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Volumn 187, Issue 9, 2005, Pages 3201-3205

The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE SYNTHASE; SERINE ACETYLTRANSFERASE;

EID: 17644423923     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.9.3201-3205.2005     Document Type: Article
Times cited : (81)

References (32)
  • 1
    • 0014669977 scopus 로고
    • The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium
    • Becker, M. A., N. M. Kredich, and G. M. Tomkins. 1969. The purification and characterization of O-acetylserine sulfhydrylase-A from Salmonella typhimurium. J. Biol. Chem. 244:2418-2427.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2418-2427
    • Becker, M.A.1    Kredich, N.M.2    Tomkins, G.M.3
  • 4
    • 0034692879 scopus 로고    scopus 로고
    • Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: Structure of the enzyme with chloride bound
    • Burkhard, P., C. H. Tai, J. N. Jansonius, and P. F. Cook. 2000. Identification of an allosteric anion-binding site on O-acetylserine sulfhydrylase: structure of the enzyme with chloride bound. J. Mol. Biol. 303:279-286.
    • (2000) J. Mol. Biol. , vol.303 , pp. 279-286
    • Burkhard, P.1    Tai, C.H.2    Jansonius, J.N.3    Cook, P.F.4
  • 5
    • 0033609810 scopus 로고    scopus 로고
    • Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium
    • Burkhard, P., C. H. Tai, C. M. Ristroph, P. F. Cook, and J. N. Jansonius. 1999. Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. J. Mol. Biol. 291:941-953.
    • (1999) J. Mol. Biol. , vol.291 , pp. 941-953
    • Burkhard, P.1    Tai, C.H.2    Ristroph, C.M.3    Cook, P.F.4    Jansonius, J.N.5
  • 6
    • 0018265576 scopus 로고
    • Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers
    • Cook, P. F., and R. T. Wedding. 1978. Cysteine synthetase from Salmonella typhimurium LT-2. Aggregation, kinetic behavior, and effect of modifiers. J. Biol. Chem. 253:7874-7879.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7874-7879
    • Cook, P.F.1    Wedding, R.T.2
  • 8
    • 16644396746 scopus 로고    scopus 로고
    • Structure of serine acetyltransferase from Haemophilus influenzae Rd
    • Gorman, J., and L. Shapiro. 2004. Structure of serine acetyltransferase from Haemophilus influenzae Rd. Acta Crystallogr. Sect. D 60:1600-1605.
    • (2004) Acta Crystallogr. Sect. D , vol.60 , pp. 1600-1605
    • Gorman, J.1    Shapiro, L.2
  • 9
    • 0034614424 scopus 로고    scopus 로고
    • Serine acetyltransferase from Escherichia coli is a dimer of trimers
    • Hindson, V. J., P. C. Moody, A. J. Rowe, and W. V. Shaw. 2000. Serine acetyltransferase from Escherichia coli is a dimer of trimers. J. Biol. Chem. 275:461-466.
    • (2000) J. Biol. Chem. , vol.275 , pp. 461-466
    • Hindson, V.J.1    Moody, P.C.2    Rowe, A.J.3    Shaw, W.V.4
  • 10
    • 0037452936 scopus 로고    scopus 로고
    • Random-order ternary complex reaction mechanism of serine acetyltransferase from Escherichia coli
    • Hindson, V. J., and W. V. Shaw. 2003. Random-order ternary complex reaction mechanism of serine acetyltransferase from Escherichia coli. Biochemistry 42:3113-3119.
    • (2003) Biochemistry , vol.42 , pp. 3113-3119
    • Hindson, V.J.1    Shaw, W.V.2
  • 11
    • 10644245071 scopus 로고    scopus 로고
    • Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae
    • Johnson, C. M., B. Huang, S. L. Roderick, and P. F. Cook. 2004. Chemical mechanism of the serine acetyltransferase from Haemophilus influenzae. Biochemistry 43:15534-15539.
