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Volumn 19, Issue 2, 2000, Pages 235-245

Overexpression and biosynthetic deuterium enrichment of TEM-1 β-lactamase for structural characterization by magnetic resonance methods

Author keywords

[No Author keywords available]

Indexed keywords

BETAINE; CLONING VECTOR; CULTURE MEDIUM; GENE FUSION; GENE OVEREXPRESSION; GENETIC TRANSFORMATION; MOLECULAR CLONING; MUTANT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OMPA PROTEIN; PROTEIN INDUCTION; SUCROSE; TEM 1 BETA LACTAMASE;

EID: 0033937550     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2000.1243     Document Type: Article
Times cited : (34)

References (51)
  • 1
    • 0031595590 scopus 로고
    • 15N multidimensional NMR to study the structure and dynamics of proteins
    • 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct. 27:1988;367-406.
    • (1988) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 367-406
    • Gardner, K.H.1    Kay, L.E.2
  • 2
    • 0014012048 scopus 로고
    • Deuterated organisms: Cultivation and uses - Living organisms of unusual isotopic composition can be used for magnetic resonance studies
    • Katz J. J., Crespi H. L. Deuterated organisms: Cultivation and uses - Living organisms of unusual isotopic composition can be used for magnetic resonance studies. Science. 151:1966;1187-1194.
    • (1966) Science , vol.151 , pp. 1187-1194
    • Katz, J.J.1    Crespi, H.L.2
  • 3
    • 0030589110 scopus 로고    scopus 로고
    • Use of deuterium labeling in NMR: Overcoming a sizeable problem
    • Sattler M., Fesik S. W. Use of deuterium labeling in NMR: Overcoming a sizeable problem. Structure. 4:1996;1245-1249.
    • (1996) Structure , vol.4 , pp. 1245-1249
    • Sattler, M.1    Fesik, S.W.2
  • 4
    • 0001258823 scopus 로고
    • Isotope labeling in solution: Protein labeling and structure analysis
    • LeMaster D. M. Isotope labeling in solution: Protein labeling and structure analysis. Prog. NMR Spectrosc. 26:1994;371-419.
    • (1994) Prog. NMR Spectrosc. , vol.26 , pp. 371-419
    • Lemaster, D.M.1
  • 6
    • 0028136596 scopus 로고
    • Structure at the active site of an acylenzyme of α-chymotrypsin and implications for the catalytic mechanism: An electron nuclear double resonance study
    • Wells G. B., Mustafi D., Makinen M. W. Structure at the active site of an acylenzyme of α-chymotrypsin and implications for the catalytic mechanism: An electron nuclear double resonance study. J. Biol. Chem. 269:1994;4577-4586.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4577-4586
    • Wells, G.B.1    Mustafi, D.2    Makinen, M.W.3
  • 7
    • 0028111532 scopus 로고
    • Catalytic conformation of carboxypeptidase A: Structure of a true enzyme reaction intermediate determined by electron nuclear double resonance
    • Mustafi D., Makinen M. W. Catalytic conformation of carboxypeptidase A: Structure of a true enzyme reaction intermediate determined by electron nuclear double resonance. J. Biol. Chem. 269:1994;4587-4595.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4587-4595
    • Mustafi, D.1    Makinen, M.W.2
  • 8
    • 0032242182 scopus 로고    scopus 로고
    • Electron nuclear double resonance determined structures of enzyme reaction intermediates: Structural evidence for substrate destabilization
    • Makinen M. W. Electron nuclear double resonance determined structures of enzyme reaction intermediates: Structural evidence for substrate destabilization. Spectrochim. Acta Ser. A. 54:1998;2269-2281.
    • (1998) Spectrochim. Acta Ser. a , vol.54 , pp. 2269-2281
    • Makinen, M.W.1
  • 10
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F. W., Moffat B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffat, B.A.2
  • 12
    • 0031259782 scopus 로고    scopus 로고
    • Optimized gene synthesis, high level expression, isotopic enrichment, and refolding of human interleukin-5
    • Metha D. V., Di Gate R. J., Banville D. L., Guiles R. D. Optimized gene synthesis, high level expression, isotopic enrichment, and refolding of human interleukin-5. Protein Express. Purif. 11:1997;86-94.
