메뉴 건너뛰기




Volumn 51, Issue 35, 2012, Pages 7000-7016

The catalytic mechanism of the hotdog-fold enzyme superfamily 4-hydroxybenzoyl-coa thioesterase from arthrobacter sp. Strain SU

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; ARTHROBACTER SP; BASE CATALYSIS; CATALYTIC EFFICIENCIES; CATALYTIC MECHANISMS; COENZYME A; COVALENT ENZYME INTERMEDIATES; DOUBLE MUTANTS; ENZYME SUPERFAMILIES; HYDROGEN-BOND FORMATION; HYDROLYSIS REACTION; KINETIC ANALYSIS; NUCLEOPHILIC CATALYSIS; SINGLE MUTANT; SINGLE-STEP; STEADY-STATE KINETICS; SUBSTRATE BINDING; THIOESTERASES; THIOESTERS; TRANSITION-STATE; TWO-STEP PROCESS; WILD TYPES; X-RAY STRUCTURE;

EID: 84865756646     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301059m     Document Type: Article
Times cited : (23)

References (44)
  • 2
    • 0000047442 scopus 로고
    • Generation and stability of a simple thiol enolate in aqueous solution
    • Amyes, T. L. and Richard, J. P. (1992) Generation and stability of a simple thiol enolate in aqueous solution J. Am. Chem. Soc. 114, 10297-10302
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10297-10302
    • Amyes, T.L.1    Richard, J.P.2
  • 3
    • 0028601410 scopus 로고
    • Enoyl-coenzyme A hydratase-catalyzed exchange of the alpha-protons of coenzyme A thiol esters: A model for an enolized intermediate in the enzyme-catalyzed elimination?
    • D'Ordine, R. L, Bahnson, B. J., Tonge, P. J, and Anderson, V. E. (1994) Enoyl-coenzyme A hydratase-catalyzed exchange of the alpha-protons of coenzyme A thiol esters: a model for an enolized intermediate in the enzyme-catalyzed elimination? Biochemistry 33, 14733-4142
    • (1994) Biochemistry , vol.33 , pp. 14733-24142
    • D'Ordine, R.L.1    Bahnson, B.J.2    Tonge, P.J.3    Anderson, V.E.4
  • 4
    • 0036775842 scopus 로고    scopus 로고
    • The Claisen condensation in biology
    • Heath, R. J. and Rock, C. O. (2002) The Claisen condensation in biology Nat. Prod. Rep. 19, 581-596
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 581-596
    • Heath, R.J.1    Rock, C.O.2
  • 6
    • 64349120214 scopus 로고    scopus 로고
    • Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: Substrate specificities and mutagenic studies on the active-site residues
    • Guo, Z. F., Sun, Y., Zheng, S., and Guo, Z. (2009) Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues Biochemistry 48, 1712-1722
    • (2009) Biochemistry , vol.48 , pp. 1712-1722
    • Guo, Z.F.1    Sun, Y.2    Zheng, S.3    Guo, Z.4
  • 7
    • 59249107241 scopus 로고    scopus 로고
    • In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH
    • Chen, D., Wu, R., Bryan, T. L., and Dunaway-Mariano, D. (2009) In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH Biochemistry 48, 511-513
    • (2009) Biochemistry , vol.48 , pp. 511-513
    • Chen, D.1    Wu, R.2    Bryan, T.L.3    Dunaway-Mariano, D.4
  • 8
    • 57149116350 scopus 로고    scopus 로고
    • Selective removal of aberrant extender units by a type II thioesterase for efficient FR-008/candicidin biosynthesis in Streptomyces sp. strain FR-008
    • Zhou, Y., Meng, Q., You, D., Li, J., Chen, S., Ding, D., Zhou, X., Zhou, H., Bai, L., and Deng, Z. (2008) Selective removal of aberrant extender units by a type II thioesterase for efficient FR-008/candicidin biosynthesis in Streptomyces sp. strain FR-008 Appl. Environ. Microbiol. 74, 7235-7242
