메뉴 건너뛰기




Volumn 291, Issue 4, 1999, Pages 941-953

Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium

Author keywords

Catalytic mechanism; Conformational change; Cysteine biosynthesis; O acetylserine sulfhydrylase; Pyridoxal 5' phosphate

Indexed keywords

CYSTEINE SYNTHASE; METHIONINE; PYRIDOXAL 5 PHOSPHATE;

EID: 0033609810     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3002     Document Type: Article
Times cited : (120)

References (49)
  • 1
    • 0028044574 scopus 로고
    • Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families
    • Alexander F. W., Sandmeier E., Mehta P. K., Christen P. Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Regio-specific alpha, beta and gamma families. Eur. J. Biochem. 219:1994;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
  • 2
    • 0030722376 scopus 로고    scopus 로고
    • Time-resolved fluorescence of O -acetylserine sulfhydrylase catalytic intermediates
    • Benci S., Vaccari S., Mozzarelli A., Cook P. F. Time-resolved fluorescence of O -acetylserine sulfhydrylase catalytic intermediates. Biochemistry. 36:1997;15419-15427.
    • (1997) Biochemistry , vol.36 , pp. 15419-15427
    • Benci, S.1    Vaccari, S.2    Mozzarelli, A.3    Cook, P.F.4
  • 4
    • 0344157394 scopus 로고    scopus 로고
    • Three-dimensional structure of O -acetylserine sulfhydrylase from Salmonella typhimurium at 2.2 Å
    • Burkhard P., Rao G. S. J., Hohenester E., Schnackerz K. D., Cook P. F., Jansonius J. N. Three-dimensional structure of O -acetylserine sulfhydrylase from Salmonella typhimurium at 2.2 Å J. Mol. Biol. 283:1998;121-131.
    • (1998) J. Mol. Biol. , vol.283 , pp. 121-131
    • Burkhard, P.1    Rao, G.S.J.2    Hohenester, E.3    Schnackerz, K.D.4    Cook, P.F.5    Jansonius, J.N.6
  • 5
    • 0024040340 scopus 로고
    • DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH
    • Byrne C. R., Monroe R. S., Ward K. A., Kredich N. M. DNA sequences of the cysK regions of Salmonella typhimurium and Escherichia coli and linkage of the cysK regions to ptsH. J. Bacteriol. 170:1988;3150-3157.
    • (1988) J. Bacteriol. , vol.170 , pp. 3150-3157
    • Byrne, C.R.1    Monroe, R.S.2    Ward, K.A.3    Kredich, N.M.4
  • 7
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland W. W. Statistical analysis of enzyme kinetic data. Methods Enzymol. 63:1979;103-138.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 8
    • 0017281552 scopus 로고
    • A reaction mechanism from steady-state kinetic studies for O -acetylserine sulfhydrylase from Salmonella typhimurium LT-2
    • Cook P. F., Wedding R. T. A reaction mechanism from steady-state kinetic studies for O -acetylserine sulfhydrylase from Salmonella typhimurium LT-2. J. Biol. Chem. 251:1976;2023-2029.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2023-2029
    • Cook, P.F.1    Wedding, R.T.2
  • 9
    • 0026511957 scopus 로고
    • 31P NMR spectra of O -acetylserine sulfhydrylase in the absence and presence of O -acetyl- L -serine
    • 31P NMR spectra of O -acetylserine sulfhydrylase in the absence and presence of O -acetyl- L -serine. Biochemistry. 31:1992;2298-2303.
    • (1992) Biochemistry , vol.31 , pp. 2298-2303
    • Cook, P.F.1    Hara, S.2    Nalabolu, S.3    Schnackerz, K.D.4
  • 11
    • 0022344850 scopus 로고
    • Detection and identification of intermediates in the reaction of L -serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy
    • Drewe W. F. Jr, Dunn M. F. Detection and identification of intermediates in the reaction of L -serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy. Biochemistry. 24:1985;3977-3987.
    • (1985) Biochemistry , vol.24 , pp. 3977-3987
    • Drewe W.F., Jr.1    Dunn, M.F.2
  • 12
    • 0028072488 scopus 로고
    • Energetics of cooperative ligand binding to the active sites of biosynthetic threonine deaminase from Escherichia coli
    • Eisenstein E. Energetics of cooperative ligand binding to the active sites of biosynthetic threonine deaminase from Escherichia coli. J. Biol. Chem. 269:1994;29416-29422.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29416-29422
