메뉴 건너뛰기




Volumn 262, Issue 2, 1996, Pages 202-224

Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83 Å

Author keywords

Cystathionine lyase; Enzyme catalysis; Protein structure; Pyridoxal 5' phosphate; Suicide inactivation; Transsulfuration; Trifluoroalanine

Indexed keywords

ALANINE DERIVATIVE; AMINOTRANSFERASE; CYSTATHIONINE; LYASE; PYRIDOXAL 5 PHOSPHATE;

EID: 0030595364     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0508     Document Type: Article
Times cited : (155)

References (65)
  • 1
    • 0015915298 scopus 로고
    • Acetylenic enzyme inactivators. Inactivation of γ-cystathionase, in vitro and in vivo by propargylglycine
    • Abeles, R. H. & Walsh, C. T. (1973). Acetylenic enzyme inactivators. Inactivation of γ-cystathionase, in vitro and in vivo by propargylglycine. J. Am. Chem. Soc. 95, 6124-6125.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 6124-6125
    • Abeles, R.H.1    Walsh, C.T.2
  • 2
    • 0028044574 scopus 로고
    • Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regionspecific α, β and γ subgroups
    • Alexander, F. W., Sandmeier, E., Mehta, P. K. & Christen, P. (1994). Evolutionary relationships among pyridoxal-5'-phosphate-dependent enzymes. Regionspecific α, β and γ subgroups. Eur. J. Biochem. 219, 953-960.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 953-960
    • Alexander, F.W.1    Sandmeier, E.2    Mehta, P.K.3    Christen, P.4
  • 4
    • 0001353133 scopus 로고
    • Evolution in biosynthetic pathways: Two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region
    • Belfaiza, J., Parsot, C., Martel, A., Bouthier de la Tour, C., Margerita, D., Cohen, G. N. & Saint-Girons, I. (1986). Evolution in biosynthetic pathways: two enzymes catalyzing consecutive steps in methionine biosynthesis originate from a common ancestor and possess a similar regulatory region. Proc. Natl Acad. Sci. USA, 83, 867-871.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 867-871
    • Belfaiza, J.1    Parsot, C.2    Martel, A.3    Bouthier De La Tour, C.4    Margerita, D.5    Cohen, G.N.6    Saint-Girons, I.7
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. sect. D, 50, 760-763.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 760-763
  • 8
    • 0023910932 scopus 로고
    • Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis
    • Cronin, C. N. & Kirsch, J. F. (1988). Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis. Biochemistry, 27, 4572-4579.
    • (1988) Biochemistry , vol.27 , pp. 4572-4579
    • Cronin, C.N.1    Kirsch, J.F.2
  • 10
    • 0013902457 scopus 로고
    • Conformation and reaction specificity in pyridoxal phosphate enzymes
    • Dunathan, H. C. (1966). Conformation and reaction specificity in pyridoxal phosphate enzymes. Proc. Natl Acad. Sci. USA, 55, 712-716.
    • (1966) Proc. Natl Acad. Sci. USA , vol.55 , pp. 712-716
    • Dunathan, H.C.1
  • 11
    • 0000951818 scopus 로고
    • Stereochemical evidence for the evolution of pyridoxal-phosphate enzymes of various function from a common ancestor
    • Dunathan, H. C. & Voet, J. G. (1974). Stereochemical evidence for the evolution of pyridoxal-phosphate enzymes of various function from a common ancestor. Proc. Natl Acad. Sci. USA, 71, 3888-3891.
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 3888-3891
    • Dunathan, H.C.1    Voet, J.G.2
  • 12
    • 0020317656 scopus 로고
    • Cloning, purification and characterization of β-cystathionase from E. coli
    • Dwivedi, C. M., Ragin, R. C. & Uren, J. R. (1982). Cloning, purification and characterization of β-cystathionase from E. coli. Biochemistry, 21, 3064-3069.
    • (1982) Biochemistry , vol.21 , pp. 3064-3069
    • Dwivedi, C.M.1    Ragin, R.C.2    Uren, J.R.3
  • 13
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein-structure refinement
    • Engh, R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallog. sect. A. 47, 392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 14
    • 0025374330 scopus 로고
    • Sequence of cDNA for rat cystathionine γ-lyase and comparison of deduced amino acid sequence with related Escherichia coli enzymes
    • Erickson, P. F., Maxwell, I. H., Su, L. J., Baumann, M. & Glode, L. M. (1990). Sequence of cDNA for rat cystathionine γ-lyase and comparison of deduced amino acid sequence with related Escherichia coli enzymes. Biochem. J. 269, 335-340.
    • (1990) Biochem. J. , vol.269 , pp. 335-340
    • Erickson, P.F.1    Maxwell, I.H.2    Su, L.J.3    Baumann, M.4    Glode, L.M.5
  • 15
    • 0020474213 scopus 로고
    • Identification of the active-site residue of γ-cystathionase labeled by the suicide inactivator β,β,β-trifluoroalanine
    • Fearon, C. W., Rodkey, J. A. & Abeles, R. H. (1982). Identification of the active-site residue of γ-cystathionase labeled by the suicide inactivator β,β,β-trifluoroalanine. Biochemistry, 21, 3790-3794.
    • (1982) Biochemistry , vol.21 , pp. 3790-3794
    • Fearon, C.W.1    Rodkey, J.A.2    Abeles, R.H.3
  • 16
    • 0019014846 scopus 로고
    • Three-dimensional structure of a pyridoxal phosphate dependent enzyme, mitochondrial aspartate aminotransferase
    • Ford, G. C., Eichele, G. & Jansonius, J. N. (1980). Three-dimensional structure of a pyridoxal phosphate dependent enzyme, mitochondrial aspartate aminotransferase. Proc. Natl Acad. Sci. USA, 77, 2559-2563.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 2559-2563
    • Ford, G.C.1    Eichele, G.2    Jansonius, J.N.3
  • 17
    • 0027407222 scopus 로고
    • Toxicity of Bordella avium β-cystathionase toward MC3T3-E1 osteogenic cells
    • Gentry-Weeks, C. R., Keith, J. M. & Thompson, J. (1993). Toxicity of Bordella avium β-cystathionase toward MC3T3-E1 osteogenic cells. J. Biol. Chem. 268, 7298-7314.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7298-7314
    • Gentry-Weeks, C.R.1    Keith, J.M.2    Thompson, J.3
  • 18
    • 0025270921 scopus 로고
    • Effects of replacement of tryptophane-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase
    • Hayashi, H., Inoue, Y., Kuramitsu, S., Morino, Y. & Kagamiyama, H. (1990). Effects of replacement of tryptophane-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase. Biochem. Biophys. Res. Commun. 167, 407-412.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 407-412
    • Hayashi, H.1    Inoue, Y.2    Kuramitsu, S.3    Morino, Y.4    Kagamiyama, H.5
  • 19
    • 0021978310 scopus 로고
    • The role of the α-helix dipole in protein function and structure
    • Hol, W. G. (1985). The role of the α-helix dipole in protein function and structure. Progr. Biophys. Mol. Biol. 45, 149-195.
    • (1985) Progr. Biophys. Mol. Biol. , vol.45 , pp. 149-195
    • Hol, W.G.1
  • 20
    • 0011893916 scopus 로고
    • Die faltmolekülmethode und ihre Anwendung in der röntgenographischen Konstitutionsanalyse von Biflorin
    • Hoppe, W. (1957). Die Faltmolekülmethode und ihre Anwendung in der röntgenographischen Konstitutionsanalyse von Biflorin. Z. Elektrochem. 61, 1076-1083.
    • (1957) Z. Elektrochem. , vol.61 , pp. 1076-1083
    • Hoppe, W.1
  • 21
    • 0000693863 scopus 로고
    • Structural basis for catalysis by aspartate aminotransferase
    • (Jurnak, F. A. & McPherson, A., eds), Wiley & Sons, New York
    • Jansonius, J. N. & Vincent, M. G. (1987). Structural basis for catalysis by aspartate aminotransferase. In Biological Macromolecules and Assemblies (Jurnak, F. A. & McPherson, A., eds), vol. 3, pp. 187-288. Wiley & Sons, New York.
    • (1987) Biological Macromolecules and Assemblies , vol.3 , pp. 187-288
    • Jansonius, J.N.1    Vincent, M.G.2
  • 22
    • 0028914569 scopus 로고
    • Pyridoxal phosphate-dependent enzymes
    • John, R. A. (1995). Pyridoxal phosphate-dependent enzymes. Biochim. Biophys. Acta, 1248, 81-96.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 81-96
    • John, R.A.1
  • 24
    • 0022701772 scopus 로고
    • Using known substructures in protein model building and crystallography
    • Jones, T. A. & Thirup, S. (1986). Using known substructures in protein model building and crystallography. EMBO J. 5, 819-822.
    • (1986) EMBO J. , vol.5 , pp. 819-822
    • Jones, T.A.1    Thirup, S.2
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgard, M.4
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 29
    • 0028100244 scopus 로고
    • Purification and properties of cystathionine γ-synthase from wheat (Triticum aestivum L.)
    • Kreft, B. D., Townsend, A., Pohlenz, H. D. & Laber, B. (1994). Purification and properties of cystathionine γ-synthase from wheat (Triticum aestivum L.). Plant Physiol. 104, 1215-1220.
    • (1994) Plant Physiol. , vol.104 , pp. 1215-1220
    • Kreft, B.D.1    Townsend, A.2    Pohlenz, H.D.3    Laber, B.4
  • 30
    • 0028218431 scopus 로고
    • Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors
    • Laber, B., Gerbling, K. P., Harde, C., Neff, K. H., Nordhoff, E. & Pohlenz, H. D. (1994a). Mechanisms of interaction of Escherichia coli threonine synthase with substrates and inhibitors. Biochemistry, 33, 3413-3423.
    • (1994) Biochemistry , vol.33 , pp. 3413-3423
    • Laber, B.1    Gerbling, K.P.2    Harde, C.3    Neff, K.H.4    Nordhoff, E.5    Pohlenz, H.D.6
  • 31
    • 0028290467 scopus 로고
    • Inactivation of Escherichia coli threonine synthase by DL-Z-2-amino-5-phosphono-3-pentenoic acid
    • Laber, B., Lindell, S. D. & Pohlenz, H. D. (1994b). Inactivation of Escherichia coli threonine synthase by DL-Z-2-amino-5-phosphono-3-pentenoic acid. Arch. Microbiol. 161, 400-403.
    • (1994) Arch. Microbiol. , vol.161 , pp. 400-403
    • Laber, B.1    Lindell, S.D.2    Pohlenz, H.D.3
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 34
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B. K. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55, 379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 36
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la détermination des structures cristallines
    • Luzatti, V. (1952). Traitement statistique des erreurs dans la détermination des structures cristallines. Acta Crystallog. sect. A, 5, 802-810.
    • (1952) Acta Crystallog. Sect. A , vol.5 , pp. 802-810
    • Luzatti, V.1
  • 37
    • 0027738034 scopus 로고
    • Crystal structures of true enzymatic reaction intermediates: Aspartate and glutamate ketimines in aspartate aminotransferase
    • Malashkevich, V. N., Toney, M. D. & Jansonius, J. N. (1993). Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase. Biochemistry, 32, 13451-13462.
    • (1993) Biochemistry , vol.32 , pp. 13451-13462
    • Malashkevich, V.N.1    Toney, M.D.2    Jansonius, J.N.3
  • 38
    • 0023656228 scopus 로고
    • Pyridoxal-5'-phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase. Comparison of their sequences
    • Martel, A., Bouthier de la Tour, C. & Le Goffic, F. (1987). Pyridoxal-5'-phosphate binding site of Escherichia coli beta cystathionase and cystathionine gamma synthase. Comparison of their sequences. Biochem. Biophy. Res. Commun. 147, 565-571.
    • (1987) Biochem. Biophy. Res. Commun. , vol.147 , pp. 565-571
    • Martel, A.1    Bouthier De La Tour, C.2    Le Goffic, F.3
  • 39
    • 0026751404 scopus 로고
    • X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
    • McPhalen, C. A., Vincent, M. G. & Jansonius, J. N. (1992). X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J. Mol. Biol. 225, 495-517.
    • (1992) J. Mol. Biol. , vol.225 , pp. 495-517
    • McPhalen, C.A.1    Vincent, M.G.2    Jansonius, J.N.3
  • 40
    • 0027297771 scopus 로고
    • Aminotransferases: Demonstration of homology and division into evolutionary subgroups
    • Mehta, P. K., Hale, T. I. & Christen, P. (1993). Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem. 214, 549-561.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 549-561
    • Mehta, P.K.1    Hale, T.I.2    Christen, P.3
  • 41
    • 0028057108 scopus 로고
    • RASTER3D Version 2.0. A program for photorealistic molecular graphics
    • Merrit, E. A. & Murphy, M. E. P. (1994). RASTER3D Version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. sect. D, 50, 869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 42
    • 0028907826 scopus 로고
    • The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 Å resolution
    • Mirwaldt, C., Korndoerfer, I. & Huber, R. (1995). The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 Å resolution. J. Mol. Biol. 246, 227-239.
    • (1995) J. Mol. Biol. , vol.246 , pp. 227-239
    • Mirwaldt, C.1    Korndoerfer, I.2    Huber, R.3
  • 43
    • 0029131487 scopus 로고
    • Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution
    • Momany, C., Ernst, S., Ghosh, R., Chang, N.-L. & Hackert, M. L. (1995). Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution. J. Mol. Biol. 252, 643-655.
    • (1995) J. Mol. Biol. , vol.252 , pp. 643-655
    • Momany, C.1    Ernst, S.2    Ghosh, R.3    Chang, N.-L.4    Hackert, M.L.5
  • 44
    • 0024589745 scopus 로고
    • DNA sequence of the metC gene and its flanking regions from Salmonella typhimurium LT2 and homology with the correspending sequence of Escherichia coli
    • Park, Y. M. & Staufer, G. V. (1989). DNA sequence of the metC gene and its flanking regions from Salmonella typhimurium LT2 and homology with the correspending sequence of Escherichia coli. Mol. Gen. Genet. 216, 164-169.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 164-169
    • Park, Y.M.1    Staufer, G.V.2
  • 45
    • 0023415372 scopus 로고
    • Enzyme specialization during the evolution of amino acid biosynthetic pathways
    • Parsot, C., Saint-Girons, I. & Cohen, G. N. (1987). Enzyme specialization during the evolution of amino acid biosynthetic pathways. Microbiol. Sci. 4, 258-262.
    • (1987) Microbiol. Sci. , vol.4 , pp. 258-262
    • Parsot, C.1    Saint-Girons, I.2    Cohen, G.N.3
  • 47
    • 0029410831 scopus 로고
    • Cloning of an Arabidopsis thaliana cDNA encoding cystathionine beta-lyase by functional complementation in E. coli
    • Ravanel, S., Ruffet, M. L., Droux, M. & Douce, R. (1995). Cloning of an Arabidopsis thaliana cDNA encoding cystathionine beta-lyase by functional complementation in E. coli. Plant Molecular Biology 29(4), 875-882.
    • (1995) Plant Molecular Biology , vol.29 , Issue.4 , pp. 875-882
    • Ravanel, S.1    Ruffet, M.L.2    Droux, M.3    Douce, R.4
  • 48
    • 0025848324 scopus 로고
    • The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system
    • Reidl, J. & Boos, W. (1991). The malX malY operon of Escherichia coli encodes a novel enzyme II of the phosphotransferase system recognizing glucose and maltose and an enzyme abolishing the endogenous induction of the maltose system. J. Bacteriol. 173, 4862-4876.
    • (1991) J. Bacteriol. , vol.173 , pp. 4862-4876
    • Reidl, J.1    Boos, W.2
  • 49
    • 0019443447 scopus 로고
    • The anatomy and taxonony of protein structure
    • Richardson, J. S. (1981). The anatomy and taxonony of protein structure. Advan. Protein Chem. 34, 167-339.
    • (1981) Advan. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 50
    • 0002660809 scopus 로고
    • The detection of subunits within the crystallographic asymmetric unit
    • Rossmann, M. G. & Blow, D. M. (1962). The detection of subunits within the crystallographic asymmetric unit. Acta Crystallog. 15, 24-31.
    • (1962) Acta Crystallog. , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blow, D.M.2
  • 51
    • 0020490851 scopus 로고
    • Chemical modifications of a functional arginyl residue (Arg292) of mitochondrial aspartate aminotransferase
    • Sandmeier, E. & Christen, P. (1982). Chemical modifications of a functional arginyl residue (Arg292) of mitochondrial aspartate aminotransferase. J. Biol. Chem. 257, 6745-6750.
    • (1982) J. Biol. Chem. , vol.257 , pp. 6745-6750
    • Sandmeier, E.1    Christen, P.2
  • 52
    • 0017566996 scopus 로고
    • Mechanism of inactivation of γ-cystathionase by β,β,β-trifluoroalanine
    • Silverman, R. B. & Abeles, H. A. (1977). Mechanism of inactivation of γ-cystathionase by β,β,β-trifluoroalanine. Biochemistry, 16, 5515-5520.
    • (1977) Biochemistry , vol.16 , pp. 5515-5520
    • Silverman, R.B.1    Abeles, H.A.2
  • 53
    • 0017191814 scopus 로고
    • Inactivation of pyridoxal phosphate dependent enzymes by mono-and polyhaloalanines
    • Silverman, R. B. & Abeles, R. H. (1976). Inactivation of pyridoxal phosphate dependent enzymes by mono-and polyhaloalanines. Biochemistry, 15, 4718-4723.
    • (1976) Biochemistry , vol.15 , pp. 4718-4723
    • Silverman, R.B.1    Abeles, R.H.2
  • 54
    • 0011854382 scopus 로고
    • Ph.D. thesis, Technische Universität München, FRG
    • Steigemann, W. (1974). Ph.D. thesis, Technische Universität München, FRG.
    • (1974)
    • Steigemann, W.1
  • 55
    • 0027182377 scopus 로고
    • Dialkylglycine decarboxylase structure: Bifunctional active site and alkali metal sites
    • Toney, M. D., Hohenester, E., Cowan, S. W. & Jansonius, J. N. (1993). Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites. Science, 261, 756-759.
    • (1993) Science , vol.261 , pp. 756-759
    • Toney, M.D.1    Hohenester, E.2    Cowan, S.W.3    Jansonius, J.N.4
  • 56
    • 0028885266 scopus 로고
    • Structural and mechanistic analysis of the pyridoxal-phosphate dependent enzyme dialkylglycine decarboxylase
    • Toney, M. D., Hohenester, E., Keller, J. W. & Jansonius, J. N. (1995). Structural and mechanistic analysis of the pyridoxal-phosphate dependent enzyme dialkylglycine decarboxylase. J. Mol. Biol. 245, 151-179.
    • (1995) J. Mol. Biol. , vol.245 , pp. 151-179
    • Toney, M.D.1    Hohenester, E.2    Keller, J.W.3    Jansonius, J.N.4
  • 57
    • 0023656215 scopus 로고
    • Tyrosine 70 increases the coenzyme affinity of aspartate aminotransferase
    • Toney, M. D. & Kirsch, J. F. (1987). Tyrosine 70 increases the coenzyme affinity of aspartate aminotransferase. J. Biol. Chem. 262, 12403-12405.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12403-12405
    • Toney, M.D.1    Kirsch, J.F.2
  • 59
    • 0015523668 scopus 로고
    • Inactivation of a flavoprotein, lactate oxidase, by an acetylenic substrate
    • Walsh, C. T., Schonbrunn, A., Lockridge, O., Massey, V. & Abeles, R. H. (1972). Inactivation of a flavoprotein, lactate oxidase, by an acetylenic substrate. J. Biol. Chem. 247, 6004-6006.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6004-6006
    • Walsh, C.T.1    Schonbrunn, A.2    Lockridge, O.3    Massey, V.4    Abeles, R.H.5
  • 60
    • 0017404062 scopus 로고
    • Mechanism of inactivation of γ-cystathionase by the acetylenic substrate analogue propargylglycine
    • Washtien, W. & Abeles, R. H. (1977). Mechanism of inactivation of γ-cystathionase by the acetylenic substrate analogue propargylglycine. Biochemistry, 16, 2485-2491.
    • (1977) Biochemistry , vol.16 , pp. 2485-2491
    • Washtien, W.1    Abeles, R.H.2
  • 61
    • 20244378184 scopus 로고
    • Crystal structure analysis of ω-amino acid:Pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchroton radiation
    • Watanable, N., Sakabe, K., Sakabe, N., Higashi, T., Sasaki, K., Aibara, S., Morita, Y., Yonaha, K., Toyama, S. & Fukutani, H. (1989). Crystal structure analysis of ω-amino acid:pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchroton radiation. J. Biochem. 105, 1-3.
    • (1989) J. Biochem. , vol.105 , pp. 1-3
    • Watanable, N.1    Sakabe, K.2    Sakabe, N.3    Higashi, T.4    Sasaki, K.5    Aibara, S.6    Morita, Y.7    Yonaha, K.8    Toyama, S.9    Fukutani, H.10
  • 62
    • 0025922823 scopus 로고
    • The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase
    • Yano, T., Kuramitsu, S., Tanase, S., Yoshimasa, M., Hiromi, K. & Kagamiyama, H. (1991). The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase. J. Biol. Chem. 266, 6079-6085.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6079-6085
    • Yano, T.1    Kuramitsu, S.2    Tanase, S.3    Yoshimasa, M.4    Hiromi, K.5    Kagamiyama, H.6
  • 63
    • 0011893919 scopus 로고
    • Role of Asp222 in the catalytic mechanism of Escherichia Coli aspartate aminotransferase
    • Yano, T., Kuramitsu, S., Tanase, S., Morino, Y. & Kagamiyama, H. (1992). Role of Asp222 in the catalytic mechanism of Escherichia Coli aspartate aminotransferase. J. Biol. Chem. 267, 12506-12510.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12506-12510
    • Yano, T.1    Kuramitsu, S.2    Tanase, S.3    Morino, Y.4    Kagamiyama, H.5
  • 64
    • 0027536099 scopus 로고
    • A hydrogen-bonding network modulating enzyme function: Asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase
    • Yano, T., Mizuno, T. & Kagamiyama, H. (1993). A hydrogen-bonding network modulating enzyme function: asparagine-194 and tyrosine-225 of Escherichia coli aspartate aminotransferase. Biochemistry, 32, 1810-1815.
    • (1993) Biochemistry , vol.32 , pp. 1810-1815
    • Yano, T.1    Mizuno, T.2    Kagamiyama, H.3
  • 65
    • 0029127483 scopus 로고
    • MalY of Escherichia coli is an enzyme with the activity of a βC-S lyase (cystathionase)
    • Zdych, E., Peist, R., Reidl, J. & Boos, W. (1995). MalY of Escherichia coli is an enzyme with the activity of a βC-S lyase (cystathionase). J. Bacteriol. 177, 5035-5039.
    • (1995) J. Bacteriol. , vol.177 , pp. 5035-5039
    • Zdych, E.1    Peist, R.2    Reidl, J.3    Boos, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.