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 7235-7242
    • Zhou, Y.1    Meng, Q.2    You, D.3    Li, J.4    Chen, S.5    Ding, D.6    Zhou, X.7    Zhou, H.8    Bai, L.9    Deng, Z.10
  • 9
    • 64149117037 scopus 로고    scopus 로고
    • Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway
    • Claxton, H. B., Akey, D. L., Silver, M. K., Admiraal, S. J., and Smith, J. L. (2009) Structure and functional analysis of RifR, the type II thioesterase from the rifamycin biosynthetic pathway J. Biol. Chem. 284, 5021-5029
    • (2009) J. Biol. Chem. , vol.284 , pp. 5021-5029
    • Claxton, H.B.1    Akey, D.L.2    Silver, M.K.3    Admiraal, S.J.4    Smith, J.L.5
  • 12
    • 13244267005 scopus 로고    scopus 로고
    • The Hotdog fold: Wrapping up a superfamily of thioesterases and dehydratases
    • Dillon, S. C. and Bateman, A. (2004) The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratases BMC Bioinformatics 5, 109
    • (2004) BMC Bioinformatics , vol.5 , pp. 109
    • Dillon, S.C.1    Bateman, A.2
  • 13
    • 77954011231 scopus 로고    scopus 로고
    • Thioesterases: A new perspective based on their primary and tertiary structures
    • Cantu, D. C., Chen, Y., and Reilly, P. (2010) Thioesterases: a new perspective based on their primary and tertiary structures J. Protein Sci. 19, 1281-1295
    • (2010) J. Protein Sci. , vol.19 , pp. 1281-1295
    • Cantu, D.C.1    Chen, Y.2    Reilly, P.3
  • 14
    • 85027930482 scopus 로고    scopus 로고
    • Evolutionary divergence and functions of the human acyl-CoA thioesterase gene (ACOT) family
    • Brocker, C., Carpenter, C., Nebert, D. W., and Vasiliou, V. (2010) Evolutionary divergence and functions of the human acyl-CoA thioesterase gene (ACOT) family Hum. Genomics 4, 411-420
    • (2010) Hum. Genomics , vol.4 , pp. 411-420
    • Brocker, C.1    Carpenter, C.2    Nebert, D.W.3    Vasiliou, V.4
  • 15
    • 0034285515 scopus 로고    scopus 로고
    • Alpha/Beta-hydrolase fold enzymes: Structures, functions and mechanisms
    • Holmquist, M. (2000) Alpha/Beta-hydrolase fold enzymes: structures, functions and mechanisms Curr. Protein Pept. Sci. 1, 209-235
    • (2000) Curr. Protein Pept. Sci. , vol.1 , pp. 209-235
    • Holmquist, M.1
  • 16
    • 0032509337 scopus 로고    scopus 로고
    • The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3
    • Benning, M. M., Wesenberg, G., Liu, R., Taylor, K. L., Dunaway-Mariano, D., and Holden, H. M. (1998) The three-dimensional structure of 4-hydroxybenzoyl-CoA thioesterase from Pseudomonas sp. Strain CBS-3 J. Biol. Chem. 273, 33572-33579
    • (1998) J. Biol. Chem. , vol.273 , pp. 33572-33579
    • Benning, M.M.1    Wesenberg, G.2    Liu, R.3    Taylor, K.L.4    Dunaway-Mariano, D.5    Holden, H.M.6
  • 17
    • 0030584655 scopus 로고    scopus 로고
    • Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: Two catalytic activities in one active site
    • Leesong, M., Henderson, B. S., Gillig, J. R., Schwab, J. M., and Smith, J. L. (1996) Structure of a dehydratase-isomerase from the bacterial pathway for biosynthesis of unsaturated fatty acids: two catalytic activities in one active site Structure 4, 253-264
    • (1996) Structure , vol.4 , pp. 253-264
    • Leesong, M.1    Henderson, B.S.2    Gillig, J.R.3    Schwab, J.M.4    Smith, J.L.5
