메뉴 건너뛰기




Volumn 70, Issue 1, 2008, Pages 63-71

Structure and quantum chemical analysis of NAD+-dependent isocitrate dehydrogenase: Hydride transfer and co-factor specificity

Author keywords

Chemolithotrophic bacterium; Crystal structure; Decarboxylating dehydrogenase; Hydride migration; Semi empirical molecular orbital calculation

Indexed keywords

ADENOSINE; ADENOSINE RIBOSE; AMIDE; ASPARTIC ACID; BACTERIAL ENZYME; CARBON; CITRIC ACID; HYDRIDE; HYDROGEN; HYDROXYL GROUP; ISOCITRATE DEHYDROGENASE; ISOPROPYLMALATE DEHYDROGENASE; MALATE DEHYDROGENASE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; RIBOSE; UNCLASSIFIED DRUG;

EID: 37349078630     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21486     Document Type: Article
Times cited : (22)

References (38)
  • 1
    • 0027494760 scopus 로고
    • Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5 Å-resolution: A pseudo-Michaelis ternary complex
    • Stoddard BL, Dean A, Koshland DE, Jr. Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5 Å-resolution: a pseudo-Michaelis ternary complex. Biochemistry 1993;32:9310-9316.
    • (1993) Biochemistry , vol.32 , pp. 9310-9316
    • Stoddard, B.L.1    Dean, A.2    Koshland Jr., D.E.3
  • 4
    • 0035941275 scopus 로고    scopus 로고
    • Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation
    • Steen IH, