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Volumn 252, Issue 3, 1998, Pages 447-457

Comparative study of the catalytic domain of phosphorylating glyceraldehyde-3-phosphate dehydrogenases from bacteria and archaea via essential cysteine probes and site-directed mutagenesis

Author keywords

Archaea; Base catalyst; Glyceraldehyde 3 phosphate dehydrogenase; Hydride transfer; Thiol reactivity

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

EID: 0032521628     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2520447.x     Document Type: Article
Times cited : (58)

References (56)
  • 1
    • 63849332835 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase
    • (Boyer, P. D., ed.) Academic Press, New York
    • Harris, J. I. & Waters, M. (1976) Glyceraldehyde-3-phosphate dehydrogenase, in The enzymes (Boyer, P. D., ed.) vol. 13, pp. 1-49, Academic Press, New York.
    • (1976) The Enzymes , vol.13 , pp. 1-49
    • Harris, J.I.1    Waters, M.2
  • 3
    • 0016772655 scopus 로고
    • Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase
    • Moras, D., Olsen, K. W., Sabesan, M. N., Buehner, M. Ford, G. C. & Rossmann, M. G. (1975) Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem. 250, 9137-9162.
    • (1975) J. Biol. Chem. , vol.250 , pp. 9137-9162
    • Moras, D.1    Olsen, K.W.2    Sabesan, M.N.3    Buehner, M.4    Ford, G.C.5    Rossmann, M.G.6
  • 4
    • 0023644310 scopus 로고
    • Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution
    • Skarzynski, T., Moody, P. C. E. & Wonacott, A. J. (1987) Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution, J. Mol. Biol. 193, 171-187.
    • (1987) J. Mol. Biol. , vol.193 , pp. 171-187
    • Skarzynski, T.1    Moody, P.C.E.2    Wonacott, A.J.3
  • 5
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer, I., Steipe, B., Huber, R., Tomschy, A. & Jaenicke, R. (1995) The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution, J. Mol. Biol. 246, 511-521.
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 6
    • 0038058016 scopus 로고    scopus 로고
    • Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde-3-phosphate dehydrogenases: Implication for NAD binding and cooperatively
    • Duée, E., Olivier-Deyris, L., Fanchon, E., Corbier, C., Branlant, G. & Dideberg, O. (1996) Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde-3-phosphate dehydrogenases: implication for NAD binding and cooperatively, J. Mol. Biol. 257, 814-838.
    • (1996) J. Mol. Biol. , vol.257 , pp. 814-838
    • Duée, E.1    Olivier-Deyris, L.2    Fanchon, E.3    Corbier, C.4    Branlant, G.5    Dideberg, O.6
  • 7
    • 0027383390 scopus 로고
    • Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: Role of the acidic residue in the fingerprint region of the micleotide binding fold
    • Clermont, S., Corbier, C., Mely, Y., Gerard, D., Wonacott, A. & Branlant, G. (1993) Determinants of coenzyme specificity in glyceraldehyde-3-phosphate dehydrogenase: role of the acidic residue in the fingerprint region of the micleotide binding fold, Biochemistry 32, 10 178-10 184.
    • (1993) Biochemistry , vol.32 , pp. 10178-10184
    • Clermont, S.1    Corbier, C.2    Mely, Y.3    Gerard, D.4    Wonacott, A.5    Branlant, G.6
  • 8
    • 0028203761 scopus 로고
    • Characterization of the two anion-recognition sites of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus by site-directed mutagenesis and chemical modification
    • Corbier, C., Michels, S., Wonacott, A. J. & Branlant, G. (1994) Characterization of the two anion-recognition sites of glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus by site-directed mutagenesis and chemical modification, Biochemistry 33, 3260-3265.