    • (1997) Protein Express. Purif. , vol.11 , pp. 86-94
    • Metha, D.V.1    Di Gate, R.J.2    Banville, D.L.3    Guiles, R.D.4
  • 13
    • 0029310455 scopus 로고
    • High-level expression and isotope labeling of Lactobacillus casei dihydrofolate reducatase for nuclear magnetic resonance spectroscopy
    • Badii R., Baiam J., Casarotto M. G., Roberts G. C. K. High-level expression and isotope labeling of Lactobacillus casei dihydrofolate reducatase for nuclear magnetic resonance spectroscopy. Protein Express. Purif. 6:1995;237-243.
    • (1995) Protein Express. Purif. , vol.6 , pp. 237-243
    • Badii, R.1    Baiam, J.2    Casarotto, M.G.3    Roberts, G.C.K.4
  • 16
    • 0025123399 scopus 로고
    • Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli
    • Bowden G. A., Georgiou G. Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli. J. Biol. Chem. 265:1990;16760-16766.
    • (1990) J. Biol. Chem. , vol.265 , pp. 16760-16766
    • Bowden, G.A.1    Georgiou, G.2
  • 17
    • 0027669539 scopus 로고
    • Molecular characterization of protein inclusion bodies in Escherichia coli. 1. Composition
    • Valax P., Georgiou G. Molecular characterization of protein inclusion bodies in Escherichia coli. 1. Composition. Biotechnol. Prog. 9:1993;539-547.
    • (1993) Biotechnol. Prog. , vol.9 , pp. 539-547
    • Valax, P.1    Georgiou, G.2
  • 18
    • 0021329693 scopus 로고
    • The functional origin of bacteriophage f1 DNA replication: Its signals and domains
    • Dotto G. P., Horiuchi K., Zinder N. D. The functional origin of bacteriophage f1 DNA replication: Its signals and domains. J. Mol. Biol. 172:1984;507-521.
    • (1984) J. Mol. Biol. , vol.172 , pp. 507-521
    • Dotto, G.P.1    Horiuchi, K.2    Zinder, N.D.3
  • 19
    • 85031580885 scopus 로고
    • Site-directed mutagenesis using the Altered Sites® II systems
    • Lesley S. A., Bohnsack R. N. Site-directed mutagenesis using the Altered Sites® II systems. Promega Notes Magazine. 46:1994;6-10.
    • (1994) Promega Notes Magazine , vol.46 , pp. 6-10
    • Lesley, S.A.1    Bohnsack, R.N.2
  • 21
    • 0025801845 scopus 로고
    • Site-directed mutants, at position 166, of RTEM-1 β-lactamase that form an stable acyl-enzyme intermediate with penicillin
    • Adachi H., Otha T., Matsuzawa H. Site-directed mutants, at position 166, of RTEM-1 β-lactamase that form an stable acyl-enzyme intermediate with penicillin. J. Biol. Chem. 266:1991;3186-3191.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3186-3191
    • Adachi, H.1    Otha, T.2    Matsuzawa, H.3
  • 23
    • 0024520745 scopus 로고
    • Site directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S. N., Hunt H. D., Horton R. M., Pullen J. K., Pease L. R. Site directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:1989;51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 24
    • 0026327753 scopus 로고
    • A novel strategy for production of a highly expressed recombinant protein in an active form
    • Blackwell J. R., Horgan R. A novel strategy for production of a highly expressed recombinant protein in an active form. FEBS Lett. 295:1991;10-12.
    • (1991) FEBS Lett. , vol.295 , pp. 10-12
    • Blackwell, J.R.1    Horgan, R.2
  • 25
    • 0001305955 scopus 로고
    • Improved mass accuracy in matrix-assisted laser desorption ionization time-of-flight mass spectrometry of peptides
    • Vorm O., Mann M. Improved mass accuracy in matrix-assisted laser desorption ionization time-of-flight mass spectrometry of peptides. J. Am. Soc. Mass. Spectrom. 5:1994;955-958.
    • (1994) J. Am. Soc. Mass. Spectrom. , vol.5 , pp. 955-958
    • Vorm, O.1    Mann, M.2
  • 28
    • 0017929007 scopus 로고
    • Cryostat for enzymology in the subzero temperature range
    • Churg A. K., Gibson G., Makinen M. W. Cryostat for enzymology in the subzero temperature range. Rev. Sci. Instrum. 49:1978;212-214.
    • (1978) Rev. Sci. Instrum. , vol.49 , pp. 212-214
    • Churg, A.K.1    Gibson, G.2    Makinen, M.W.3
  • 29
