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Volumn 48, Issue 36, 2009, Pages 8731-8737

Interactions between large and small subunits of different acetohydroxyacid synthase isozymes of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ACETOHYDROXYACID SYNTHASE; ACTIVATED ENZYMES; CATALYTIC SUBUNITS; FEEDBACK SENSITIVITY; INDUCED DISSOCIATION; N-TERMINALS; NON-SPECIFIC INTERACTIONS; REGULATORY SUBUNITS; SMALL SUBUNITS; SYNTHASES; THIAMIN DIPHOSPHATE-DEPENDENT ENZYMES;

EID: 70149088808     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9009488     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 0035849510 scopus 로고    scopus 로고
    • Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit
    • Lee, Y. T., and Duggleby, R. G. (2001) Identification of the regulatory subunit of Arabidopsis thaliana acetohydroxyacid synthase and reconstitution with its catalytic subunit. Biochemistry 40, 6836-6844.
    • (2001) Biochemistry , vol.40 , pp. 6836-6844
    • Lee, Y.T.1    Duggleby, R.G.2
  • 2
    • 0000660166 scopus 로고    scopus 로고
    • Expression, purification, characterization, and reconstitution of the large and small subunits of yeast acetohydroxyacid synthase
    • Pang, S. S., and Duggleby, R. G. (1999) Expression, purification, characterization, and reconstitution of the large-and small subunits of yeast acetohydroxyacid synthase. Biochemistry 38, 5222-5231. (Pubitemid 129514798)
    • (1999) Biochemistry , vol.38 , Issue.16 , pp. 5222-5231
    • Pang, S.S.1    Duggleby, R.G.2
  • 3
    • 0033167288 scopus 로고    scopus 로고
    • Cloning and functional expression of the small subunit of acetolactate synthase from Nicotiana plumbaginifolia
    • Hershey, H. P., Schwartz, L. J., Gale, J. P., and Abell, L. M. (1999) Cloning and functional expression of the small subunit of acetolactate synthase from Nicotiana plumbaginifolia. Plant. Mol. Biol. 40, 795-806.
    • (1999) Plant. Mol. Biol. , vol.40 , pp. 795-806
    • Hershey, H.P.1    Schwartz, L.J.2    Gale, J.P.3    Abell, L.M.4
  • 4
    • 0017816893 scopus 로고
    • A comparative study of the acetohydroxy acid synthase isozymes of Escherichia coli K-12. Biochim
    • DeFelice, M., Squires, C. H., and Levinthal, M. (1978) A comparative study of the acetohydroxy acid synthase isozymes of Escherichia coli K-12. Biochim. Biophys. Acta 541, 9-17.
    • (1978) Biophys. Acta , vol.541 , pp. 9-17
    • Defelice, M.1    Squires, C.H.2    Levinthal, M.3
  • 6
    • 0021352116 scopus 로고
    • Purification and subunit composition of acetohydroxyacid synthase I from Escherichia coli K-12
    • Eoyang, L., and Silverman, P. M. (1984) Purification and subunit composition of acetohydroxyacid synthase I from Escherichia coli K-12. J. Bacteriol. 157, 184-189. (Pubitemid 14222474)
    • (1984) Journal of Bacteriology , vol.157 , Issue.1 , pp. 184-189
    • Eoyang, L.1    Silverman, P.M.2
  • 7
    • 0023096487 scopus 로고
    • Effects of deletion and insertion mutations in the ilvM gene of Escherichia coli
    • Lu, M. F., and Umbarger, H. E. (1987) Effects of deletion and insertion mutations in the ilvM gene of Escherichia coli. J. Bacteriol. 169, 600-604. (Pubitemid 17010868)
    • (1987) Journal of Bacteriology , vol.169 , Issue.2 , pp. 600-604
    • Lu, M.-F.1    Umbarger, H.E.2
  • 8
    • 0001348712 scopus 로고    scopus 로고
    • Biosynthesis of the Branched Chain Amino Acids
    • (Neidhardt, F. C., Ingraham, J. L., Low, B. L., Magasanik, B., Schaechter, M., and Umbarger, H. E., Eds.) 2nd ed., ASM Press, Washington
    • Umbarger, H. E. (1996) Biosynthesis of the Branched Chain Amino Acids, in Escherichia coli and Salmonella typhimurium. Cellular and molecular biology (Neidhardt, F. C., Ingraham, J. L., Low, B. L., Magasanik, B., Schaechter, M., and Umbarger, H. E., Eds.) 2nd ed., pp 442-457, ASM Press, Washington.