    • (1994) Biochemistry , vol.33 , pp. 3260-3265
    • Corbier, C.1    Michels, S.2    Wonacott, A.J.3    Branlant, G.4
  • 9
    • 0030053020 scopus 로고    scopus 로고
    • Phosphate binding sites in phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Michels, S., Rogalska, A. & Branlant, G. (1996) Phosphate binding sites in phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus, Eur. J. Biochem. 235, 641-647.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 641-647
    • Michels, S.1    Rogalska, A.2    Branlant, G.3
  • 11
    • 0023717499 scopus 로고
    • Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Skarzynski, T. & Wonacott, A. J. (1988) Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus, J. Mol. Biol. 203, 1097-1118.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1097-1118
    • Skarzynski, T.1    Wonacott, A.J.2
  • 12
    • 0027966874 scopus 로고
    • The double catalytic triad, Cys25-His159-Asp15X and Cys25-His159-Asn175, in papain catalysis: Role of Asp158 and Asn175
    • Wang, J., Xiang, Y. F. & Lim, C. (1994) The double catalytic triad, Cys25-His159-Asp15X and Cys25-His159-Asn175, in papain catalysis: role of Asp158 and Asn175, Protein Eng. 7, 75-82.
    • (1994) Protein Eng. , vol.7 , pp. 75-82
    • Wang, J.1    Xiang, Y.F.2    Lim, C.3
  • 13
    • 0023901879 scopus 로고
    • Primary structure of glyceraldehyde-3-phosphate dehydrogenase deduced from the nucleotide sequence of the thermophilic archaebacterium Methanothermus fervidus
    • Fabry, S. & Hensel, R. (1988) Primary structure of glyceraldehyde-3-phosphate dehydrogenase deduced from the nucleotide sequence of the thermophilic archaebacterium Methanothermus fervidus, Gene (Amst.) 64, 189-197.
    • (1988) Gene (Amst.) , vol.64 , pp. 189-197
    • Fabry, S.1    Hensel, R.2
  • 14
    • 0027377307 scopus 로고
    • Nucleotide sequence and molecular evolution of the gene coding for glyceraldehyde-3-phosphate dehydrogenase in the thermoacidophilic Archaebacterium Sulfolobus solfataricus
    • Arcari, P., Dello Russo, A., Ianniciello, G., Gallo, M. & Bocchini, V. (1993) Nucleotide sequence and molecular evolution of the gene coding for glyceraldehyde-3-phosphate dehydrogenase in the thermoacidophilic Archaebacterium Sulfolobus solfataricus, Biochem. Genet. 31, 241-251.
    • (1993) Biochem. Genet. , vol.31 , pp. 241-251
    • Arcari, P.1    Dello Russo, A.2    Ianniciello, G.3    Gallo, M.4    Bocchini, V.5
  • 15
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannashii
    • Bult, C. J. et al. (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannashii, Science 273, 1058-1073.
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 16
    • 0024555940 scopus 로고
    • Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis
    • Soukri, A., Mougin, A., Corbier, C., Wonacott, A. J., Branlant, C. & Branlant, G. (1989) Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis, Biochemistry 28, 2586-2592.
    • (1989) Biochemistry , vol.28 , pp. 2586-2592
    • Soukri, A.1    Mougin, A.2    Corbier, C.3    Wonacott, A.J.4    Branlant, C.5    Branlant, G.6
  • 17
    • 0023996184 scopus 로고
    • Use of site-directed mutagenesis to probe the role of Cys149 in the formation of charge-transfer transition in glyceraldehyde-3-phosphate dehydrogenase
    • Mougin, A., Corhier, C., Soukri, A., Wonacott, A., Branlant, C. & Branlant, G. (1988) Use of site-directed mutagenesis to probe the role of Cys149 in the formation of charge-transfer transition in glyceraldehyde-3-phosphate dehydrogenase, Protein Eng. 2, 45-48.
