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Volumn 13, Issue 9, 2006, Pages 929-936

Replacement Surgery with Unnatural Amino Acids in the Lock-and-Key Joint of Glutathione Transferase Subunits

Author keywords

[No Author keywords available]

Indexed keywords

1 IODOBUTANE; 1-IODOBUTANE; BUTANE; CYSTEINE; GLUTATHIONE TRANSFERASE P1; GSTP1 PROTEIN, HUMAN; IODINATED HYDROCARBON; METHYL IODIDE; TYROSINE;

EID: 33748554496     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2006.07.005     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 0024269217 scopus 로고
    • Glutathione transferases-structure and catalytic activity
    • Mannervik B., and Danielson U.H. Glutathione transferases-structure and catalytic activity. CRC Crit. Rev. Biochem. 23 (1988) 283-337
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 2
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong R.N. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem. Res. Toxicol. 10 (1997) 2-18
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 4
    • 0033985179 scopus 로고    scopus 로고
    • The hydrophobic lock-and-key intersubunit motif of glutathione transferase A1-1: implications for catalysis, ligandin function and stability
    • Sayed Y., Wallace L.A., and Dirr H.W. The hydrophobic lock-and-key intersubunit motif of glutathione transferase A1-1: implications for catalysis, ligandin function and stability. FEBS Lett. 465 (2000) 169-172
    • (2000) FEBS Lett. , vol.465 , pp. 169-172
    • Sayed, Y.1    Wallace, L.A.2    Dirr, H.W.3
  • 5
    • 1642286478 scopus 로고    scopus 로고
    • Subunit interface residues of glutathione S-transferase A1-1 that are important in the monomer-dimer equilibrium
    • Vargo M.A., Nguyen L., and Colman R.F. Subunit interface residues of glutathione S-transferase A1-1 that are important in the monomer-dimer equilibrium. Biochemistry 43 (2004) 3327-3335
    • (2004) Biochemistry , vol.43 , pp. 3327-3335
    • Vargo, M.A.1    Nguyen, L.2    Colman, R.F.3
  • 6
    • 2242443511 scopus 로고    scopus 로고
    • Molecular recognition at the dimer interface of a class mu glutathione transferase: role of a hydrophobic interaction motif in dimer stability and protein function
    • Hornby J.A., Codreanu S.G., Armstrong R.N., and Dirr H.W. Molecular recognition at the dimer interface of a class mu glutathione transferase: role of a hydrophobic interaction motif in dimer stability and protein function. Biochemistry 41 (2002) 14238-14247
    • (2002) Biochemistry , vol.41 , pp. 14238-14247
    • Hornby, J.A.1    Codreanu, S.G.2    Armstrong, R.N.3    Dirr, H.W.4
  • 7
    • 0034728774 scopus 로고    scopus 로고
    • Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function
    • Stenberg G., Abdalla A.M., and Mannervik B. Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function. Biochem. Biophys. Res. Commun. 271 (2000) 59-63
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 59-63
    • Stenberg, G.1    Abdalla, A.M.2    Mannervik, B.3
  • 8
    • 0026722795 scopus 로고
    • Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution
    • Reinemer P., Dirr H.W., Ladenstein R., Huber R., Lo Bello M., Federici G., and Parker M.W. Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. J. Mol. Biol. 227 (1992) 214-226
    • (1992) J. Mol. Biol. , vol.227 , pp. 214-226
    • Reinemer, P.1    Dirr, H.W.2    Ladenstein, R.3    Huber, R.4    Lo Bello, M.5    Federici, G.6    Parker, M.W.7
  • 9
    • 0028218792 scopus 로고
    • Molecular structure at 1.8 Å of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors
    • Garcia-Saez I., Parraga A., Phillips M.F., Mantle T.J., and Coll M. Molecular structure at 1.8 Å of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors. J. Mol. Biol. 237 (1994) 298-314
