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Volumn 250, Issue 2, 1997, Pages 578-582

Structural constraints in protein engineering. The coenzyme specificity of Escherichia Coli isocitrate dehydrogenase

Author keywords

Coenzyme specificity; Isocitrate dehydrogenase; Isopropylmalate dehydrogenase; Molecular recognition; Protein engineering

Indexed keywords

ISOCITRATE DEHYDROGENASE;

EID: 0031436547     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.0578a.x     Document Type: Article
Times cited : (19)

References (25)
  • 1
    • 0027383273 scopus 로고
    • The kinetic mechanism of Escherichia coli isocitrate dehydrogenase
    • Dean, A. M. & Koshland D. E. Jr (1993) The kinetic mechanism of Escherichia coli isocitrate dehydrogenase, Biochemistry 32, 9302-9308.
    • (1993) Biochemistry , vol.32 , pp. 9302-9308
    • Dean, A.M.1    Koshland Jr., D.E.2
  • 2
    • 0030063709 scopus 로고    scopus 로고
    • The determinants of performance in the isocitrate dehydrogenase of Escherichia coli
    • Dean, A. M., Shiau, A. K. & Koshland, D. E. Jr (1996) The determinants of performance in the isocitrate dehydrogenase of Escherichia coli, Protein Science 5, 341-347.
    • (1996) Protein Science , vol.5 , pp. 341-347
    • Dean, A.M.1    Shiau, A.K.2    Koshland Jr., D.E.3
  • 3
    • 0000996934 scopus 로고
    • β-Decarboxylation of α-keto acids as calalyzed by divalent metal cations
    • Steinberger, R. & Westheimer, F. H. (1951) β-Decarboxylation of α-keto acids as calalyzed by divalent metal cations, J. Am. Chem. Soc. 73, 429-435.
    • (1951) J. Am. Chem. Soc. , vol.73 , pp. 429-435
    • Steinberger, R.1    Westheimer, F.H.2
  • 4
    • 0008010106 scopus 로고
    • The enzymatic properties of isocitric dehydrogenase
    • Siebert, G., Carsiotis, M. & Plaut, G. W. E. (1957) The enzymatic properties of isocitric dehydrogenase, J. Biol. Chem. 226, 977-991.
    • (1957) J. Biol. Chem. , vol.226 , pp. 977-991
    • Siebert, G.1    Carsiotis, M.2    Plaut, G.W.E.3
  • 5
    • 0001414364 scopus 로고
    • The stereospecific protonation of the enolate form of α-ketoglutarate hound to isocitrate dehydrogenase
    • Lienhard, G. E. & Rose, I. A. (1964) The stereospecific protonation of the enolate form of α-ketoglutarate hound to isocitrate dehydrogenase, Biochemistry 3, 185-190.
    • (1964) Biochemistry , vol.3 , pp. 185-190
    • Lienhard, G.E.1    Rose, I.A.2
  • 6
    • 0014353609 scopus 로고
    • The mechanisms of reductive carboxylation reactions
    • Londesborough, J. C. & Dalziel, K. (1968) The mechanisms of reductive carboxylation reactions, Biochem. J. 110, 223-230.
    • (1968) Biochem. J. , vol.110 , pp. 223-230
    • Londesborough, J.C.1    Dalziel, K.2
  • 8
    • 0024291638 scopus 로고
    • Isotope effect studies of the chemical mechanism of pig heart NADP isocitrate dehydrogenase
    • Grissom, C. B. & Cleland, W. W. (1988) Isotope effect studies of the chemical mechanism of pig heart NADP isocitrate dehydrogenase. Biochemistry 27, 2934-2943.
    • (1988) Biochemistry , vol.27 , pp. 2934-2943
    • Grissom, C.B.1    Cleland, W.W.2
  • 10
  • 12
    • 0027494760 scopus 로고
    • The 2.5 Å structure of isocitrate dehydrogenase with isocitrate, NADP and calcium at 2.5 Å resolution: A pseudo-Michaelis ternary complex
    • Stoddard, B. L., Dean, A. M. & Koshland, D. H. Jr (1993) The 2.5 Å structure of isocitrate dehydrogenase with isocitrate, NADP and calcium at 2.5 Å resolution: a pseudo-Michaelis ternary complex, Biochemistry 32, 9310-9316.
    • (1993) Biochemistry , vol.32 , pp. 9310-9316
    • Stoddard, B.L.1    Dean, A.M.2    Koshland Jr., D.H.3
  • 14
    • 0029940466 scopus 로고    scopus 로고