    • (1988) Protein Eng. , vol.2 , pp. 45-48
    • Mougin, A.1    Corhier, C.2    Soukri, A.3    Wonacott, A.4    Branlant, C.5    Branlant, G.6
  • 18
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracyl-containing DNA
    • Kunkel, T. A., Bebenek, K. & McClary, J. (1991) Efficient site-directed mutagenesis using uracyl-containing DNA, in Methods Enzymol. 204, 125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assemhly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assemhly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0025328922 scopus 로고
    • Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenase by site-directed mutagenesis
    • Corbier, C., Clermont, S., Billard, P., Skarzynski, T., Branlant, C., Wonacott, A. & Branlant, G. (1990) Probing the coenzyme specificity of glyceraldehyde-3-phosphate dehydrogenase by site-directed mutagenesis, Biochemistry 29, 7101-7106.
    • (1990) Biochemistry , vol.29 , pp. 7101-7106
    • Corbier, C.1    Clermont, S.2    Billard, P.3    Skarzynski, T.4    Branlant, C.5    Wonacott, A.6    Branlant, G.7
  • 23
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng, W. P. & Nickoloff, J. A. (1992) Site-directed mutagenesis of virtually any plasmid by eliminating a unique site, Anal. Biochem. 200, 81-88.
    • (1992) Anal. Biochem. , vol.200 , pp. 81-88
    • Deng, W.P.1    Nickoloff, J.A.2
  • 24
    • 0001534761 scopus 로고
    • The mechanism of oxidation of aldehydes by glyceraldehyde-3-phosphate dehydrogenase
    • Racker, H. & Krimsky, I. (1952) The mechanism of oxidation of aldehydes by glyceraldehyde-3-phosphate dehydrogenase, J. Biol. Chem. 198, 731-743.
    • (1952) J. Biol. Chem. , vol.198 , pp. 731-743
    • Racker, H.1    Krimsky, I.2
  • 25
    • 0016160429 scopus 로고
    • Measurement of protein by spectrophotometry at 205 nm
    • Scopes, R. K. (1974) Measurement of protein by spectrophotometry at 205 nm, Anal. Biochem. 59, 277-282.
    • (1974) Anal. Biochem. , vol.59 , pp. 277-282
    • Scopes, R.K.1
  • 26
    • 0027499868 scopus 로고
    • Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: Resolution of ambiguity by electronic perturbation of the quasi-2-mercatopyridine leaving group in a new pyrimidyl disulfide reactivity probe
    • Mellor, G. W., Thomas, H. W., Topham, C. M. & Brocklehurst, K. (1993) Ionization characteristics of the Cys-25/His-159 interactive system and of the modulatory group of papain: resolution of ambiguity by electronic perturbation of the quasi-2-mercatopyridine leaving group in a new pyrimidyl disulfide reactivity probe, Biochem. J. 290, 289-296.
    • (1993) Biochem. J. , vol.290 , pp. 289-296
    • Mellor, G.W.1    Thomas, H.W.2    Topham, C.M.3    Brocklehurst, K.4
  • 27
    • 0015021901 scopus 로고
    • Rate determining processes and the number of simultaneously active sites of D-glyceraldehyde-3-phosphate dehydrogenase
    • Tremham, D. R. (1971) Rate determining processes and the number of simultaneously active sites of D-glyceraldehyde-3-phosphate dehydrogenase, Biochem. J 122, 71-77.
    • (1971) Biochem. J , vol.122 , pp. 71-77
    • Tremham, D.R.1
  • 28
    • 0026732565 scopus 로고
    • Progress in rate limiting features and kinetic mechanism of the glyceraldehyde-3-phosphate dehydrogenase reaction
    • Liu, L. & Huskey, W. P. (1992) Progress in rate limiting features and kinetic mechanism of the glyceraldehyde-3-phosphate dehydrogenase reaction, Biochemistry 31, 6898-6903.
    • (1992) Biochemistry , vol.31 , pp. 6898-6903
    • Liu, L.1    Huskey, W.P.2
  • 29
    • 0016714846 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase mutants of Escherichia coli
    • Hillman, J. D. & Fraenkel, D. G. (1975) Glyceraldehyde-3-phosphate dehydrogenase mutants of Escherichia coli, J. Bacteriol. 122, 1175-1179.