  • 18
    • 0242290213 scopus 로고    scopus 로고
    • The structure of 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU
    • Thoden, J. B., Zhuang, Z., Dunaway-Mariano, D., and Holden, H. M. (2003) The structure of 4-hydroxybenzoyl-CoA thioesterase from Arthrobacter sp. strain SU J. Biol. Chem. 278, 43709-43716
    • (2003) J. Biol. Chem. , vol.278 , pp. 43709-43716
    • Thoden, J.B.1    Zhuang, Z.2    Dunaway-Mariano, D.3    Holden, H.M.4
  • 19
    • 0037178828 scopus 로고    scopus 로고
    • X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase
    • Thoden, J. B., Holden, H. M., Zhuang, Z., and Dunaway-Mariano, D. (2002) X-ray crystallographic analyses of inhibitor and substrate complexes of wild-type and mutant 4-hydroxybenzoyl-CoA thioesterase J. Biol. Chem. 277, 27468-2776
    • (2002) J. Biol. Chem. , vol.277 , pp. 27468-32776
    • Thoden, J.B.1    Holden, H.M.2    Zhuang, Z.3    Dunaway-Mariano, D.4
  • 20
    • 0028672051 scopus 로고
    • On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway
    • Dunaway-Mariano, D. and Babbitt, P. C. (1994) On the origins and functions of the enzymes of the 4-chlorobenzoate to 4-hydroxybenzoate converting pathway Biodegradation 5, 259-276
    • (1994) Biodegradation , vol.5 , pp. 259-276
    • Dunaway-Mariano, D.1    Babbitt, P.C.2
  • 21
    • 0032054709 scopus 로고    scopus 로고
    • Isotope effects on enzyme-catalyzed acyl transfer from p -nitrophenyl acetate: Concerted mechanisms and increased hyperconjugation in the transition state
    • Hess, R. A., Hengge, A. C., and Cleland, W. W. (1998) Isotope effects on enzyme-catalyzed acyl transfer from p -nitrophenyl acetate: Concerted mechanisms and increased hyperconjugation in the transition state J. Am. Chem. Soc. 120, 2703-2709
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 2703-2709
    • Hess, R.A.1    Hengge, A.C.2    Cleland, W.W.3
  • 22
    • 33846199962 scopus 로고    scopus 로고
    • Structure-activity analysis of base and enzyme-catalyzed 4-hydroxybenzoyl coenzyme A hydrolysis
    • Song, F., Zhuang, Z., and Dunaway-Mariano, D. (2007) Structure-activity analysis of base and enzyme-catalyzed 4-hydroxybenzoyl coenzyme A hydrolysis Bioorg. Chem. 35, 1-10
    • (2007) Bioorg. Chem. , vol.35 , pp. 1-10
    • Song, F.1    Zhuang, Z.2    Dunaway-Mariano, D.3
  • 23
    • 0037883296 scopus 로고    scopus 로고
    • Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU
    • Zhuang, Z., Gartemann, K. H., Eichenlaub, R., and Dunaway-Mariano, D. (2003) Characterization of the 4-hydroxybenzoyl-coenzyme A thioesterase from Arthrobacter sp. strain SU Appl. Environ. Microbiol. 69, 2707-2711
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 2707-2711
    • Zhuang, Z.1    Gartemann, K.H.2    Eichenlaub, R.3    Dunaway-Mariano, D.4
  • 24
    • 0035951110 scopus 로고    scopus 로고
    • Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis
    • Luo, L., Taylor, K. L, Xiang, H., Wei, Y., Zhang, W., and Dunaway-Mariano., D. (2001) Role of active site binding interactions in 4-chlorobenzoyl-coenzyme A dehalogenase catalysis Biochemistry 40, 15684-15692
    • (2001) Biochemistry , vol.40 , pp. 15684-15692
    • Luo, L.1    Taylor, K.L.2    Xiang, H.3    Wei, Y.4    Zhang, W.5    Dunaway-Mariano, D.6
  • 25
    • 0033659999 scopus 로고    scopus 로고
