12
    • Secor, J.1    Cseke, C.2
  • 32
    • 0034712697 scopus 로고    scopus 로고
    • New reactions in the crotonase superfamily: Structure of methylmalonyl CoA decarboxylase from Escherichia coli
    • Benning MM, Haller T, Gerlt JA, Holden HM. 2000. New reactions in the crotonase superfamily: structure of methylmalonyl CoA decarboxylase from Escherichia coli. Biochemistry 39:4630-4639. http://dx.doi.org/10.1021/bi9928896.
    • (2000) Biochemistry , vol.39 , pp. 4630-4639
    • Benning, M.M.1    Haller, T.2    Gerlt, J.A.3    Holden, H.M.4
  • 33
    • 3242887525 scopus 로고    scopus 로고
    • STRIDE: A web server for secondary structure assignment from known atomic coordinates of proteins
    • Heinig M, Frishman D. 2004. STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins. Nucleic Acids Res. 32:W500-W502. http://dx.doi.org/10.1093/nar/gkh429.
    • (2004) Nucleic Acids Res. , vol.32 , pp. W500-W502
    • Heinig, M.1    Frishman, D.2
  • 34
    • 3242885425 scopus 로고    scopus 로고
    • CaspR: A web server for automated molecular replacement using homology modeling
    • Claude JB, Suhre K, Notredame C, Claverie JM, Abergel C. 2004. CaspR: a web server for automated molecular replacement using homology modeling. Nucleic Acids Res. 32:W606-W609. http://dx.doi.org/10 .1093/nar/gkh400.
    • (2004) Nucleic Acids Res. , vol.32 , pp. W606-W609
    • Claude, J.B.1    Suhre, K.2    Notredame, C.3    Claverie, J.M.4    Abergel, C.5
  • 36
    • 8344220571 scopus 로고    scopus 로고
    • Crystal structure of the beta-subunit of acyl- CoA carboxylase: Structure-based engineering of substrate specificity
    • Diacovich L, Mitchell DL, Pham H, Gago G, Melgar MM, Khosla C, Gramajo H, Tsai SC. 2004. Crystal structure of the beta-subunit of acyl- CoA carboxylase: structure-based engineering of substrate specificity. Biochemistry 43:14027-14036. http://dx.doi.org/10.1021/bi049065v.
    • (2004) Biochemistry , vol.43 , pp. 14027-14036
    • Diacovich, L.1    Mitchell, D.L.2    Pham, H.3    Gago, G.4    Melgar, M.M.5    Khosla, C.6    Gramajo, H.7    Tsai, S.C.8
  • 37
  • 39
    • 0037163047 scopus 로고    scopus 로고
    • Kinetic and structural analysis of a new group of acyl- CoA carboxylases found in Streptomyces coelicolor A3 (2)
    • Diacovich L, Peiru S, Kurth D, Rodriguez E, Podesta F, Khosla C, Gramajo H. 2002. Kinetic and structural analysis of a new group of acyl- CoA carboxylases found in Streptomyces coelicolor A3(2). J. Biol. Chem. 277:31228-31236. http://dx.doi.org/10.1074/jbc.M203263200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31228-31236
    • Diacovich, L.1    Peiru, S.2    Kurth, D.3    Rodriguez, E.4    Podesta, F.5    Khosla, C.6    Gramajo, H.7
  • 40
    • 0037470947 scopus 로고    scopus 로고
    • Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase
    • Zhang H, Yang Z, Shen Y, Tong L. 2003. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Science 299:2064-2067. http://dx.doi.org/10.1126/science.1081366.
    • (2003) Science , vol.299 , pp. 2064-2067
    • Zhang, H.1    Yang, Z.2    Shen, Y.3    Tong, L.4
  • 41
    • 34250745809 scopus 로고    scopus 로고
    • Compensating enthalpic and entropic changes hinder binding affinity op-timization
    • Lafont V, Armstrong AA, Ohtaka H, Kiso Y, Amzel LM, Freire E. 2007. Compensating enthalpic and entropic changes hinder binding affinity op- timization. Chem. Biol. Drug Des. 69:413-422. http://dx.doi.org/10.1111/j.1747-0285.2007.00519.x.
    • (2007) Chem. Biol. Drug Des. , vol.69 , pp. 413-422
    • Lafont, V.1    Armstrong, A.A.2    Ohtaka, H.3    Kiso, Y.4    Amzel, L.M.5    Freire, E.6
  • 42
    • 0034093758 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors: Enthalpic versus entropic optimization of the binding affinity
    • Velazquez-Campoy A, Todd MJ, Freire E. 2000. HIV-1 protease inhibitors: enthalpic versus entropic optimization of the binding affinity. Biochemistry 39:2201-2207. http://dx.doi.org/10.1021/bi992399d.
    • (2000) Biochemistry , vol.39 , pp. 2201-2207
    • Velazquez-Campoy, A.1    Todd, M.J.2    Freire, E.3
  • 43
    • 0344823654 scopus 로고    scopus 로고
    • Multidrug resistance to HIV-1 protease inhibition requires cooperative coupling between distal mutations
    • Ohtaka H, Schön A, Freire E. 2003. Multidrug resistance to HIV-1 protease inhibition requires cooperative coupling between distal mutations. Biochemistry 42:13659-13666. http://dx.doi.org/10.1021/bi0350405.
    • (2003) Biochemistry , vol.42 , pp. 13659-13666
    • Ohtaka, H.1    Schön, A.2    Freire, E.3
  • 44
    • 0033634971 scopus 로고    scopus 로고
    • A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis
    • Glickman MS, Cox JS, Jacobs WR. 2000. A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis. Mol. Cell 5:717-727. http://dx.doi.org/10.1016/S1097-2765(00)80250-6.
    • (2000) Mol. Cell , vol.5 , pp. 717-727
    • Glickman, M.S.1    Cox, J.S.2    Jacobs, W.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.