    • (1975) J. Bacteriol. , vol.122 , pp. 1175-1179
    • Hillman, J.D.1    Fraenkel, D.G.2
  • 30
    • 0023219801 scopus 로고
    • Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus
    • Fabry, S. & Hensel, R. (1987) Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus, Eur. J. Biochem. 165, 147-155.
    • (1987) Eur. J. Biochem. , vol.165 , pp. 147-155
    • Fabry, S.1    Hensel, R.2
  • 31
    • 0024285075 scopus 로고
    • Expression of the glyceraldehyde-3-phosphate dehydrogenase gene from the extremely thermophilic archaebacterium Methanothermus fervidus in E. coli
    • Fabry, S., Lehmacher, W., Bode, W. & Hensel, R. (1988) Expression of the glyceraldehyde-3-phosphate dehydrogenase gene from the extremely thermophilic archaebacterium Methanothermus fervidus in E. coli, FEBS Lett. 237, 213-217.
    • (1988) FEBS Lett. , vol.237 , pp. 213-217
    • Fabry, S.1    Lehmacher, W.2    Bode, W.3    Hensel, R.4
  • 32
    • 0000373477 scopus 로고
    • The acid strengh of the -SH group in cysteine and related compounds
    • Benesch, R. H. & Benesch, R. (1955) The acid strengh of the -SH group in cysteine and related compounds, J. Am. Chem. Soc. 77, 5877-5881.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 5877-5881
    • Benesch, R.H.1    Benesch, R.2
  • 33
    • 0015962432 scopus 로고
    • Spectrophotometric determination of mercaptide ion, an activated form of SH-group in thiol enzymes
    • Polgar, U (1974) Spectrophotometric determination of mercaptide ion, an activated form of SH-group in thiol enzymes, FEBS Lett. 38, 187-190.
    • (1974) FEBS Lett. , vol.38 , pp. 187-190
    • Polgar, U.1
  • 34
    • 0024588467 scopus 로고
    • Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase
    • Graminski, G. F., Kubo, Y. & Armstrong, R. N. (1989) Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase. Biochemistry 28, 3562-3568.
    • (1989) Biochemistry , vol.28 , pp. 3562-3568
    • Graminski, G.F.1    Kubo, Y.2    Armstrong, R.N.3
  • 36
    • 0028360184 scopus 로고
    • Reactivity and ionization at the active site cysteine residues of DsbA. a protein required for disulfide bond in vivo
    • Nelson, J. W. & Creighton, T. E. (1994) Reactivity and ionization at the active site cysteine residues of DsbA. a protein required for disulfide bond in vivo, Biochemistry 33, 5974-5983.
    • (1994) Biochemistry , vol.33 , pp. 5974-5983
    • Nelson, J.W.1    Creighton, T.E.2
  • 37
    • 0017089701 scopus 로고
    • Potentiometric determination of ionizations at the active site of papain
    • Lewis, S. D., Johnson, F. A. & Shafer, J. A. (1976) Potentiometric determination of ionizations at the active site of papain, Biochemistry 15, 5009-5017.
    • (1976) Biochemistry , vol.15 , pp. 5009-5017
    • Lewis, S.D.1    Johnson, F.A.2    Shafer, J.A.3
  • 38
    • 0019322092 scopus 로고
    • Solvent isotope effects on tautomerization equilibria of papain and model thiolamines
    • Creighton, D. J. & Schamp, D. J. (1980) Solvent isotope effects on tautomerization equilibria of papain and model thiolamines, FEBS Lett. 110, 313-318.
    • (1980) FEBS Lett. , vol.110 , pp. 313-318
    • Creighton, D.J.1    Schamp, D.J.2
  • 39
    • 0026013590 scopus 로고
    • Removal of an inter-domain hydrogen bond through site-directed mutagenesis: Role of serine 176 in the mechanism of papain
    • Menard, R., Plouffe, C., Khouri, H. E., Dupras, R., Tessier, D. C., Vernet, T., Thomas, D. Y. & Storer, A. C. (1991) Removal of an inter-domain hydrogen bond through site-directed mutagenesis: role of serine 176 in the mechanism of papain, Protein. Eng. 4, 307-311.