    • (2004) Biochemistry , vol.43 , pp. 15534-15539
    • Johnson, C.M.1    Huang, B.2    Roderick, S.L.3    Cook, P.F.4
  • 12
    • 4143109064 scopus 로고    scopus 로고
    • Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae
    • Johnson, C. M., B. Huang, S. L. Roderick, and P. F. Cook. 2004. Kinetic mechanism of the serine acetyltransferase from Haemophilus influenzae. Arch. Biochem. Biophys. 429:115-122.
    • (2004) Arch. Biochem. Biophys. , vol.429 , pp. 115-122
    • Johnson, C.M.1    Huang, B.2    Roderick, S.L.3    Cook, P.F.4
  • 13
    • 9744250218 scopus 로고    scopus 로고
    • The serine acetyltransferase reaction: Acetyl transfer from an acylpantothenyl donor to an alcohol
    • Johnson, C. M., S. L. Roderick, and P. F. Cook. 2005. The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol. Arch. Biochem. Biophys. 433:85-95.
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 85-95
    • Johnson, C.M.1    Roderick, S.L.2    Cook, P.F.3
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J.-Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47:110-119.
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 16
    • 0014670046 scopus 로고
    • Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium
    • Kredich, N. M., M. A. Becker, and G. M. Tomkins. 1969. Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium. J. Biol. Chem. 244:2428-2439.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2428-2439
    • Kredich, N.M.1    Becker, M.A.2    Tomkins, G.M.3
  • 17
    • 0014011576 scopus 로고
    • The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium
    • Kredich, N. M., and G. M. Tomkins. 1966. The enzymic synthesis of L-cysteine in Escherichia coli and Salmonella typhimurium. J. Biol. Chem. 241:4955-4965.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4955-4965
    • Kredich, N.M.1    Tomkins, G.M.2
  • 18
    • 2442709743 scopus 로고
    • The biosynthesis of L-cysteine in Escherichia coli and Salmonella typhimurium by a multifunctional enzyme complex
    • H. J. Vogel, J. O. Lampen, and V. Bryson (ed.) Academic Press, New York, N.Y.
    • Kredich, N. M., and G. M. Tomkins. 1967. The biosynthesis of L-cysteine in Escherichia coli and Salmonella typhimurium by a multifunctional enzyme complex, p. 189-198. In H. J. Vogel, J. O. Lampen, and V. Bryson (ed.), Organizational biosynthesis. Academic Press, New York, N.Y.
    • (1967) Organizational Biosynthesis , pp. 189-198
    • Kredich, N.M.1    Tomkins, G.M.2
  • 19
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthur, S. D. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26:283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, S.D.3    Thornton, J.M.4
  • 20
    • 0034278207 scopus 로고    scopus 로고
    • Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus
    • Mino, K., K. Hiraoka, K. Imamura, T. Sakiyama, N. Eisaki, A. Matsuyama, and K. Nakanishi. 2000. Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus. Biosci. Biotechnol. Biochem. 64:1874-1880.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1874-1880
    • Mino, K.1    Hiraoka, K.2    Imamura, K.3    Sakiyama, T.4    Eisaki, N.5    Matsuyama, A.6    Nakanishi, K.7
  • 21
    • 0035316451 scopus 로고    scopus 로고
    • Increase in the stability of serine acetyltransferase from Escherichia coli against cold inactivation and proteolysis by forming a bienzyme complex
    • Mino, K., K. Imamura, T. Sakiyama, N. Eisaki, A. Matsuyama, and K. Nakanishi. 2001. Increase in the stability of serine acetyltransferase from Escherichia coli against cold inactivation and proteolysis by forming a bienzyme complex. Biosci. Biotechnol. Biochem. 65:865-874.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 865-874
    • Mino, K.1    Imamura, K.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5    Nakanishi, K.6
  • 22
    • 0032610016 scopus 로고    scopus 로고
    • Purification and characterization of serine acetyltransferase from Escherichia coli partially truncated at the C-terminal region
    • Mino, K., T. Yamanoue, T. Sakiyama, N. Eisaki, A. Matsuyama, and K. Nakanishi. 1999. Purification and characterization of serine acetyltransferase from Escherichia coli partially truncated at the C-terminal region. Biosci. Biotechnol. Biochem. 63:168-179.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 168-179
    • Mino, K.1    Yamanoue, T.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5    Nakanishi, K.6
  • 23
    • 0034251888 scopus 로고    scopus 로고
    • Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics
    • Mino, K., T. Yamanoue, T. Sakiyama, N. Eisaki, A. Matsuyama, and K. Nakanishi. 2000. Effects of bienzyme complex formation of cysteine synthetase from Escherichia coli on some properties and kinetics. Biosci. Biotechnol. Biochem. 64:1628-1640.
