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Volumn 12, Issue 1, 2011, Pages

Comparative thermodynamic studies on substrate and product binding of O-Acetylserine Sulfhydrylase reveals two different ligand recognition modes

Author keywords

Enthalpy; Entropy; Fluorescence; Isothermal Titration Calorimetry; Ligand Binding

Indexed keywords

CYSTEINE; CYSTEINE SYNTHASE; METHIONINE; DRUG DERIVATIVE; LIGAND; O ACETYLSERINE; O-ACETYLSERINE; SERINE; SODIUM CHLORIDE;

EID: 79957793364     PISSN: None     EISSN: 14712091     Source Type: Journal    
DOI: 10.1186/1471-2091-12-31     Document Type: Article
Times cited : (5)

References (36)
  • 1
    • 0014670046 scopus 로고
    • Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium
    • 4977445
    • Purification and characterization of cysteine synthetase, a bifunctional protein complex, from Salmonella typhimurium. NM Kredich MA Becker GM Tomkins, J Biol Chem 1969 244 2428 2439 4977445
    • (1969) J Biol Chem , vol.244 , pp. 2428-2439
    • Kredich, N.M.1    Becker, M.A.2    Tomkins, G.M.3
  • 2
    • 0017594294 scopus 로고
    • Initial kinetic characterization of the multienzyme complex, cysteine synthetase
    • DOI 10.1016/0003-9861(77)90194-1
    • Initial kinetic characterization of the multienzyme complex, cysteine synthetase. PF Cook RT Wedding, Arch Biochem Biophys 1977 178 293 302 10.1016/0003-9861(77)90194-1 319757 (Pubitemid 8035442)
    • (1977) Archives of Biochemistry and Biophysics , vol.178 , Issue.1 , pp. 293-302
    • Cook, P.F.1    Wedding, R.T.2
  • 3
    • 65649133057 scopus 로고    scopus 로고
    • Assembly of the cysteine synthase complex and the regulatory role of protein-protein interactions
    • 10.1074/jbc.M900154200. 19213732
    • Assembly of the cysteine synthase complex and the regulatory role of protein-protein interactions. S Kumaran H Yi HB Krishnan JM Jez, J Biol Chem 2009 284 10268 10275 10.1074/jbc.M900154200 19213732
    • (2009) J Biol Chem , vol.284 , pp. 10268-10275
    • Kumaran, S.1    Yi, H.2    Krishnan, H.B.3    Jez, J.M.4
  • 4
    • 3042616599 scopus 로고    scopus 로고
    • Structure and mechanism of O-acetylserine sulfhydrylase
    • DOI 10.1074/jbc.R400001200
    • Structure and mechanism of O-acetylserine Sulfhydrylase. WM Rabeh PF Cook, J Biol Chem 2004 279 26803 26806 10.1074/jbc.R400001200 15073190 (Pubitemid 38812512)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 26803-26806
    • Rabeh, W.M.1    Cook, P.F.2
  • 5
    • 33644685874 scopus 로고    scopus 로고
    • Molecular basis of cysteine biosynthesis in plants: Structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana
    • DOI 10.1074/jbc.M505313200
    • Molecular basis of cysteine biosynthesis in plants: structural and functional analysis of O-acetylserine sulfhydrylase from Arabidopsis thaliana. ER Bonner RE Cahoon SM Knapke JM Jez, J Biol Chem 2005 280 38803 38813 10.1074/jbc.M505313200 16166087 (Pubitemid 43853783)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.46 , pp. 38803-38813
    • Bonner, E.R.1    Cahoon, R.E.2    Knapke, S.M.3    Jez, J.M.4
  • 6
    • 0027183564 scopus 로고
    • Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants
    • Kinetic mechanisms of the A and B isozymes of O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2 using the natural and alternative reactants. CH Tai SR Nalabolu TM Jacobson DE Minter PF Cook, Biochemistry 1993 32 6433 6442 10.1021/bi00076a017 8518286 (Pubitemid 23208827)
    • (1993) Biochemistry , vol.32 , Issue.25 , pp. 6433-6442
    • Tai, C.-H.1    Nalabolu, S.R.2    Jacobson, T.M.3    Minter, D.E.4    Cook, P.F.5
  • 7
    • 0035313606 scopus 로고    scopus 로고
    • Plant concepts for mineral acquisition and allocation
    • DOI 10.1016/S0958-1669(00)00193-2
    • Plant concepts for mineral acquisition and allocation. R Hell H Hillebrand, Curr Opin Biotech 2001 12 161 168 10.1016/S0958-1669(00)00193-2 11287231 (Pubitemid 32247402)
    • (2001) Current Opinion in Biotechnology , vol.12 , Issue.2 , pp. 161-168