    • Raman difference spectroscopic studies of dithiobenzoyl substrate and product analogs binding to the enzyme dehologenase: Pi-electron polarization is prevented by C - O to C - S substitution
    • Dong, J., Luo, L., Liang, P., Dunaway-Mariano, D., and Carey, P. (2000) Raman difference spectroscopic studies of dithiobenzoyl substrate and product analogs binding to the enzyme dehologenase: pi-electron polarization is prevented by C - O to C - S substitution J. Raman Spectrosc. 31, 365-371
    • (2000) J. Raman Spectrosc. , vol.31 , pp. 365-371
    • Dong, J.1    Luo, L.2    Liang, P.3    Dunaway-Mariano, D.4    Carey, P.5
  • 26
    • 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
  • 28
    • 71549171706 scopus 로고    scopus 로고
    • Fitting enzyme kinetic data with KinTek Global Kinetic Explorer
    • Johnson, K. A. (2009) Fitting enzyme kinetic data with KinTek Global Kinetic Explorer Methods Enzymol. 467, 601-626
    • (2009) Methods Enzymol. , vol.467 , pp. 601-626
    • Johnson, K.A.1
  • 32
    • 64349123693 scopus 로고    scopus 로고
    • The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis
    • Cao, J., Xu, H., Zhao, H., Gong, W, and Dunaway-Mariano, D. (2009) The mechanisms of human hotdog-fold thioesterase 2 (hTHEM2) substrate recognition and catalysis illuminated by a structure and function based analysis Biochemistry 48, 1293-1304
    • (2009) Biochemistry , vol.48 , pp. 1293-1304
    • Cao, J.1    Xu, H.2    Zhao, H.3    Gong, W.4    Dunaway-Mariano, D.5
  • 33
    • 84856418868 scopus 로고    scopus 로고
    • A thioester substrate binds to the enzyme arthrobacter thioesterase in two ionization states; evidence from raman difference spectroscopy
    • Dong, J., Zhuang, Z., Song, F., Dunaway-Mariano, D., and Carey, P. R. (2012) A Thioester Substrate Binds to the Enzyme Arthrobacter Thioesterase in Two Ionization States; Evidence from Raman Difference Spectroscopy J. Raman Spectrosc. 43, 65-71
    • (2012) J. Raman Spectrosc. , vol.43 , pp. 65-71
    • Dong, J.1    Zhuang, Z.2    Song, F.3    Dunaway-Mariano, D.4    Carey, P.R.5
  • 35
    • 52449133104 scopus 로고    scopus 로고
    • Benzoyl-coenzyme A thioesterase of Azoarcus evansii: Properties and function
    • Ismail, W. (2008) Benzoyl-coenzyme A thioesterase of Azoarcus evansii: properties and function Arch. Microbiol. 190, 451-460
    • (2008) Arch. Microbiol. , vol.190 , pp. 451-460
    • Ismail, W.1
  • 36
    • 64349120214 scopus 로고    scopus 로고
    • Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: Substrate specificities and mutagenic studies on the active-site residues
    • Guo, Z. F., Sun, Y., Zheng, S., and Guo, Z. (2009) Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues Biochemistry 48, 1712-1722
    • (2009) Biochemistry , vol.48 , pp. 1712-1722
    • Guo, Z.F.1    Sun, Y.2    Zheng, S.3    Guo, Z.4
  • 37
    • 34948820655 scopus 로고    scopus 로고
    • In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH
    • Leduc, D., Battesti, A., and Bouveret, E. (2007) In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH J. Bacteriol. 189, 7112-7126
    • (2007) J. Bacteriol. , vol.189 , pp. 7112-7126
    • Leduc, D.1    Battesti, A.2    Bouveret, E.3
  • 38
    • 51549103286 scopus 로고    scopus 로고
    • A novel paradigm of fatty acid beta-oxidation exemplified by the thioesterase-dependent partial degradation of conjugated linoleic acid that fully supports growth of Escherichia coli