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1628-1640
    • Mino, K.1    Yamanoue, T.2    Sakiyama, T.3    Eisaki, N.4    Matsuyama, A.5    Nakanishi, K.6
  • 24
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris, R. J., A. Perrakis, and V. S. Lamzin. 2003. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374:229-244.
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 25
    • 2442644099 scopus 로고    scopus 로고
    • Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor
    • Olsen, L. R., B. Huang, M. W. Vetting, and S. L. Roderick. 2004. Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor. Biochemistry 43:6013-6019.
    • (2004) Biochemistry , vol.43 , pp. 6013-6019
    • Olsen, L.R.1    Huang, B.2    Vetting, M.W.3    Roderick, S.L.4
  • 26
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C. W. Carter, Jr., and R. M. Sweet (ed.) Academic Press, New York, N.Y.
    • Otwinoski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode, p. 307-326. In C. W. Carter, Jr., and R. M. Sweet (ed.), Methods in enzymology. Academic Press, New York, N.Y.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinoski, Z.1    Minor, W.2
  • 27
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis, A., R. Morris, and V. S. Lamzin. 1999. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6:458-463.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 28
    • 4644272171 scopus 로고    scopus 로고
    • The structure and mechanism of serine acetyltransferase from Escherichia coli
    • Pye, V. E., A. P. Tingey, R. L. Robson, and P. C. Moody. 2004. The structure and mechanism of serine acetyltransferase from Escherichia coli. J. Biol. Chem. 279:40729-40736.
    • (2004) J. Biol. Chem. , vol.279 , pp. 40729-40736
    • Pye, V.E.1    Tingey, A.P.2    Robson, R.L.3    Moody, P.C.4
  • 29
    • 3042616599 scopus 로고    scopus 로고
    • Structure and mechanism of O-acetylserine sulfhydrylase
    • Rabeh, W. M., and P. F. Cook. 2004. Structure and mechanism of O-acetylserine sulfhydrylase. J. Biol. Chem. 279:26803-26806.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26803-26806
    • Rabeh, W.M.1    Cook, P.F.2
  • 31
    • 0037007971 scopus 로고    scopus 로고
    • Cysteine biosynthetic enzymes are the pieces of a metabolic energy pump
    • Wei, J., Q. X. Tang, O. Varlamova, C. Roche, R. Lee, and T. S. Leyh. 2002. Cysteine biosynthetic enzymes are the pieces of a metabolic energy pump. Biochemistry 41:8493-8498.
    • (2002) Biochemistry , vol.41 , pp. 8493-8498
    • Wei, J.1    Tang, Q.X.2    Varlamova, O.3    Roche, C.4    Lee, R.5    Leyh, T.S.6
  • 32
    • 0034825333 scopus 로고    scopus 로고
    • The cysteine synthase complex from plants. Mitochondrial serine acetyltransferase from Arabidopsis thaliana carries a bifunctional domain for catalysis and protein-protein interaction
    • Wirtz, M., O. Berkowitz, M. Droux, and R. Hell. 2001. The cysteine synthase complex from plants. Mitochondrial serine acetyltransferase from Arabidopsis thaliana carries a bifunctional domain for catalysis and protein-protein interaction. Eur. J. Biochem. 268:686-693.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 686-693
    • Wirtz, M.1    Berkowitz, O.2    Droux, M.3    Hell, R.4


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