    • Hell, R.1    Hillebrand, H.2
  • 9
    • 0020686355 scopus 로고
    • Biochemistry of sulfur-containing amino acids
    • Biochemistry of sulfur-containing amino acids. AJ Cooper, Annu Rev Biochem 1983 53 187 222
    • (1983) Annu Rev Biochem , vol.53 , pp. 187-222
    • Cooper, A.J.1
  • 10
    • 0034780485 scopus 로고    scopus 로고
    • Nonreplicating persistence of Mycobacterium tuberculosis
    • DOI 10.1146/annurev.micro.55.1.139
    • Non replicating persistence of Mycobacterium tuberculosis. LG Wayne CD Schoskey, Annu Rev Microbiol 2001 55 139 163 10.1146/annurev.micro.55.1.139 11544352 (Pubitemid 32978103)
    • (2001) Annual Review of Microbiology , vol.55 , pp. 139-163
    • Wayne, L.G.1    Sohaskey, C.D.2
  • 11
    • 0036271841 scopus 로고    scopus 로고
    • Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo
    • DOI 10.1046/j.1365-2958.2002.02771.x
    • Functional genomics reveals the sole sulphate transporter of the Mycobacterium tuberculosis complex and its relevance to the acquisition of sulphur in vivo. E Wooff SL Michell SV Gordon MA Chambers S Bardarov WR Jacobs Jr RG Hewinson PR Wheeler, Mol Microbiol 2002 43 653 663 10.1046/j.1365-2958. 2002.02771.x 11929522 (Pubitemid 34597260)
    • (2002) Molecular Microbiology , vol.43 , Issue.3 , pp. 653-663
    • Wooff, E.1    Michell, S.Ll.2    Gordon, S.V.3    Chambers, M.A.4    Bardarov, S.5    Jacobs Jr., W.R.6    Hewinson, R.G.7    Wheeler, P.R.8
  • 12
    • 57349162179 scopus 로고    scopus 로고
    • L-Cysteine is required for induced antibiotic resistance in actively swarming S. enterica serovar typhimurium
    • 10.1099/mic.0.2008/020347-0. 18957594
    • L-Cysteine is required for induced antibiotic resistance in actively swarming S. enterica serovar typhimurium. AL Turbull MG Survette, Microbiology 2008 154 3410 3415 10.1099/mic.0.2008/020347-0 18957594
    • (2008) Microbiology , vol.154 , pp. 3410-3415
    • Turbull, A.L.1    Survette, M.G.2
  • 15
    • 0033609810 scopus 로고    scopus 로고
    • Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium
    • DOI 10.1006/jmbi.1999.3002
    • Ligand binding induces a large conformational change in O-acetylserine sulfhydrylase from Salmonella typhimurium. P Burkhard CH Tai CM Ristroph PF Cook JN Jansonius, J Mol Biol 1999 291 941 953 10.1006/jmbi.1999.3002 10452898 (Pubitemid 29403622)
    • (1999) Journal of Molecular Biology , vol.291 , Issue.4 , pp. 941-953
    • Burkhard, P.1    Tai, C.-H.2    Ristroph, C.M.3    Cook, P.F.4    Jansonius, J.N.5
  • 16
    • 17644423923 scopus 로고    scopus 로고
    • The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase
    • DOI 10.1128/JB.187.9.3201-3205.2005
    • The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. B Huang MW Vetting, J Bacteriol 2005 187 3201 3205 10.1128/JB.187.9.3201-3205.2005 15838047 (Pubitemid 40571613)
    • (2005) Journal of Bacteriology , vol.187 , Issue.9 , pp. 3201-3205
    • Huang, B.1    Vetting, M.W.2    Roderick, S.L.3
  • 17
    • 0029089919 scopus 로고
    • Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction
    • 10.1021/bi00038a008. 7547955
    • Identification and spectral characterization of the external aldimine of the O-acetylserine sulfhydrylase reaction. KD Schnackerz CH Tai JW Simmons TM Jacobson GS Rao PF Cook, Biochemistry 1995 34 12152 12160 10.1021/bi00038a008 7547955
    • (1995) Biochemistry , vol.34 , pp. 12152-12160
    • Schnackerz, K.D.1    Tai, C.H.2    Simmons, J.W.3    Jacobson, T.M.4    Rao, G.S.5    Cook, P.F.6
  • 18
    • 51349147518 scopus 로고    scopus 로고
    • Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: Structural evidence for cysteine binding and lack of interactions with serine acetyl transferase
    • 10.1002/prot.22013. 21644255
    • Crystal structure of native O-acetyl-serine sulfhydrylase from Entamoeba histolytica and its complex with cysteine: structural evidence for cysteine binding and lack of interactions with serine acetyl transferase. K Chinthalapudi M Kumar S Kumar S Jain N Alam S Gourinath, Proteins; Struc Funct Bioinform 2008 72 1222 1232 10.1002/prot.22013 21644255