    • (1996) Escherichia Coli and Salmonella Typhimurium. Cellular and Molecular Biology , pp. 442-457
    • Umbarger, H.E.1
  • 9
    • 0026804680 scopus 로고
    • Properties of subcloned subunits of bacterial acetohydroxy acid synthases
    • Weinstock, O., Sella, C., Chipman, D. M., and Barak, Z. (1992) Properties of subcloned subunits of bacterial acetohydroxy acid synthases. J. Bacteriol. 174, 5560-5566.
    • (1992) J. Bacteriol. , vol.174 , pp. 5560-5566
    • Weinstock, O.1    Sella, C.2    Chipman, D.M.3    Barak, Z.4
  • 10
    • 0031857516 scopus 로고    scopus 로고
    • Branched-chain amino acid biosynthesis in Salmonella typhimurium: A quantitative analysis
    • Epelbaum, S., LaRossa, R. A., VanDyk, T. K., Elkayam, T., Chipman, D. M., and Barak, Z. (1998) Branched-chain amino acid biosynthesis in Salmonella typhimurium: a quantitative analysis. J. Bacteriol. 180, 4056-4067. (Pubitemid 28373507)
    • (1998) Journal of Bacteriology , vol.180 , Issue.16 , pp. 4056-4067
    • Epelbaum, S.1    Larossa, R.A.2    Vandyk, T.K.3    Elkayam, T.4    Chipman, D.M.5    Barak, Z.6
  • 11
    • 0030025785 scopus 로고    scopus 로고
    • Metabolic effects of inhibitors of two enzymes of the branched-chain amino acid pathway in Salmonella typhimurium
    • Epelbaum, S., Chipman, D. M., and Barak, Z. (1996) Metabolic effects of inhibitors of two enzymes of the branched-chain amino acid pathway in Salmonella typhimurium. J. Bacteriol. 178, 1187-1196. (Pubitemid 26048039)
    • (1996) Journal of Bacteriology , vol.178 , Issue.4 , pp. 1187-1196
    • Epelbaum, S.1    Chipman, D.M.2    Barak, Z.3
  • 13
    • 0035150199 scopus 로고    scopus 로고
    • High-density microarray-mediated gene expression profiling of Escherichia coli
    • Wei, Y., Lee, J. M., Richmond, C., Blattner, F. R., Rafalski, J. A., and LaRossa, R. A. (2001) High-density microarray-mediated gene expression profiling of Escherichia coli. J. Bacteriol. 183, 545-556.
    • (2001) J. Bacteriol. , vol.183 , pp. 545-556
    • Wei, Y.1    Lee, J.M.2    Richmond, C.3    Blattner, F.R.4    Rafalski, J.A.5    Larossa, R.A.6
  • 14
    • 0008961265 scopus 로고
    • A Need for Metabolic Insulation: Lessons from Sulfonylurea Genetics
    • Barak, Z., Chipman, D. M., and Schloss, J. V., Eds. VCH, Weinheim, Germany
    • LaRossa, R. A., VanDyk, T. K., Smulski, D. R. (1990) A Need for Metabolic Insulation: Lessons from Sulfonylurea Genetics, in Biosynthesis of Branched Chain Amino Acids (Barak, Z., Chipman, D. M., and Schloss, J. V., Eds.) pp 109-121, VCH, Weinheim, Germany.
    • (1990) Biosynthesis of Branched Chain Amino Acids , pp. 109-121
    • Larossa, R.A.1    Vandyk, T.K.2    Smulski, D.R.3
  • 15
    • 0005857199 scopus 로고
    • Prevention of Endogenous 2-Ketobutyrate Toxicity in Salmonella Typhimurium
    • Barak, Z., Chipman, D. M., and Schloss, J. V., Eds. VCH, Weinheim, Germany
    • VanDyk, T. K., LaRossa, R. A. (1990) Prevention of Endogenous 2-Ketobutyrate Toxicity in Salmonella Typhimurium, in Biosynthesis of Branched Chain Amino Acids (Barak, Z., Chipman, D. M., and Schloss, J. V., Eds.) pp 123-130, VCH, Weinheim, Germany.
