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Volumn 187, Issue 7, 2005, Pages 2386-2394

Characterization of the acetate binding pocket in the Methanosarcina thermophila acetate kinase

Author keywords

[No Author keywords available]

Indexed keywords

ACETATE KINASE; ADENOSINE DIPHOSPHATE; BUTYRIC ACID DERIVATIVE; CARBOXYL GROUP; CARBOXYLIC ACID;

EID: 15244359850     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.7.2386-2394.2005     Document Type: Article
Times cited : (39)

References (41)
  • 1
    • 0024297194 scopus 로고
    • Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis
    • Aceti, D. J., and J. G. Ferry. 1988. Purification and characterization of acetate kinase from acetate-grown Methanosarcina thermophila. Evidence for regulation of synthesis. J. Biol. Chem. 263:15444-15448.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15444-15448
    • Aceti, D.J.1    Ferry, J.G.2
  • 2
    • 0032518372 scopus 로고    scopus 로고
    • The mechanism of regulation of hexokinase: New insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate
    • Aleshin, A. E., C. Zeng, G. P. Bourenkov, H. D. Bartunik, H. J. Fromm, and R. B. Honzatko. 1998. The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate. Structure 6:39-50.
    • (1998) Structure , vol.6 , pp. 39-50
    • Aleshin, A.E.1    Zeng, C.2    Bourenkov, G.P.3    Bartunik, H.D.4    Fromm, H.J.5    Honzatko, R.B.6
  • 5
    • 0031573453 scopus 로고    scopus 로고
    • Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability
    • Auerbach, G., R. Huber, M. Grattinger, K. Zaiss, H. Schurig, R. Jaenicke, and U. Jacob. 1997. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure 5:1475-1483.
    • (1997) Structure , vol.5 , pp. 1475-1483
    • Auerbach, G.1    Huber, R.2    Grattinger, M.3    Zaiss, K.4    Schurig, H.5    Jaenicke, R.6    Jacob, U.7
  • 6
    • 0018781487 scopus 로고
    • 18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase
    • 18O]triphosphate and the mechanistic consequences for the reactions catalyzed by glycerol kinase, hexokinase, pyruvate kinase, and acetate kinase. Biochemistry 18:3927-3933.
    • (1979) Biochemistry , vol.18 , pp. 3927-3933
    • Blattler, W.A.1    Knowles, J.R.2
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0035158122 scopus 로고    scopus 로고
    • Urkinase: Structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases
    • Buss, K. A., D. R. Cooper, C. Ingram-Smith, J. G. Ferry, D. A. Sanders, and M. S. Hasson. 2001. Urkinase: structure of acetate kinase, a member of the ASKHA superfamily of phosphotransferases. J. Bacteriol. 183:680-686.
    • (2001) J. Bacteriol. , vol.183 , pp. 680-686
    • Buss, K.A.1    Cooper, D.R.2    Ingram-Smith, C.3    Ferry, J.G.4    Sanders, D.A.5    Hasson, M.S.6
  • 9
    • 0031457064 scopus 로고    scopus 로고
    • Crystallization of acetate kinase from Methanosarcina thermophila and prediction of its fold
    • Buss, K. A., C. Ingram-Smith, J. G. Ferry, D. A. Sanders, and M. S. Hasson. 1997. Crystallization of acetate kinase from Methanosarcina thermophila and prediction of its fold. Protein Sci. 6:2659-2662.
    • (1997) Protein Sci. , vol.6 , pp. 2659-2662
    • Buss, K.A.1    Ingram-Smith, C.2    Ferry, J.G.3    Sanders, D.A.4    Hasson, M.S.5
  • 10
    • 0033596853 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli glycerol kinase variant S58→W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion
    • Bystrom, C. E., D. W. Pettigrew, B. P. Branchaud, P. O'Brien, and S. J. Remington. 1999. Crystal structures of Escherichia coli glycerol kinase variant S58→W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion. Biochemistry 38:3508-3518.
    • (1999) Biochemistry , vol.38 , pp. 3508-3518
    • Bystrom, C.E.1    Pettigrew, D.W.2    Branchaud, B.P.3    O'Brien, P.4    Remington, S.J.5
  • 11
    • 0027318150 scopus 로고
    • Change in direction of flagellar rotation in Escherichia coli mediated by acetate kinase
    • Dailey, F. E., and H. C. Berg. 1993. Change in direction of flagellar rotation in Escherichia coli mediated by acetate kinase. J. Bacteriol. 175:3236-3239.
    • (1993) J. Bacteriol. , vol.175 , pp. 3236-3239
    • Dailey, F.E.1    Berg, H.C.2
  • 12
    • 0030838597 scopus 로고    scopus 로고
    • Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila
    • Ferry, J. G. 1997. Enzymology of the fermentation of acetate to methane by Methanosarcina thermophila. Biofactors 6:25-35.
    • (1997) Biofactors , vol.6 , pp. 25-35
    • Ferry, J.G.1
  • 13
    • 0022967087 scopus 로고
    • Phosphate transfer between acetate kinase and enzyme I of the bacterial phosphotransferase system
    • Fox, D. K., N. D. Meadow, and S. Roseman. 1986. Phosphate transfer between acetate kinase and enzyme I of the bacterial phosphotransferase system. J. Biol. Chem. 261:13498-13503.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13498-13503
    • Fox, D.K.1    Meadow, N.D.2    Roseman, S.3
  • 14
    • 15444365167 scopus 로고    scopus 로고
    • Structural and kinetic analyses of arginine residues in the active-site of the acetate kinase from Methanosarcina thermophila
    • in press
    • Gorrell, A., S. H. Lawrence, and J. G. Ferry. Structural and kinetic analyses of arginine residues in the active-site of the acetate kinase from Methanosarcina thermophila. J. Biol. Chem., in press.
    • J. Biol. Chem.
    • Gorrell, A.1    Lawrence, S.H.2    Ferry, J.G.3
  • 15
    • 0029948487 scopus 로고    scopus 로고
    • The sugar kinase/heat shock protein 70/actin superfamily: Implications of conserved structure for mechanism
    • Hurley, J. H. 1996. The sugar kinase/heat shock protein 70/actin superfamily: implications of conserved structure for mechanism. Annu. Rev. Biophys. Biomol. Struct. 25:137-162.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 137-162
    • Hurley, J.H.1
  • 16
    • 0034721788 scopus 로고    scopus 로고
    • The role of histidines in the acetate kinase from Methanosarcina thermophila
    • Ingram-Smith, C., R. D. Barber, and J. G. Ferry. 2000. The role of histidines in the acetate kinase from Methanosarcina thermophila. J. Biol. Chem. 275:33765-33770.
    • (2000) J. Biol. Chem. , vol.275 , pp. 33765-33770
    • Ingram-Smith, C.1    Barber, R.D.2    Ferry, J.G.3
  • 17
    • 84889120137 scopus 로고
    • Improved methods for binding 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 binding 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
  • 19
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt, G. J., and T. A. Jones. 1994. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. Sect. D 50:178-185.
    • (1994) Acta Crystallogr. Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 20
    • 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. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0027382864 scopus 로고
    • Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila
    • Latimer, M. T., and J. G. Ferry. 1993. Cloning, sequence analysis, and hyperexpression of the genes encoding phosphotransacetylase and acetate kinase from Methanosarcina thermophila. J. Bacteriol. 175:6822-6829.
    • (1993) J. Bacteriol. , vol.175 , pp. 6822-6829
    • Latimer, M.T.1    Ferry, J.G.2
  • 24
    • 0002758108 scopus 로고
    • Enzymatic synthesis of acetyl phosphate
    • Lipmann, F. 1944. Enzymatic synthesis of acetyl phosphate. J. Biol. Chem. 155:55-70.
    • (1944) J. Biol. Chem. , vol.155 , pp. 55-70
    • Lipmann, F.1
  • 25
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D photorealistic molecular graphics
    • Merritt, E., and D. Bacon. 1997. Raster3D photorealistic molecular graphics. Methods Enzymol. 277:505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.1    Bacon, D.2
  • 26
    • 0037151123 scopus 로고    scopus 로고
    • Evidence for a transition state analog, MgADP-aluminum fluoride-acetate, in acetate kinase from Methanosarcina thermophila
    • Miles, R. D., A. Gorrell, and J. G. Ferry. 2002. Evidence for a transition state analog, MgADP-aluminum fluoride-acetate, in acetate kinase from Methanosarcina thermophila. J. Biol. Chem. 277:22547-22552.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22547-22552
    • Miles, R.D.1    Gorrell, A.2    Ferry, J.G.3
  • 27
    • 0035976897 scopus 로고    scopus 로고
    • Site-directed mutational analysis of active site residues in the acetate kinase from Methanosarcina thermophila
    • Miles, R. D., P. P. Iyer, and J. G. Ferry. 2001. Site-directed mutational analysis of active site residues in the acetate kinase from Methanosarcina thermophila. J. Biol. Chem. 276:45059-45064.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45059-45064
