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Volumn 65, Issue 3, 2001, Pages 404-421

Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; BACTERIAL ENZYME; CHORISMATE MUTASE; FUNGAL ENZYME;

EID: 0034821747     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.65.3.404-421.2001     Document Type: Review
Times cited : (60)

References (116)
  • 10
    • 0014248410 scopus 로고
    • Allosteric interactions in aspartate transcarbamylase. 3. Interpretation of experimental data in terms of the model of Monod, Wyman, and Changeux
    • (1968) Biochemistry , vol.7 , pp. 553-561
    • Changeux, J.P.1    Rubin, M.M.2
  • 13
    • 0024593467 scopus 로고
    • Discrimination between nucleotide effector response of aspartate transcarbamoylase due to a single site substitution in the allosteric binding site
    • (1990) J. Biol. Chem. , vol.264 , pp. 7425-7430
    • Corder, T.S.1    Wild, J.R.2
  • 15
    • 0028120126 scopus 로고
    • The use of alanine scanning mutagenesis to determine the role of the N-terminus of the regulatory chain in the heterotropic mechanism of Escherichia coli aspartate transcarbamoylase
    • (1994) Protein Eng. , vol.7 , pp. 673-679
    • Dembowski, N.J.1    Kantrowitz, E.R.2
  • 18
    • 0032537602 scopus 로고    scopus 로고
    • The influence of the regulatory chain amino acids Glu-62 and Ile-12 on the heterotropic properties of Escherichia coli aspartate transcarbamoylase
    • (1998) Biochemistry , vol.37 , pp. 8653-8658
    • Dutta, M.1    Kantrowitz, E.R.2
  • 19
    • 0027422228 scopus 로고
    • Cloning and expression in yeast of a higher plant chorismate mutase. Molecular cloning, sequencing of the cDNA and characterization of the Arabidopsis thaliana enzyme expressed in yeast
    • (1993) FEBS Lett. , vol.334 , pp. 233-236
    • Eberhard, J.1    Raesecke, H.R.2    Schmid, J.3    Amrhein, N.4
  • 20
    • 0001163089 scopus 로고
    • Kinetics of reaction control and information transfer in enzymes and nucleic acids
    • (1967) Nobel Symp. , vol.5 , pp. 333-369
    • Eigen, M.1
  • 38
    • 0023909184 scopus 로고
    • Effectors of Escherichia coli aspartate transcarbamoylase differentially perturb aspartate binding rather than the T-R transition
    • (1988) J. Biol. Chem. , vol.263 , pp. 4172-4181
    • Hsuanyu, Y.C.1    Wedler, F.C.2
  • 40
    • 0032747749 scopus 로고    scopus 로고
    • Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 Å
    • (1999) Proteins , vol.37 , pp. 729-742
    • Jin, L.1    Stec, B.2    Lipscomb, W.N.3    Kantrowitz, E.R.4
  • 52
    • 0003704291 scopus 로고    scopus 로고
    • Reference deleted
  • 54
    • 0024284766 scopus 로고
    • A possible model for the concerted allosteric transition in Escherichia coli aspartate transcarbamylase as deduced from site-directed mutagenesis studies
    • (1988) Biochemistry , vol.27 , pp. 276-283
    • Ladjimi, M.M.1    Kantrowitz, E.R.2
  • 68
    • 0032743418 scopus 로고    scopus 로고
    • Identification, characterization and comparative analysis of a novel chorismate mutase gene in Arabidopsis thaliana
    • (1999) Gene , vol.240 , pp. 115-123
    • Mobley, E.M.1    Kunkel, B.N.2    Keith, B.3
  • 71
    • 0025216234 scopus 로고
    • The regulatory subunit of Escherichia coli aspartate carbamoyltransferase may influence homotropic cooperativity and heterotropic interactions by a direct interaction with the loop containing residues 230-245 of the catalytic chain
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2309-2313
    • Newton, C.J.1    Kantrowitz, E.R.2
  • 72
    • 0003610601 scopus 로고    scopus 로고
    • Reference deleted
  • 77
    • 0032488598 scopus 로고    scopus 로고
    • The N-terminus of the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for both nucleotide binding and heterotropic effects
    • (1998) Biochemistry , vol.37 , pp. 281-288
    • Sakash, J.B.1    Kantrowitz, E.R.2
  • 79
    • 0024289426 scopus 로고
    • Can a simple model account for the allosteric transition of aspartate transcarbamoylase?
    • (1988) J. Biol. Chem. , vol.263 , pp. 18583-18586
    • Schachman, H.K.1
  • 92
    • 0025002987 scopus 로고
    • Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: Crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-Å resolution
    • (1990) Biochemistry , vol.29 , pp. 7691-7701
    • Stevens, R.C.1    Gouaux, J.E.2    Lipscomb, W.N.3
  • 101
    • 0018233269 scopus 로고
    • The stimulation of Escherichia coli aspartate transcarbamylase activity by adenosine triphosphate. Relation with the other regulatory conformational changes; a model
    • (1978) J. Mol. Biol. , vol.125 , pp. 515-534
    • Thiry, L.1    Hervé, G.2
  • 103
    • 0014426681 scopus 로고
    • New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain
    • (1968) Nature , vol.218 , pp. 1116-1119
    • Weber, K.1
  • 109
    • 0028426888 scopus 로고
    • Molecular cloning and characterization of the pyrB1 and pyrB2 genes encoding aspartate transcarbamoylase in pea (Pisum sativum L.)
    • (1994) Plant Physiol. , vol.105 , pp. 377-384
    • Williamson, C.L.1    Slocum, R.D.2
  • 113
    • 0028842603 scopus 로고
    • Location of the active site of allosteric chorismate mutase from Saccharomyces cerevisiae, and comments on the catalytic and regulatory mechanisms
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10595-10598
    • Xue, Y.1    Lipscomb, W.N.2
  • 115
    • 0024962397 scopus 로고
    • Lysine-60 in the regulatory chain of Escherichia coli aspartate transcarbamoylase is important for the discrimination between CTP and ATP
    • (1989) Biochemistry , vol.28 , pp. 7313-7318
    • Zhang, Y.1    Kantrowitz, E.R.2
  • 116
    • 0025837016 scopus 로고
    • The synergistic inhibition of Escherichia coli aspartate carbamoyltransferase by UTP in the presence of CTP is due to the binding of UTP to the low affinity CTP sites
    • (1991) J. Biol. Chem. , vol.266 , pp. 22154-22158
    • Zhang, Y.1    Kantrowitz, E.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.