    • (1990) Biosynthesis of Branched Chain Amino Acids , pp. 123-130
    • Vandyk, T.K.1    Larossa, R.A.2
  • 16
    • 0023406320 scopus 로고
    • Metabolic mayhem caused by 2-ketoacid imbalances
    • LaRossa, R. A., and VanDyk, T. K. (1987) Metabolic mayhem caused by 2-ketoacid imbalances. Bioessays 7, 125-130.
    • (1987) Bioessays , vol.7 , pp. 125-130
    • Larossa, R.A.1    Vandyk, T.K.2
  • 17
    • 0023267311 scopus 로고
    • Toxic accumulation of R-ketobutyrate caused by inhibition of the branched-chain amino acid biosynthetic enzyme acetolactate synthase in Salmonella typhimurium
    • LaRossa, R. A., VanDyk, T. K., and Smulski, D. R. (1987) Toxic accumulation of R-ketobutyrate caused by inhibition of the branched-chain amino acid biosynthetic enzyme acetolactate synthase in Salmonella typhimurium. J. Bacteriol. 169, 1372-1378.
    • (1987) J. Bacteriol. , vol.169 , pp. 1372-1378
    • Larossa, R.A.1    Vandyk, T.K.2    Smulski, D.R.3
  • 18
    • 0024539228 scopus 로고
    • Pyruvate decarboxylase is like acetolactate synthase (ILV2) and not like the pyruvate dehydrogenase E1 subunit
    • Green, J. B. (1989) Pyruvate decarboxylase is like acetolactate synthase (ILV2) and not like the pyruvate dehydrogenase E1 subunit. FEBS Lett. 246, 1-5.
    • (1989) FEBS Lett. , vol.246 , pp. 1-5
    • Green, J.B.1
  • 19
    • 0022652882 scopus 로고
    • Role of small subunit (IlvN polypeptide) of acetohydroxyacid synthase I from Escherichia coli K-12 in sensitivity of the enzyme to valine inhibition
    • Eoyang, L., and Silverman, P. M. (1986) Role of small subunit (IlvN polypeptide) of acetohydroxyacid synthase I from Escherichia coli K-12 in sensitivity of the enzyme to valine inhibition. J. Bacteriol. 166, 901-904. (Pubitemid 16098173)
    • (1986) Journal of Bacteriology , vol.166 , Issue.3 , pp. 901-904
    • Eoyang, L.1    Silverman, P.M.2
  • 20
    • 0015523313 scopus 로고
    • Two forms of biosynthetic acetohydroxy acid synthase in Salmonella typhimurium. Biochem
    • O'Neill, J. P., and Freundlich, M. (1972) Two forms of biosynthetic acetohydroxy acid synthase in Salmonella typhimurium. Biochem. Biophys. Res. Commun. 48, 437-443.
    • (1972) Biophys. Res. Commun. , vol.48 , pp. 437-443
    • O'Neill, J.P.1    Freundlich, M.2
  • 21
    • 0015523316 scopus 로고
    • Isoleucine and valine metabolism in Escherichia coli. XX. Multiple forms of acetohydroxy acid synthase
    • Blatt, J. M., Pledger, W. J., and Umbarger, H. E. (1972) Isoleucine and valine metabolism in Escherichia coli. XX. Multiple forms of acetohydroxy acid synthase. Biochem. Biophys. Res. Commun. 48, 444-450.
    • (1972) Biochem. Biophys. Res. Commun. , vol.48 , pp. 444-450
    • Blatt, J.M.1    Pledger, W.J.2    Umbarger, H.E.3
  • 22
    • 0030717640 scopus 로고    scopus 로고
    • Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II and reconstitution of active enzyme from its individual pure subunits
    • Hill, C. M., Pang, S. S., and Duggleby, R. G. (1997) Purification of Escherichia coli acetohydroxyacid synthase isoenzyme II and reconstitution of active enzyme from its individual pure subunits. Biochem. J. 327, 891-898.