    • (2008) Proteins; Struc Funct Bioinform , vol.72 , pp. 1222-1232
    • Chinthalapudi, K.1    Kumar, M.2    Kumar, S.3    Jain, S.4    Alam, N.5    Gourinath, S.6
  • 19
    • 34548188995 scopus 로고    scopus 로고
    • Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis: Crystal structures of the enzyme α-aminoacrylate intermediate and an enzyme-inhibitor complex
    • DOI 10.1074/jbc.M703518200
    • Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis: crystal structures of the enzyme -aminoacrylate intermediate and an enzyme-inhibitor complex. R Schnell W Oehlmann M Singh G Schneider, J Biol Chem 2007 282 23473 23481 10.1074/jbc.M703518200 17567578 (Pubitemid 47311931)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.32 , pp. 23473-23481
    • Schnell, R.1    Oehlmann, W.2    Singh, M.3    Schneider, G.4
  • 20
    • 0017281552 scopus 로고
    • A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2
    • 773932
    • A reaction mechanism from steady state kinetic studies for O-acetylserine sulfhydrylase from Salmonella typhimurium LT-2. PF Cook RT Wedding, J Biol Chem 1976 251 2023 2029 773932
    • (1976) J Biol Chem , vol.251 , pp. 2023-2029
    • Cook, P.F.1    Wedding, R.T.2
  • 21
    • 0017386141 scopus 로고
    • Overall mechanism and rate equation for O acetylserine sulfhydrylase
    • Overall mechanism and rate equation for O-acetylserine sulfhydrylase. PF Cook RT Wedding, J Biol Chem 1977 252 3459 863890 (Pubitemid 8113937)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.10 , pp. 3459
    • Cook, P.F.1    Wedding, R.T.2
  • 22
    • 33645319676 scopus 로고    scopus 로고
    • Overcoming roadblocks in lead optimization: A thermodynamic perspective
    • DOI 10.1111/j.1747-0285.2005.00314.x
    • Overcoming road blocks in lead optimization: A thermodynamic perpective. AJ Ruben Y Kiso E Frierie, Chem Biol Drug Design 2006 67 2 4 10.1111/j.1747-0285.2005.00314.x (Pubitemid 43881382)
    • (2006) Chemical Biology and Drug Design , vol.67 , Issue.1 , pp. 2-4
    • Ruben, A.J.1    Kiso, Y.2    Freire, E.3
  • 23
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • DOI 10.1016/0003-2697(89)90213-3
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter. T Wiseman S Williston JF Brandts LN Lin, Anal Biochem 1989 179 131 137 10.1016/0003-2697(89)90213-3 2757186 (Pubitemid 19149635)
    • (1989) Analytical Biochemistry , vol.179 , Issue.1 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 24
    • 23644440099 scopus 로고    scopus 로고
    • Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: Evidence from fluorescence spectroscopy
    • DOI 10.1110/ps.051492805
    • Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: Evidence from fluorescence spectroscopy. B Campanini F Speroni E Salsi PF Cook SL Roderick B Huang S Bettati A Mozzarelli, Protein Sci 2005 14 2115 2124 10.1110/ps.051492805 15987896 (Pubitemid 41132377)
    • (2005) Protein Science , vol.14 , Issue.8 , pp. 2115-2124
    • Campanini, B.1    Speroni, F.2    Salsi, E.3    Cook, P.F.4    Roderick, S.L.5    Huang, B.6    Bettati, S.7    Mozzarelli, A.8
  • 26
    • 0029844625 scopus 로고    scopus 로고
    • A change in internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst
    • 10.1021/bi961517j. 8873618
    • A change in internal aldimine lysine (K42) in O-acetylserine sulfhydrylase to alanine indicates its importance in transimination and as a general base catalyst. VD Rege NM Kredich CH Tai WE Karsten KD Schnackerz PF Cook, Biochemistry 1996 35 13485 13495 10.1021/bi961517j 8873618
    • (1996) Biochemistry , vol.35 , pp. 13485-13495
    • Rege, V.D.1    Kredich, N.M.2    Tai, C.H.3    Karsten, W.E.4    Schnackerz, K.D.5    Cook, P.F.6
  • 27
    • 0029865896 scopus 로고    scopus 로고
    • Formation of the α-aminoacrylate intermediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase
    • DOI 10.1021/bi952938o