    • (1991) Protein. Eng. , vol.4 , pp. 307-311
    • Menard, R.1    Plouffe, C.2    Khouri, H.E.3    Dupras, R.4    Tessier, D.C.5    Vernet, T.6    Thomas, D.Y.7    Storer, A.C.8
  • 40
    • 0016115206 scopus 로고
    • Mercaptide-imidazolium ion-pair: The reactive nucleophile in papain catalysis
    • Polgar, L. (1974) Mercaptide-imidazolium ion-pair: the reactive nucleophile in papain catalysis, FEBS Lett. 47, 15-18.
    • (1974) FEBS Lett. , vol.47 , pp. 15-18
    • Polgar, L.1
  • 42
    • 0016440071 scopus 로고
    • Ion-pair formation as a source of enhanced reactivity of the essential thiol group of D-glyceraldehyde-3-phosphate dehydrogenase
    • Polgar, L. (1975) Ion-pair formation as a source of enhanced reactivity of the essential thiol group of D-glyceraldehyde-3-phosphate dehydrogenase, Eur. J. Biochem. 51, 63-71.
    • (1975) Eur. J. Biochem. , vol.51 , pp. 63-71
    • Polgar, L.1
  • 43
    • 0026969320 scopus 로고
    • A new chemical mechanism catalyzed by a mutated aldehyde dehydrogenase
    • Corbier, C., Della Seta, F. & Branlant, G. (1992) A new chemical mechanism catalyzed by a mutated aldehyde dehydrogenase, Biochemistry 31, 12532-12535.
    • (1992) Biochemistry , vol.31 , pp. 12532-12535
    • Corbier, C.1    Della Seta, F.2    Branlant, G.3
  • 44
    • 0026744397 scopus 로고
    • A study of the stabilization of tetrahedral adducts by trypsin and delta-chymotrypsin
    • Finucane, M. D. & Malthouse, J. P. G. (1992) A study of the stabilization of tetrahedral adducts by trypsin and delta-chymotrypsin, Biochem. J. 286, 889-900.
    • (1992) Biochem. J. , vol.286 , pp. 889-900
    • Finucane, M.D.1    Malthouse, J.P.G.2
  • 45
    • 0017760156 scopus 로고
    • Negatively charged reactants as probes in the study of the essential mercaptide-imidazolium ion-pair of thiolenzymes
    • Halasz, P. & Polgar, L. (1977) Negatively charged reactants as probes in the study of the essential mercaptide-imidazolium ion-pair of thiolenzymes, Eur. J. Biochem. 79, 491-494.
    • (1977) Eur. J. Biochem. , vol.79 , pp. 491-494
    • Halasz, P.1    Polgar, L.2
  • 46
    • 0018452287 scopus 로고
    • On the role of the active site helix in papain, an ah initio molecular orbital study
    • Van Duijnen, P. Th., Thole, B. Th. & Hol, W. G. J. (1979) On the role of the active site helix in papain, an ah initio molecular orbital study, Biophys. Chem. 9, 273-280.
    • (1979) Biophys. Chem. , vol.9 , pp. 273-280
    • Van Duijnen, P.Th.1    Thole, B.Th.2    Hol, W.G.J.3
  • 47
    • 0024961758 scopus 로고
    • The active site of papain: All-atom study of interactions with protein matrix and solvent
    • Rullmann, S. A., Bellido, M. N. & Van Duijnen, P. Th. (1989) The active site of papain: All-atom study of interactions with protein matrix and solvent, J. Mol. Biol. 206, 101-118.
    • (1989) J. Mol. Biol. , vol.206 , pp. 101-118
    • Rullmann, S.A.1    Bellido, M.N.2    Van Duijnen, P.Th.3
  • 48
    • 0021873417 scopus 로고
    • Nucleotide sequence of the Escherichia coli gap gene
    • Branlant, G. & Branlant, C. (1985) Nucleotide sequence of the Escherichia coli gap gene, Eur. J. Biochem. 150, 61-66.