    • (1997) Biochem. J. , vol.327 , pp. 891-898
    • Hill, C.M.1    Pang, S.S.2    Duggleby, R.G.3
  • 23
    • 0029798076 scopus 로고    scopus 로고
    • Isolation and characterization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme
    • DOI 10.1021/bi9605604
    • Vyazmensky, M., Sella, C., Barak, Z., and Chipman, D. M. (1996) Isolation and characterization of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme. Biochemistry 35, 10339-10346. (Pubitemid 26277292)
    • (1996) Biochemistry , vol.35 , Issue.32 , pp. 10339-10346
    • Vyazmensky, M.1    Sella, C.2    Barak, Z.3    Chipman, D.M.4
  • 24
    • 33646520567 scopus 로고    scopus 로고
    • Construction of an active acetohydroxyacid synthase I with a flexible linker connecting the catalytic and the regulatory subunits
    • Vyazmensky, M., Engel, S., Kryukov, O., Berkovich-Berger, D., and Kaplun, L. (2006) Construction of an active acetohydroxyacid synthase I with a flexible linker connecting the catalytic and the regulatory subunits. Biochim. Biophys. Acta 1764, 955-960.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 955-960
    • Vyazmensky, M.1    Engel, S.2    Kryukov, O.3    Berkovich-Berger, D.4    Kaplun, L.5
  • 25
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • Aravind, L., and Koonin, E. V. (1999) Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 287, 1023-1040.
    • (1999) J. Mol. Biol. , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 26
    • 0035896041 scopus 로고    scopus 로고
    • Acetohydroxyacid Synthase:A proposed structure for regulatory subunits supported by evidence from mutagenesis
    • Mendel, S., Elkayam, T., Sella, C., Vinogradov, V., Vyazmensky, M., Chipman, D. M., and Barak, Z. (2001) Acetohydroxyacid Synthase:A proposed structure for regulatory subunits supported by evidence from mutagenesis. J. Mol. Biol. 307, 465-477.
    • (2001) J. Mol. Biol. , vol.307 , pp. 465-477
    • Mendel, S.1    Elkayam, T.2    Sella, C.3    Vinogradov, V.4    Vyazmensky, M.5    Chipman, D.M.6    Barak, Z.7
  • 28
    • 0037229214 scopus 로고    scopus 로고
    • The N-terminal domain of the regulatory subunit is sufficient for complete activation of acetohydroxyacid synthase III from Escherichia coli
    • Mendel, S., Vinogradov, M., Vyazmensky, M., Chipman, D. M., and Barak, Z. (2003) The N-terminal domain of the regulatory subunit is sufficient for complete activation of acetohydroxyacid synthase III from Escherichia coli. J. Mol. Biol. 325, 275-284.
    • (2003) J. Mol. Biol. , vol.325 , pp. 275-284
    • Mendel, S.1    Vinogradov, M.2    Vyazmensky, M.3    Chipman, D.M.4    Barak, Z.5
  • 29
    • 0033852212 scopus 로고    scopus 로고
    • Isolation of subunits of acetohydroxy acid synthase isozyme III and reconstitution of holoenzyme
    • Vyazmensky, M., Elkayam, T., Chipman, D. M., and Barak, Z. (2000) Isolation of subunits of acetohydroxy acid synthase isozyme III and reconstitution of the holoenzyme. Methods Enzymol. 324, 95-103. (Pubitemid 30679603)
    • (2000) Methods in Enzymology , vol.324 , pp. 95-103
    • Vyazmensky, M.1    Elkayam, T.2    Chipman, D.M.3    Barak, Z.4
  • 30
    • 2642521392 scopus 로고    scopus 로고
    • Role of a conserved arginine in the mechanism of acetohydroxyacid synthase: Catalysis of condensation with a specific ketoacid substrate
    • Engel, S., Vyazmensky, M., Vinogradov, M., Berkovich, D., Bar-Ilan, A., Qimron, U., Rosiansky, Y., Barak, Z., and Chipman, D. M. (2004) Role of a conserved arginine in the mechanism of acetohydroxyacid synthase: catalysis of condensation with a specific ketoacid substrate. J. Biol. Chem. 279, 24803-24812.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24803-24812
    • Engel, S.1    Vyazmensky, M.2    Vinogradov, M.3    Berkovich, D.4    Bar-Ilan, A.5    Qimron, U.6    Rosiansky, Y.7    Barak, Z.8    Chipman, D.M.9
  • 31
    • 0033082686 scopus 로고    scopus 로고
    • Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors
    • Sheffield, P., Garrard, S., and Derewenda, Z. (1999) Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expression Purif. 15, 34-39.