    • (1994) J. Mol. Biol. , vol.237 , pp. 298-314
    • Garcia-Saez, I.1    Parraga, A.2    Phillips, M.F.3    Mantle, T.J.4    Coll, M.5
  • 10
    • 1542304694 scopus 로고    scopus 로고
    • Functional role of the lock and key motif at the subunit interface of glutathione transferase P1-1
    • Hegazy U.M., Mannervik B., and Stenberg G. Functional role of the lock and key motif at the subunit interface of glutathione transferase P1-1. J. Biol. Chem. 279 (2004) 9586-9596
    • (2004) J. Biol. Chem. , vol.279 , pp. 9586-9596
    • Hegazy, U.M.1    Mannervik, B.2    Stenberg, G.3
  • 12
    • 0033516322 scopus 로고    scopus 로고
    • Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of cysteine mutants
    • Plettner E., DeSantis G., Stabile M.R., and Jones J.B. Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of cysteine mutants. J. Am. Chem. Soc. 121 (1999) 4977-4981
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 4977-4981
    • Plettner, E.1    DeSantis, G.2    Stabile, M.R.3    Jones, J.B.4
  • 13
    • 0024973018 scopus 로고
    • Generation of a catalytic sequence-specific hybrid Dnase
    • Corey D.R., Pei D., and Schultz P.G. Generation of a catalytic sequence-specific hybrid Dnase. Biochemistry 28 (1989) 8277-8286
    • (1989) Biochemistry , vol.28 , pp. 8277-8286
    • Corey, D.R.1    Pei, D.2    Schultz, P.G.3
  • 14
    • 0027269748 scopus 로고
    • Transforming the Escherichia coli Trp repressor into a site-specific nuclease
    • Sutton C.L., Mazumder A., Chen C.H., and Sigman D.S. Transforming the Escherichia coli Trp repressor into a site-specific nuclease. Biochemistry 32 (1993) 4225-4230
    • (1993) Biochemistry , vol.32 , pp. 4225-4230
    • Sutton, C.L.1    Mazumder, A.2    Chen, C.H.3    Sigman, D.S.4
  • 15
    • 0032496408 scopus 로고    scopus 로고
    • Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105
    • Johansson A.-S., Stenberg G., Widersten W., and Mannervik B. Structure-activity relationships and thermal stability of human glutathione transferase P1-1 governed by the H-site residue 105. J. Mol. Biol. 278 (1998) 687-698
    • (1998) J. Mol. Biol. , vol.278 , pp. 687-698
    • Johansson, A.-S.1    Stenberg, G.2    Widersten, W.3    Mannervik, B.4
  • 17
    • 0037428005 scopus 로고    scopus 로고
    • Unnatural amino acid mutagenesis of green fluorescent protein
    • Wang L., Xie J., Deniz A.A., and Schultz P.G. Unnatural amino acid mutagenesis of green fluorescent protein. J. Org. Chem. 68 (2003) 174-176
    • (2003) J. Org. Chem. , vol.68 , pp. 174-176
    • Wang, L.1    Xie, J.2    Deniz, A.A.3    Schultz, P.G.4
  • 20
    • 0024403619 scopus 로고
    • High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis
    • Cunningham B.C., and Wells J.A. High-resolution epitope mapping of hGH-receptor interactions by alanine-scanning mutagenesis. Science 244 (1989) 1081-1085
    • (1989) Science , vol.244 , pp. 1081-1085
    • Cunningham, B.C.1    Wells, J.A.2
  • 21
    • 0027289570 scopus 로고
    • Cysteine scanning mutagenesis of putative transmembrane helices IX and X in the lactose permease of Escherichia coli
    • Sahin-Toth M., and Kaback H.R. Cysteine scanning mutagenesis of putative transmembrane helices IX and X in the lactose permease of Escherichia coli. Protein Sci. 2 (1993) 1024-1033
    • (1993) Protein Sci. , vol.2 , pp. 1024-1033
    • Sahin-Toth, M.1    Kaback, H.R.2
  • 23
    • 0032508478 scopus 로고    scopus 로고
    • Probing pore topology and conformational changes of Kir2.1 potassium channels by cysteine scanning mutagenesis
    • Kubo Y., Yoshimichi M., and Heinemann S.H. Probing pore topology and conformational changes of Kir2.1 potassium channels by cysteine scanning mutagenesis. FEBS Lett. 435 (1998) 69-73
    • (1998) FEBS Lett. , vol.435 , pp. 69-73