    • Miles, R.D.1    Iyer, P.P.2    Ferry, J.G.3
  • 29
    • 0037406882 scopus 로고    scopus 로고
    • Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol
    • Palacios, S., V. J. Starai, and J. C. Escalante-Semerena. 2003. Propionyl coenzyme A is a common intermediate in the 1,2-propanediol and propionate catabolic pathways needed for expression of the prpBCDE operon during growth of Salmonella enterica on 1,2-propanediol. J. Bacteriol. 185:2802-2810.
    • (2003) J. Bacteriol. , vol.185 , pp. 2802-2810
    • Palacios, S.1    Starai, V.J.2    Escalante-Semerena, J.C.3
  • 30
    • 0032518195 scopus 로고    scopus 로고
    • Conserved active site aspartates and domain-domain interactions in regulatory properties of the sugar kinase superfamily
    • Pettigrew, D. W., G. B. Smith, K. P. Thomas, and D. C. Dodds. 1998. Conserved active site aspartates and domain-domain interactions in regulatory properties of the sugar kinase superfamily. Arch. Biochem. Biophys. 349:236-245.
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 236-245
    • Pettigrew, D.W.1    Smith, G.B.2    Thomas, K.P.3    Dodds, D.C.4
  • 32
    • 0031932848 scopus 로고    scopus 로고
    • Identification of essential glutamates in the acetate kinase from Methanosarcina thermophila
    • Erratum, J. Bacteriol. 180: 3018
    • Singh-Wissmann, K., C. Ingram-Smith, R. D. Miles, and J. G. Ferry. 1998. Identification of essential glutamates in the acetate kinase from Methanosarcina thermophila. J. Bacteriol. 180:1129-1134. (Erratum, J. Bacteriol. 180: 3018.)
    • (1998) J. Bacteriol. , vol.180 , pp. 1129-1134
    • Singh-Wissmann, K.1    Ingram-Smith, C.2    Miles, R.D.3    Ferry, J.G.4
  • 33
    • 0034603706 scopus 로고    scopus 로고
    • Identification of essential arginines in the acetate kinase from Methanosarcina thermophila
    • Singh-Wissmann, K., R. D. Miles, C. Ingram-Smith, and J. G. Ferry. 2000. Identification of essential arginines in the acetate kinase from Methanosarcina thermophila. Biochemistry 39:3671-3677.
    • (2000) Biochemistry , vol.39 , pp. 3671-3677
    • Singh-Wissmann, K.1    Miles, R.D.2    Ingram-Smith, C.3    Ferry, J.G.4
  • 34
    • 0017091311 scopus 로고
    • Escherichia coli acetate kinase mechanism studied by net initial rate, equilibrium, and independent isotopic exchange kinetics
    • Skarstedt, M. T., and E. Silverstein. 1976. Escherichia coli acetate kinase mechanism studied by net initial rate, equilibrium, and independent isotopic exchange kinetics. J. Biol. Chem. 251:6775-6783.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6775-6783
    • Skarstedt, M.T.1    Silverstein, E.2
  • 35
    • 0011063236 scopus 로고
    • Acetate kinase: A triple-displacement enzyme
    • Spector, L. B. 1980. Acetate kinase: a triple-displacement enzyme. Proc. Natl. Acad. Sci. USA 77:2626-2630.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2626-2630
    • Spector, L.B.1
  • 37
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 38
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., T. J. Gibson, F. Plewniak, F. Jeanmougin, and D. G. Higgins. 1997. The CLUSTAL_X Windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 39
    • 0016275998 scopus 로고
    • Evidence for the formation of a gamma-phosphorylated glutamyl residue in the Escherichia coli acetate kinase reaction
    • Todhunter, J. A., and D. L. Purich. 1974. Evidence for the formation of a gamma-phosphorylated glutamyl residue in the Escherichia coli acetate kinase reaction. Biochem. Biophys. Res. Commun. 60:273-280.
    • (1974) Biochem. Biophys. Res. Commun. , vol.60 , pp. 273-280
    • Todhunter, J.A.1    Purich, D.L.2
  • 40
    • 0017129535 scopus 로고
    • A kinetically important phosphoryl-enzyme intermediary in the intrinsic purine nucleoside-5′-diphosphokinase activity of Escherichia coli acetate kinase
    • Todhunter, J. A., K. B. Reichel, and D. L. Purich. 1976. A kinetically important phosphoryl-enzyme intermediary in the intrinsic purine nucleoside-5′-diphosphokinase activity of Escherichia coli acetate kinase. Arch. Biochem. Biophys. 174:120-128.
    • (1976) Arch. Biochem. Biophys. , vol.174 , pp. 120-128
    • Todhunter, J.A.1    Reichel, K.B.2    Purich, D.L.3


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