    • Eisenstein, E.1
  • 13
    • 0017163151 scopus 로고
    • Stereochemistry of the formation of cysteine by O-acetylserine sulfhydrylase
    • Floss H. G., Schleicher E., Potts R. G. Stereochemistry of the formation of cysteine by O-acetylserine sulfhydrylase. J. Biol. Chem. 251:1976;5478-5483.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5478-5483
    • Floss, H.G.1    Schleicher, E.2    Potts, R.G.3
  • 14
    • 0006485248 scopus 로고
    • Stereochemical course of the enzymic synthesis of L-tyrosine from phenol and L-serine catalyzed by tyrosine phenol lyase
    • Fuganti C., Ghiringhelli D., Giangrasso D., Grasselli P. Stereochemical course of the enzymic synthesis of L-tyrosine from phenol and L-serine catalyzed by tyrosine phenol lyase. J. Chem. Soc. Chem. Commun. 726:1974.
    • (1974) J. Chem. Soc. Chem. Commun. , vol.726
    • Fuganti, C.1    Ghiringhelli, D.2    Giangrasso, D.3    Grasselli, P.4
  • 16
    • 0029046782 scopus 로고
    • Modeling of the spatial structure of eukar yotic ornithine decarboxylases
    • Grishin N. V., Phillips M. A., Goldsmith E. J. Modeling of the spatial structure of eukar yotic ornithine decarboxylases. Protein Sci. 4:1995;1291-1304.
    • (1995) Protein Sci. , vol.4 , pp. 1291-1304
    • Grishin, N.V.1    Phillips, M.A.2    Goldsmith, E.J.3
  • 17
    • 0017813019 scopus 로고
    • Threonine deaminase from Salmonella typhimurium. Effect of regulatory ligands on the binding of substrates and substrate analogues to the active sites and the differentiation of the activator and inhibitor sites from the active sites
    • Hofler J. G., Burns R. O. Threonine deaminase from Salmonella typhimurium. Effect of regulatory ligands on the binding of substrates and substrate analogues to the active sites and the differentiation of the activator and inhibitor sites from the active sites. J. Biol. Chem. 253:1978;1245-1251.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1245-1251
    • Hofler, J.G.1    Burns, R.O.2
  • 18
    • 0030012777 scopus 로고    scopus 로고
    • Kinetic isotope effects as a probe of the β-elimination reaction catalyzed by O -acetylserine sulfhydrylase
    • Hwang C.-C., Woehl E. U., Dunn M. F., Cook P. F. Kinetic isotope effects as a probe of the β-elimination reaction catalyzed by O -acetylserine sulfhydrylase. Biochemistry. 35:1996;6358-6365.
    • (1996) Biochemistry , vol.35 , pp. 6358-6365
    • Hwang, C.-C.1    Woehl, E.U.2    Dunn, M.F.3    Cook, P.F.4
  • 20
    • 0000693863 scopus 로고
    • Structural basis for catalysis by aspartate amino-transferase
    • F. A. Jurnak, & A. McPherson. New York: Wiley & Sons
    • Jansonius J. N., Vincent M. G. Structural basis for catalysis by aspartate amino-transferase. Jurnak F. A., McPherson A. Biological Macromolecules & Assemblies. 1987;187-288 Wiley & Sons, New York.
    • (1987) Biological Macromolecules & Assemblies , pp. 187-288
    • Jansonius, J.N.1    Vincent, M.G.2
  • 21
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T. A., Zou J. Y., Cowan S. W., Kjeldgaard. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 22
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 23
    • 0014011576 scopus 로고
    • The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium
    • Kredich N. M., Tomkins G. M. The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J. Biol. Chem. 241:1966;4955-4965.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4955-4965
    • Kredich, N.M.1    Tomkins, G.M.2
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowsky R. A., MacArthur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowsky, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0028174296 scopus 로고
    • Product binding to the α-carboxyl subsite results in a conformational change at the active site of O -acetylserine sulfhydrylase-A: Evidence from fluorescence spectroscopy
    • McClure G. D., Cook P. F. Product binding to the α-carboxyl subsite results in a conformational change at the active site of O -acetylserine sulfhydrylase-A: evidence from fluorescence spectroscopy. Biochemistry. 33:1994;1674-1683.
    • (1994) Biochemistry , vol.33 , pp. 1674-1683
    • McClure, G.D.1    Cook, P.F.2
  • 29
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt E. A., Bacon D. J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277 Part B:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 30
    • 0032538283 scopus 로고    scopus 로고
    • The catalytic competence of O -acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry
    • Mozzarelli A., Bettati S., Pucci A. M., Cook P. F. The catalytic competence of O -acetylserine sulfhydrylase in the crystal probed by polarized absorption microspectrophotometry. J. Mol. Biol. 283:1998;135-146.
    • (1998) J. Mol. Biol. , vol.283 , pp. 135-146
    • Mozzarelli, A.1    Bettati, S.2    Pucci, A.M.3    Cook, P.F.4
  • 33
    • 0025866674 scopus 로고
    • Reaction of indole and analogues with amino acid complexes of Escherichia coli tryptophan indole-lyase: Detection of a new reaction intermediate by rapid-scanning stopped-flow spectrophotometry
    • Phillips R. S. Reaction of indole and analogues with amino acid complexes of Escherichia coli tryptophan indole-lyase: detection of a new reaction intermediate by rapid-scanning stopped-flow spectrophotometry. Biochemistry. 30:1991;5927-5934.
    • (1991) Biochemistry , vol.30 , pp. 5927-5934
    • Phillips, R.S.1
  • 34
    • 0031047009 scopus 로고    scopus 로고
    • Effects of tyrosine ring fluorination on rates and equilibria of formation of intermediates in the reactions of carbon-carbon lyases
    • Phillips R. S., Von Tersch R. L., Secundo F. Effects of tyrosine ring fluorination on rates and equilibria of formation of intermediates in the reactions of carbon-carbon lyases. Eur. J. Biochem. 244:1997;658-663.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 658-663
    • Phillips, R.S.1    Von Tersch, R.L.2    Secundo, F.3
  • 36
    • 0026029016 scopus 로고
    • The open-closed conformational equilibrium of aspartate aminotransferase. Studies in the crystalline state and with a fluorescent probe in solution
    • Picot D., Sandmeier E., Thaller C., Vincent M. G., Christen P., Jansonius J. N. The open-closed conformational equilibrium of aspartate aminotransferase. Studies in the crystalline state and with a fluorescent probe in solution. Eur. J. Biochem. 196:1991;329-341.
    • (1991) Eur. J. Biochem. , vol.196 , pp. 329-341
    • Picot, D.1    Sandmeier, E.2    Thaller, C.3    Vincent, M.G.4    Christen, P.5    Jansonius, J.N.6
  • 37
    • 0027169519 scopus 로고
    • Crystallization and preliminary X-ray data for the A-isozyme of O -acetylserine sulfhydrylase fromSalmonella typhimurium
    • Rao J. G. S., Goldsmith E. J., Mottonen J., Cook P. F. Crystallization and preliminary X-ray data for the A-isozyme of O -acetylserine sulfhydrylase fromSalmonella typhimurium. J. Mol. Biol. 231:1993;1130-1132.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1130-1132
    • Rao, J.G.S.1    Goldsmith, E.J.2    Mottonen, J.3    Cook, P.F.4
  • 38
    • 0029844625 scopus 로고    scopus 로고
    • A change in the internal aldimine lysine (K42) in O -acetylserine sulfhydrylase to alanine indicates a role for the lysine in transimination and as a general base catalyst
    • Rege V., Tai C.-H., Kredich N. M., Karsten W. E., Schnackerz K. D., Cook P. F. A change in the internal aldimine lysine (K42) in O -acetylserine sulfhydrylase to alanine indicates a role for the lysine in transimination and as a general base catalyst. Biochemistry. 35:1996;13485-13493.
    • (1996) Biochemistry , vol.35 , pp. 13485-13493
    • Rege, V.1    Tai, C.-H.2    Kredich, N.M.3    Karsten, W.E.4    Schnackerz, K.D.5    Cook, P.F.6
  • 40
    • 0030800147 scopus 로고    scopus 로고
    • 2complex with ligands bound to the active sites of the α- And β-subunits reveal ligand-induced conformational changes
    • 2complex with ligands bound to the active sites of the α- and β-subunits reveal ligand-induced conformational changes. Biochemistry. 36:1997;7664-7680.
    • (1997) Biochemistry , vol.36 , pp. 7664-7680
    • Rhee, S.1    Parris, K.D.2    Hyde, C.C.3    Ahmed, S.A.4    Miles, E.W.5    Davies, D.R.6
  • 41
    • 0016860244 scopus 로고
    • Stereochemistry of β-replacement reactions catalyzed by tyrosine phenol lyase
    • Sawada S., Kimagai H., Yamada H., Hill R. K. Stereochemistry of β-replacement reactions catalyzed by tyrosine phenol lyase. J. Am. Chem. Soc. 97:1975;4334-4337.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 4334-4337
    • Sawada, S.1    Kimagai, H.2    Yamada, H.3    Hill, R.K.4
  • 42
    • 0017310098 scopus 로고
    • Stereochemistry and mechanism of reactions catalyzed by tryptophanase and tryptophan synthase
    • Schleicher E., Mascaro K., Potts R., Mann D. R., Floss H. G. Stereochemistry and mechanism of reactions catalyzed by tryptophanase and tryptophan synthase. J. Am. Chem. Soc. 98:1976;1043-1044.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 1043-1044
    • Schleicher, E.1    Mascaro, K.2    Potts, R.3    Mann, D.R.4    Floss, H.G.5
  • 43
    • 0029089919 scopus 로고
    • Identification and characterization of the external aldimine intermediate of the O -acetylserine sulfhydrylase reaction
    • Schnackerz K. D., Tai C.-H., Simmons J. W. III, Jacobson T. M., Rao G. S. J., Cook P. F. Identification and characterization of the external aldimine intermediate of the O -acetylserine sulfhydrylase reaction. Biochemistry. 34:1995;12152-12160.
    • (1995) Biochemistry , vol.34 , pp. 12152-12160
    • Schnackerz, K.D.1    Tai, C.-H.2    Simmons J.W. III3    Jacobson, T.M.4    Rao, G.S.J.5    Cook, P.F.6
  • 45
    • 0016385611 scopus 로고
    • Stereochemistry of the tryptophan synthase reaction
    • Skye G. E., Potts R., Floss H. G. Stereochemistry of the tryptophan synthase reaction. J. Am. Chem. Soc. 96:1974;1593-1595.
    • (1974) J. Am. Chem. Soc. , vol.96 , pp. 1593-1595
    • Skye, G.E.1    Potts, R.2    Floss, H.G.3
  • 46
    • 0030059159 scopus 로고    scopus 로고
    • Tryptophan luminescence as a probe of enzyme conformation along the O -acetylserine sulfhydrylase reaction pathway
    • Strambini G. B., Cioni P., Cook P. F. Tryptophan luminescence as a probe of enzyme conformation along the O -acetylserine sulfhydrylase reaction pathway. Biochemistry. 35:1996;8392-8400.
    • (1996) Biochemistry , vol.35 , pp. 8392-8400
    • Strambini, G.B.1    Cioni, P.2    Cook, P.F.3
  • 47
    • 0027183564 scopus 로고
    • Kinetic mechanisms of O -acetylserine sulfhydrylases A and B from Salmonella typhimurium with natural and alternate substrates
    • Tai C.-H., Nalabolu S. R., Jacobson T. M., Minter D. E., Cook P. F. Kinetic mechanisms of O -acetylserine sulfhydrylases A and B from Salmonella typhimurium with natural and alternate substrates. Biochemistry. 32:1993;6433-6442.
    • (1993) Biochemistry , vol.32 , pp. 6433-6442
    • Tai, C.-H.1    Nalabolu, S.R.2    Jacobson, T.M.3    Minter, D.E.4    Cook, P.F.5
  • 48
    • 0029093707 scopus 로고
    • PH dependence of kinetic parameters for O -acetylserine sulfhydrylases A and B from Salmonella typhimurium
    • Tai C.-H., Nalabolu S. R., Jacobson T. M., Simmons J. W. III, Cook P. F. pH dependence of kinetic parameters for O -acetylserine sulfhydrylases A and B from Salmonella typhimurium. Biochemistry. 34:1995;12311-12322.
    • (1995) Biochemistry , vol.34 , pp. 12311-12322
    • Tai, C.-H.1    Nalabolu, S.R.2    Jacobson, T.M.3    Simmons J.W. III4    Cook, P.F.5
  • 49
    • 0029865896 scopus 로고    scopus 로고
    • Formation of the α-aminoacrylate inter mediate limits in the overall reaction catalyzed by O -acetylserine sulfhydrylase
    • Woehl E., Tai C.-H., Dunn M. F., Cook P. F. Formation of the α-aminoacrylate inter mediate limits in the overall reaction catalyzed by O -acetylserine sulfhydrylase. Biochemistry. 35:1996;4776-4783.
    • (1996) Biochemistry , vol.35 , pp. 4776-4783
    • Woehl, E.1    Tai, C.-H.2    Dunn, M.F.3    Cook, P.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.