    • (1999) Protein Expression Purif. , vol.15 , pp. 34-39
    • Sheffield, P.1    Garrard, S.2    Derewenda, Z.3
  • 34
    • 0035797880 scopus 로고    scopus 로고
    • Binding and activation of thiamin diphosphate in acetohydroxyacid synthase
    • DOI 10.1021/bi0104524
    • Bar-Ilan, A., Balan, V., Tittmann, K., Golbik, R., Vyazmensky, M., Hubner, G., Barak, Z., and Chipman, D. M. (2001) Binding and activation of thiamin diphosphate in acetohydroxyacid synthase. Biochemistry 40, 11946-11954. (Pubitemid 32906056)
    • (2001) Biochemistry , vol.40 , Issue.39 , pp. 11946-11954
    • Bar-Ilan, A.1    Balan, V.2    Tittmann, K.3    Golbik, R.4    Vyazmensky, M.5    Hubner, G.6    Barak, Z.7    Chipman, D.M.8
  • 35
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385. (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 36
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201. (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 38
  • 39
    • 0027272523 scopus 로고
    • Subunit association in acetohydroxy acid synthase isozyme III
    • Sella, C., Weinstock, O., Barak, Z., and Chipman, D. M. (1993) Subunit association in acetohydroxy acid synthase isozyme III. J. Bacteriol. 175, 5339-5343. (Pubitemid 23264427)
    • (1993) Journal of Bacteriology , vol.175 , Issue.17 , pp. 5339-5343
    • Sella, C.1    Weinstock, O.2    Barak, Z.3    Chipman, D.M.4
  • 40
    • 0022455986 scopus 로고
    • Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon source
    • Dailey, F. E., and Cronan, J. E. Jr. (1986) Acetohydroxy acid synthase I, a required enzyme for isoleucine and valine biosynthesis in Escherichia coli K-12 during growth on acetate as the sole carbon source. J. Bacteriol. 165, 453-460.
    • (1986) J. Bacteriol. , vol.165 , pp. 453-460
    • Dailey, F.E.1    Cronan Jr., J.E.2
  • 41
    • 0023095528 scopus 로고
    • Acetohydroxy acid synthase I is required for isoleucine and valine biosynthesis by Salmonella typhimurium LT2 during growth on acetate or long-chain fatty acids
    • Dailey, F. E., Cronan, J. E. Jr, and Maloy, S. R. (1987) Acetohydroxy acid synthase I is required for isoleucine and valine biosynthesis by Salmonella typhimurium LT2 during growth on acetate or long-chain fatty acids. J. Bacteriol. 169, 917-919.
    • (1987) J. Bacteriol. , vol.169 , pp. 917-919
    • Dailey, F.E.1    Cronan Jr., J.E.2    Maloy, S.R.3
  • 42
    • 0023626886 scopus 로고
    • Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria
    • Barak, Z., Chipman, D. M., and Gollop, N. (1987) Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. J. Bacteriol. 169, 3750-3756. (Pubitemid 17160323)
    • (1987) Journal of Bacteriology , vol.169 , Issue.8 , pp. 3750-3756
    • Barak, Z.1    Chipman, D.M.2    Gollop, N.3
  • 43
    • 0025346177 scopus 로고
    • Physiological implications of the substrate specificities of acetohydroxy acid synthases from varied organisms
    • Gollop, N., Damri, B., Chipman, D. M., and Barak, Z. (1990) Physiological implications of the substrate specificities of acetohydroxy acid synthases from varied organisms. J. Bacteriol. 172, 3444-3449. (Pubitemid 20179804)
    • (1990) Journal of Bacteriology , vol.172 , Issue.6 , pp. 3444-3449
    • Gollop, N.1    Damri, B.2    Chipman, D.M.3    Barak, Z.4
  • 45
    • 38949122375 scopus 로고    scopus 로고
    • Escherichia coli ilvN interacts with the FAD binding domain of ilvB and activates the AHAS I enzyme
    • DOI 10.1021/bi701893b
    • Mitra, A., and Sarma, S. P. (2008) Escherichia coli ilvN Interacts with the FAD Binding Domain of ilvB and Activates the AHAS I Enzyme. Biochemistry 47, 1518-1531. (Pubitemid 351231203)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1518-1531
    • Mitra, A.1    Sarma, S.P.2
  • 46
    • 0043123208 scopus 로고    scopus 로고
    • ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins
    • DOI 10.1093/nar/gkg556
    • Gouet, P., Robert, X., and Courcelle, E. (2003) ESPript/ENDscript: Extracting and rendering sequence and 3D information from atomic structures of proteins. Nucleic Acids Res. 31, 3320-3323. (Pubitemid 37442149)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3320-3323
    • Gouet, P.1    Robert, X.2    Courcelle, E.3


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