    • Nie, L., Ren, Y., Janakiraman, A., Smith, S., and Schulz, H. (2008) A novel paradigm of fatty acid beta-oxidation exemplified by the thioesterase-dependent partial degradation of conjugated linoleic acid that fully supports growth of Escherichia coli Biochemistry 47, 9618-9626
    • (2008) Biochemistry , vol.47 , pp. 9618-9626
    • Nie, L.1    Ren, Y.2    Janakiraman, A.3    Smith, S.4    Schulz, H.5
  • 39
    • 34248590375 scopus 로고    scopus 로고
    • Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence
    • Wang, F., Langley, R., Gulten, G., Wang, L., and Sacchettini, J. C. (2007) Identification of a type III thioesterase reveals the function of an operon crucial for Mtb virulence Chem. Biol. 14, 543-551
    • (2007) Chem. Biol. , vol.14 , pp. 543-551
    • Wang, F.1    Langley, R.2    Gulten, G.3    Wang, L.4    Sacchettini, J.C.5
  • 40
    • 33646568459 scopus 로고    scopus 로고
    • The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: A thioesterase confers resistance to fluoroacetyl-coenzyme A
    • Huang, F., Haydock, S. F., Spitelle, D., Mironenko, T, Li, T. L., O'Hagan, D., Leadlay, P. F., and Spencer, J. B. (2006) The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme A Chem. Biol. 13, 475-484
    • (2006) Chem. Biol. , vol.13 , pp. 475-484
    • Huang, F.1    Haydock, S.F.2    Spitelle, D.3    Mironenko, T.4    Li, T.L.5    O'Hagan, D.6    Leadlay, P.F.7    Spencer, J.B.8
  • 41
    • 77954575257 scopus 로고    scopus 로고
    • The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: A thioesterase confers resistance to fluoroacetyl-coenzyme A
    • Dias, M. V., Huang, F., Chirgadze, D. Y., Tosin, M., Spiteller, D., Dry, E. F., Leadlay, P. F., Spencer, J. B., and Blundell, T. L. (2010) The gene cluster for fluorometabolite biosynthesis in Streptomyces cattleya: a thioesterase confers resistance to fluoroacetyl-coenzyme A J. Biol. Chem. 285, 22495-22504
    • (2010) J. Biol. Chem. , vol.285 , pp. 22495-22504
    • Dias, M.V.1    Huang, F.2    Chirgadze, D.Y.3    Tosin, M.4    Spiteller, D.5    Dry, E.F.6    Leadlay, P.F.7    Spencer, J.B.8    Blundell, T.L.9
  • 42
    • 78049301731 scopus 로고    scopus 로고
    • Structural and biochemical studies of a fluoroacetyl-CoA-specific thioesterase reveal a molecular basis for fluorine selectivity
    • Weeks, A. M., Coyle, S. M., Jinek, M., Doudna, J. A., and Chang, M. C. (2010) Structural and biochemical studies of a fluoroacetyl-CoA-specific thioesterase reveal a molecular basis for fluorine selectivity Biochemistry 49, 9269-79
    • (2010) Biochemistry , vol.49 , pp. 9269-9279
    • Weeks, A.M.1    Coyle, S.M.2    Jinek, M.3    Doudna, J.A.4    Chang, M.C.5
  • 44
    • 0141958038 scopus 로고    scopus 로고
    • Divergent function in the crotonase superfamily: An anhydride intermediate in the reaction catalyzed by 3-hydroxyisobutyryl-CoA hydrolase
    • Wong, B. J. and Gerlt, J. A. (2003) Divergent function in the crotonase superfamily: an anhydride intermediate in the reaction catalyzed by 3-hydroxyisobutyryl-CoA hydrolase J. Am. Chem. Soc. 125, 12076-12077
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12076-12077
    • Wong, B.J.1    Gerlt, J.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.