    • Kubo, Y.1    Yoshimichi, M.2    Heinemann, S.H.3
  • 25
    • 0035628934 scopus 로고    scopus 로고
    • Enzyme design by chemical modification of protein scaffolds
    • Tann C.M., Qi D., and Distefano M.D. Enzyme design by chemical modification of protein scaffolds. Curr. Opin. Chem. Biol. 5 (2001) 696-704
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 696-704
    • Tann, C.M.1    Qi, D.2    Distefano, M.D.3
  • 26
    • 0035471137 scopus 로고    scopus 로고
    • Generation of new enzymes via covalent modification of existing proteins
    • Qi D., Tann C.M., Haring D., and Distefano M.D. Generation of new enzymes via covalent modification of existing proteins. Chem. Rev. 101 (2001) 3081-3111
    • (2001) Chem. Rev. , vol.101 , pp. 3081-3111
    • Qi, D.1    Tann, C.M.2    Haring, D.3    Distefano, M.D.4
  • 28
    • 0026513368 scopus 로고
    • Design of two chimaeric human-rat class alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties
    • Björnestedt R., Widersten M., Board P.G., and Mannervik B. Design of two chimaeric human-rat class alpha glutathione transferases for probing the contribution of C-terminal segments of protein structure to the catalytic properties. Biochem. J. 282 (1992) 505-510
    • (1992) Biochem. J. , vol.282 , pp. 505-510
    • Björnestedt, R.1    Widersten, M.2    Board, P.G.3    Mannervik, B.4
  • 29
    • 0029310535 scopus 로고
    • High-level bacterial expression of human glutathione transferase P1-1 encoded by semisynthetic DNA
    • Kolm R.H., Stenberg G., Widersten M., and Mannervik B. High-level bacterial expression of human glutathione transferase P1-1 encoded by semisynthetic DNA. Protein Expr. Purif. 6 (1995) 265-271
    • (1995) Protein Expr. Purif. , vol.6 , pp. 265-271
    • Kolm, R.H.1    Stenberg, G.2    Widersten, M.3    Mannervik, B.4
  • 31
    • 0033643558 scopus 로고    scopus 로고
    • Sample preparation by SDS/PAGE and in-gel digestion
    • Hellman U. Sample preparation by SDS/PAGE and in-gel digestion. EXS 88 (2000) 43-54
    • (2000) EXS , vol.88 , pp. 43-54
    • Hellman, U.1
  • 32
    • 0035543071 scopus 로고    scopus 로고
    • A novel multifunctional labeling reagent for enhanced protein characterization with mass spectrometry
    • Peters E., Horn D., Tully D., and Brock A. A novel multifunctional labeling reagent for enhanced protein characterization with mass spectrometry. Rapid Commun. Mass Spectrom. 15 (2001) 2387-2392
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 2387-2392
    • Peters, E.1    Horn, D.2    Tully, D.3    Brock, A.4
  • 33
    • 0036383921 scopus 로고    scopus 로고
    • Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector
    • Hellman U., and Bhikhabhai R. Easy amino acid sequencing of sulfonated peptides using post-source decay on a matrix-assisted laser desorption/ionization time-of-flight mass spectrometer equipped with a variable voltage reflector. Rapid Commun. Mass Spectrom. 16 (2002) 1851-1859
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 1851-1859
    • Hellman, U.1    Bhikhabhai, R.2
  • 34
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 35
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 33748577156 scopus 로고    scopus 로고
    • Bardsley, W.G. (2006). Simfit (http://www.simfit.man.ac.uk/).
  • 37
    • 0141648082 scopus 로고    scopus 로고
    • The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution
    • Oakley A.J., Lo Bello M., Battistoni A., Ricci G., Rossjohn J., Villar H.O., and Parker M.W. The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution. J. Mol. Biol. 274 (1997) 84-100
    • (1997) J. Mol. Biol. , vol.274 , pp. 84-100
    • Oakley, A.J.1    Lo Bello, M.2    Battistoni, A.3    Ricci, G.4    Rossjohn, J.5    Villar, H.O.6    Parker, M.W.7


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