    • 0018800254 scopus 로고
    • Catalytic role of the metal ion of carboxypeptidase A in ester hydrolysis
    • Makinen M. W., Kuo L. C., Dymowski J. J., Jaffer S. Catalytic role of the metal ion of carboxypeptidase A in ester hydrolysis. J. Biol. Chem. 254:1979;356-366.
    • (1979) J. Biol. Chem. , vol.254 , pp. 356-366
    • Makinen, M.W.1    Kuo, L.C.2    Dymowski, J.J.3    Jaffer, S.4
  • 30
    • 0025824637 scopus 로고
    • 2+-reconstituted horse liver alcohol dehydrogenase: A mechanistic probe for the assignment of metal-linked ionizations
    • 2+-reconstituted horse liver alcohol dehydrogenase: A mechanistic probe for the assignment of metal-linked ionizations. J. Biol. Chem. 266:1991;20636-20644.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20636-20644
    • Maret, W.1    Makinen, M.W.2
  • 31
    • 0029069920 scopus 로고
    • Structure, conformation, and probable mechanism of hydrolysis of a spin-labeled penicillin revealed by electron nuclear double resonance spectroscopy
    • Mustafi D., Makinen M. W. Structure, conformation, and probable mechanism of hydrolysis of a spin-labeled penicillin revealed by electron nuclear double resonance spectroscopy. J. Am. Chem. Soc. 117:1995;6739-6746.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6739-6746
    • Mustafi, D.1    Makinen, M.W.2
  • 32
    • 0019164846 scopus 로고
    • β-Lactamase proceeds via an acyl-enzyme intermediate: Interaction of the Escherichia coli RTEM enzyme with cefoxitin
    • Fisher J., Belasco J. G., Khosla S., Knowles J. R. β-Lactamase proceeds via an acyl-enzyme intermediate: Interaction of the Escherichia coli RTEM enzyme with cefoxitin. Biochemistry. 19:1980;2895-2901.
    • (1980) Biochemistry , vol.19 , pp. 2895-2901
    • Fisher, J.1    Belasco, J.G.2    Khosla, S.3    Knowles, J.R.4
  • 34
    • 0028900778 scopus 로고
    • Substitution of asp for asn at position 132 in the active site of TEM β-lactamase
    • Osuna J., Viadiu H., Fink A. L., Soberon X. Substitution of asp for asn at position 132 in the active site of TEM β-lactamase. J. Biol. Chem. 270:1995;775-780.
    • (1995) J. Biol. Chem. , vol.270 , pp. 775-780
    • Osuna, J.1    Viadiu, H.2    Fink, A.L.3    Soberon, X.4
  • 36
    • 0001736137 scopus 로고
    • NMR and ENDOR conformational studies of the vanadyl guanosine 5′-monophosphate complex in hydrogen-bonded quartet assemblies
    • Jiang F. S., Makinen M. W. NMR and ENDOR conformational studies of the vanadyl guanosine 5′-monophosphate complex in hydrogen-bonded quartet assemblies. Inorg. Chem. 34:1995;1736-1744.
    • (1995) Inorg. Chem. , vol.34 , pp. 1736-1744
    • Jiang, F.S.1    Makinen, M.W.2
  • 37
    • 0028028398 scopus 로고
    • Characterization of calcium binding sites in the kidney stone inhibitor glycoprotein nephrocalcin with vanadyl ions using EPR and ENDOR spectroscopy
    • Mustafi D., Nakagawa Y. Characterization of calcium binding sites in the kidney stone inhibitor glycoprotein nephrocalcin with vanadyl ions using EPR and ENDOR spectroscopy. Proc. Natl. Acad. Sci. USA. 91:1994;11323-11327.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11323-11327
    • Mustafi, D.1    Nakagawa, Y.2
  • 39
    • 0031026028 scopus 로고    scopus 로고
    • Kinetic and thermodynamic consequences of the removal of the Cys77-Cys123 disulfide bond for the folding of TEM-1 β-lactamase
    • Vanhove M., Guillaume G., Ledent P., Richards J. H., Pain R. H., Frère J. M. Kinetic and thermodynamic consequences of the removal of the Cys77-Cys123 disulfide bond for the folding of TEM-1 β-lactamase. Biochem. J. 321:1997;413-417.
    • (1997) Biochem. J. , vol.321 , pp. 413-417
    • Vanhove, M.1    Guillaume, G.2    Ledent, P.3    Richards, J.H.4    Pain, R.H.5    Frère, J.M.6
  • 40
    • 0029962946 scopus 로고    scopus 로고
    • Amino acid sequence determinants of β-lactamase structure and activity
    • Huang W., Petrosino J., Hirsh M., Shenkin P. S., Palzkill T. Amino acid sequence determinants of β-lactamase structure and activity. J. Mol. Biol. 258:1996;688-703.