    • Combining Laue diffraction and molecular dynamics to study enzyme intermediates: Formation of a Michaelis complex
    • Stoddard, B. L., Dean, A. M. & Bash, P. A. (1996) Combining Laue diffraction and molecular dynamics to study enzyme intermediates: formation of a Michaelis complex, Nat. Struct. Biol. 3, 590-595.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 590-595
    • Stoddard, B.L.1    Dean, A.M.2    Bash, P.A.3
  • 15
    • 0026334204 scopus 로고
    • Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution
    • Imada, K., Sato, M., Tanaka, N., Katsube, Y., Matsuura, Y. & Oshima, T. (1991) Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution, J. Mol. Biol. 222, 725-738.
    • (1991) J. Mol. Biol. , vol.222 , pp. 725-738
    • Imada, K.1    Sato, M.2    Tanaka, N.3    Katsube, Y.4    Matsuura, Y.5    Oshima, T.6
  • 16
    • 0028774536 scopus 로고
    • +: Ligand-induced loop closing and mechanism for cofactor specificity
    • +: ligand-induced loop closing and mechanism for cofactor specificity, Structure 2, 1007-1016.
    • (1994) Structure , vol.2 , pp. 1007-1016
    • Hurley, J.H.1    Dean, A.M.2
  • 17
    • 0029557251 scopus 로고
    • A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity
    • Chen, R., Greer, A. & Dean, A. M. (1995) A highly active decarboxylating dehydrogenase with rationally inverted coenzyme specificity, Proc. Natl Acad. Sci. USA 92, 11666-11670.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11666-11670
    • Chen, R.1    Greer, A.2    Dean, A.M.3
  • 19
    • 0023645302 scopus 로고
    • Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate
    • Thorsness, P. H. & Koshland, D. K. Jr (1987) Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate, J. Biol. Chem. 262, 10422-10425.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10422-10425
    • Thorsness, P.H.1    Koshland Jr., D.K.2
  • 20
    • 0025002460 scopus 로고
    • Electrostatic and steric contributions Io regulation at the active site of isocitrate dehydrogenase
    • Dean, A. M. & Koshland D. K. Jr (1990) Electrostatic and steric contributions Io regulation at the active site of isocitrate dehydrogenase, Science 249, 1044-1046.
    • (1990) Science , vol.249 , pp. 1044-1046
    • Dean, A.M.1    Koshland Jr., D.K.2
  • 21
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection, Proc. Natl Acad. Sci. USA 82, 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 23
    • 0028047371 scopus 로고
    • Co-enzyme specificity of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8
    • Miyazaki, K. & Oshima, T. (1994) Co-enzyme specificity of 3-isopropylmalate dehydrogenase from Thermus thermophilus HB8, Protein Eng. 7, 401-403.
    • (1994) Protein Eng. , vol.7 , pp. 401-403
    • Miyazaki, K.1    Oshima, T.2
  • 24
    • 0015221183 scopus 로고
    • Yeast diphosphopyridine nucleotide specific isocitrate dehydrogenase. Purification and some properties
    • Barnes, L. D., Kuehn, G. D. & Atkinson, D. E. (1971) Yeast diphosphopyridine nucleotide specific isocitrate dehydrogenase. Purification and some properties, Biochemistry 10, 3939-3945.
    • (1971) Biochemistry , vol.10 , pp. 3939-3945
    • Barnes, L.D.1    Kuehn, G.D.2    Atkinson, D.E.3
  • 25
    • 0027432796 scopus 로고
    • Kinetic analysis of NAD(+)-isocitrate dehydrogenase with altered isocitrate binding sites: Contribution of IDH1 and IDH2 subunits to regulation and catalysis
    • Cupp, J. R. & McAlister-Henn, L. (1993) Kinetic analysis of NAD(+)-isocitrate dehydrogenase with altered isocitrate binding sites: contribution of IDH1 and IDH2 subunits to regulation and catalysis. Biochemistry 32, 9323-9328.
    • (1993) Biochemistry , vol.32 , pp. 9323-9328
    • Cupp, J.R.1    McAlister-Henn, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.