    • (1985) Eur. J. Biochem. , vol.150 , pp. 61-66
    • Branlant, G.1    Branlant, C.2
  • 49
    • 0025124855 scopus 로고
    • Yeast thioltransferase-the active site cysteines display differential reactivity
    • Gan, Z. R., Sardana, M. K., Jacobs, J. W. & Polokoff, M. A. (1990) Yeast thioltransferase-the active site cysteines display differential reactivity, Arch. Biochem. Biophys. 282, 100-115.
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 100-115
    • Gan, Z.R.1    Sardana, M.K.2    Jacobs, J.W.3    Polokoff, M.A.4
  • 50
    • 0025788552 scopus 로고
    • Identification and characterization of the functionnal amino acids at the active center of pig liver thioltransferase by site directed mutagenesis
    • Yang, Y. & Wells, W. W. (1991) Identification and characterization of the functionnal amino acids at the active center of pig liver thioltransferase by site directed mutagenesis, J. Biol. Chem. 166, 12759-12765.
    • (1991) J. Biol. Chem. , vol.166 , pp. 12759-12765
    • Yang, Y.1    Wells, W.W.2
  • 51
    • 0025887464 scopus 로고
    • Thioltransferase in human red blood cells: Kinetics and equilibrium
    • Mieyal, J. J., Starke, D. W., Gravina, S. A. & Hocevar, B. A. (1991) Thioltransferase in human red blood cells: kinetics and equilibrium, Biochemistry 30, 8883-8891.
    • (1991) Biochemistry , vol.30 , pp. 8883-8891
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Hocevar, B.A.4
  • 52
    • 0028886558 scopus 로고
    • Ionisation of cysteine residues at the termini of model α-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family
    • Kortemme, T. & Creighton, T. E. (1995) Ionisation of cysteine residues at the termini of model α-helical peptides. Relevance to unusual thiol pKa values in proteins of the thioredoxin family, J. Mol. Biol. 253, 799-812.
    • (1995) J. Mol. Biol. , vol.253 , pp. 799-812
    • Kortemme, T.1    Creighton, T.E.2
  • 53
    • 0028922730 scopus 로고
    • Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis
    • Wang, X. & Weiner, H. (1995) Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis, Biochemistry 34, 237-243.
    • (1995) Biochemistry , vol.34 , pp. 237-243
    • Wang, X.1    Weiner, H.2
  • 54
    • 0029849211 scopus 로고    scopus 로고
    • High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol
    • Thoden, J. B., Frey, P. A. & Holden, H. M. (1996) High-resolution X-ray structure of UDP-galactose 4-epimerase complexed with UDP-phenol, Protein Science 5, 2149-2161.
    • (1996) Protein Science , vol.5 , pp. 2149-2161
    • Thoden, J.B.1    Frey, P.A.2    Holden, H.M.3
  • 55
    • 0029670932 scopus 로고    scopus 로고
    • 1H NMR spectroscopy of the catalytic histidine in chloromethyl ketone-inhibited complexes of serine proteases
    • 1H NMR spectroscopy of the catalytic histidine in chloromethyl ketone-inhibited complexes of serine proteases, Biochemistry 35, 2437-2444.
    • (1996) Biochemistry , vol.35 , pp. 2437-2444
    • Tsilikounas, E.1    Rao, T.2    Gutheil, W.G.3    Bachovchin, W.4
  • 56
    • 0017576456 scopus 로고
    • Sequence and structure of D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus
    • Biesecker, G., Harris, J. I., Thierry, J. C., Walker, J. E. & Wonacott, A. J. (1977) Sequence and structure of D-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus, Nature 206, 328-333.
    • (1977) Nature , vol.206 , pp. 328-333
    • Biesecker, G.1    Harris, J.I.2    Thierry, J.C.3    Walker, J.E.4    Wonacott, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.