    • Formation of the -aminoacrylate intermediate limits the overall reaction catalyzed by O-acetyl serine sulfhydrylase. EU Woehl CH Tai MF Dunn PF Cook, Biochemistry 1996 35 4776 4783 10.1021/bi952938o 8664267 (Pubitemid 26126695)
    • (1996) Biochemistry , vol.35 , Issue.15 , pp. 4776-4783
    • Woehl, E.U.1    Tai, C.-H.2    Dunn, M.F.3    Cook, P.F.4
  • 28
    • 0032539677 scopus 로고    scopus 로고
    • Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping
    • DOI 10.1073/pnas.95.4.1505
    • Structure of the complex between a cap analogue and mRNA guanyl transferase demonstrates the structural chemistry of RNA-capping. K Hakansson DB Wigley, Proc Natl Acad Sci USA 1998 95 1505 1510 10.1073/pnas.95.4.1505 9465045 (Pubitemid 28103422)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.4 , pp. 1505-1510
    • Hakansson, K.1    Wigley, D.B.2
  • 29
    • 0036416144 scopus 로고    scopus 로고
    • TROSY-NMR studies of the 91 kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility
    • DOI 10.1016/S0022-2836(02)00940-3
    • TROSY-NMR studies of the 91 kDa protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility. C McElroy A Manfredo A Wendt P Gollnick M Foster, J Mol Biol 2002 323 463 473 10.1016/S0022-2836(02) 00940-3 12381302 (Pubitemid 35291050)
    • (2002) Journal of Molecular Biology , vol.323 , Issue.3 , pp. 463-473
    • McElroy, C.1    Manfredo, A.2    Wendt, A.3    Gollnick, P.4    Foster, M.5
  • 30
    • 33749238188 scopus 로고    scopus 로고
    • Contribution of ligand desolvation to binding thermodynamics in a ligand-protein interaction
    • DOI 10.1002/anie.200602227
    • Contribution of ligand desolvation to binding thermodynamics in a ligand-protein interaction. N Shimokhina A Bronowska SW Homans, Angrew Chem Int Ed 2006 45 6374 6376 10.1002/anie.200602227 (Pubitemid 44483868)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.38 , pp. 6374-6376
    • Shimokhina, N.1    Bronowska, A.2    Homans, S.W.3
  • 31
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces. WC Wimley SH White, Nat Struct Biol 1996 10 842 848 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 32
    • 7644232169 scopus 로고
    • Rates of bimolecular substitution reaction
    • Rates of bimolecular substitution reaction. AJ Parker, Adv Phys Org Chem 1967 5 173 175
    • (1967) Adv Phys Org Chem , vol.5 , pp. 173-175
    • Parker, A.J.1
  • 34
    • 0000810027 scopus 로고
    • Active site of -chymotrypsin activation by association-desolvation
    • 10.1073/pnas.66.2.249. 16591836
    • Active site of -chymotrypsin activation by association-desolvation. SG Cohen VM Vaidya RM Schultz, Proc Natl Acad Sci USA 1970 66 249 256 10.1073/pnas.66.2.249 16591836
    • (1970) Proc Natl Acad Sci USA , vol.66 , pp. 249-256
    • Cohen, S.G.1    Vaidya, V.M.2    Schultz, R.M.3
  • 35
    • 0032125745 scopus 로고    scopus 로고
    • Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants. Structural and kinetic properties of the free and bound enzymes
    • Interactions between serine acetyl tranferase and O-acetylserine (thiol) lyase in higher plants-structural and kinetic properties of the free enzyme and bound enzymes. M Droux ML Ruffet R Douce D Job, E J Biochem 1998 255 235 245 10.1046/j.1432-1327.1998.2550235.x (Pubitemid 28316858)
    • (1998) European Journal of Biochemistry , vol.255 , Issue.1 , pp. 235-245
    • Droux, M.1    Ruffet, M.-L.2    Douce, R.3    Job, D.4
  • 36
    • 0037336269 scopus 로고    scopus 로고
    • High levels of intracellular cysteine promote oxidative DNA damage by driving the Fenton reaction
    • DOI 10.1128/JB.185.6.1942-1950.2003
    • High levels of intracellular cysteine promote oxidative DNA damage by driving the fenton reaction. S Park JA Imlay, J Bactriol 2003 185 1942 1950 10.1128/JB.185.6.1942-1950.2003 (Pubitemid 36297894)
    • (2003) Journal of Bacteriology , vol.185 , Issue.6 , pp. 1942-1950
    • Park, S.1    Imlay, J.A.2


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