    • (1996) J. Mol. Biol. , vol.258 , pp. 688-703
    • Huang, W.1    Petrosino, J.2    Hirsh, M.3    Shenkin, P.S.4    Palzkill, T.5
  • 41
    • 0022467352 scopus 로고
    • Active-site mutants of β-lactamase: Use of an inactive double mutant to study requirements for catalysis
    • Dalbie-McFarland G., Neitzel J. J., Richards J. H. Active-site mutants of β-lactamase: Use of an inactive double mutant to study requirements for catalysis. Biochemistry. 25:1986;332-338.
    • (1986) Biochemistry , vol.25 , pp. 332-338
    • Dalbie-McFarland, G.1    Neitzel, J.J.2    Richards, J.H.3
  • 42
    • 0024279223 scopus 로고
    • Release of periplasmic enzymes and other physiological effects of β-lactamase overproduction in Escherichia coli
    • Georgiou G., Schuler M. L., Wilson D. B. Release of periplasmic enzymes and other physiological effects of β-lactamase overproduction in Escherichia coli. Biotech. Bioeng. 32:1988;741-748.
    • (1988) Biotech. Bioeng. , vol.32 , pp. 741-748
    • Georgiou, G.1    Schuler, M.L.2    Wilson, D.B.3
  • 43
    • 0026086673 scopus 로고
    • Ragged N-termini and other variants of class A β-lactamases
    • Matagne A., Joris B., Van Beeumen J., Frère J. M. Ragged N-termini and other variants of class A β-lactamases. Biochem. J. 273:1991;503-510.
    • (1991) Biochem. J. , vol.273 , pp. 503-510
    • Matagne, A.1    Joris, B.2    Van Beeumen, J.3    Frère, J.M.4
  • 45
    • 0028170640 scopus 로고
    • TEM β-lactamase mutants hydrolyzing third-generation cephalosporins: A kinetic and molecular modeling analysis
    • Raquet X., Lamotte-Brasseur J., Fonze E., Goussard S., Courvalin P., Frère J. M. TEM β-lactamase mutants hydrolyzing third-generation cephalosporins: A kinetic and molecular modeling analysis. J. Mol. Biol. 244:1994;625-639.
    • (1994) J. Mol. Biol. , vol.244 , pp. 625-639
    • Raquet, X.1    Lamotte-Brasseur, J.2    Fonze, E.3    Goussard, S.4    Courvalin, P.5    Frère, J.M.6
  • 46
    • 0031585682 scopus 로고    scopus 로고
    • Conformational changes in spin-labeled cephalosporin and penicillin upon hydrolysis revealed by electron nuclear double resonance spectroscopy
    • Mustafi D., Knock M. M., Shaw R. W., Makinen M. W. Conformational changes in spin-labeled cephalosporin and penicillin upon hydrolysis revealed by electron nuclear double resonance spectroscopy. J. Am. Chem. Soc. 119:1997;12619-12628.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12619-12628
    • Mustafi, D.1    Knock, M.M.2    Shaw, R.W.3    Makinen, M.W.4
  • 47
    • 0020490170 scopus 로고
    • Isolation of a covalent intermediate in β-lactamase I catalysis
    • Cartwright S. J., Fink A. L. Isolation of a covalent intermediate in β-lactamase I catalysis. FEBS Lett. 137:1982;186-188.
    • (1982) FEBS Lett. , vol.137 , pp. 186-188
    • Cartwright, S.J.1    Fink, A.L.2
  • 48
    • 0024467115 scopus 로고
    • Trapping the acyl-enzyme intermediate in β-lactamase I catalysis
    • Cartwright S. J., Tan A. K., Fink A. L. Trapping the acyl-enzyme intermediate in β-lactamase I catalysis. Biochem. J. 263:1989;905-912.
    • (1989) Biochem. J. , vol.263 , pp. 905-912
    • Cartwright, S.J.1    Tan, A.K.2    Fink, A.L.3
  • 49
    • 0025022038 scopus 로고
    • Cryoenzymology of staphylococcal β-lactamase: Trapping a serine-70-linked acyl-enzyme
    • Virden R., Tan A. K., Fink A. L. Cryoenzymology of staphylococcal β-lactamase: Trapping a serine-70-linked acyl-enzyme. Biochemistry. 29:1990;145-153.
    • (1990) Biochemistry , vol.29 , pp. 145-153
    • Virden, R.1    Tan, A.K.2    Fink, A.L.3
  • 50
    • 0001203676 scopus 로고
    • The effective dipolar position of the unpaired electron of nitoxyl spin-labels defined by ENDOR spectroscopy
    • Mustafi D., Joela H., Makinen M. W. The effective dipolar position of the unpaired electron of nitoxyl spin-labels defined by ENDOR spectroscopy. J. Magn. Reson. 91:1991;497-504.
    • (1991) J. Magn. Reson. , vol.91 , pp. 497-504
    • Mustafi, D.1    Joela, H.2    Makinen, M.W.3


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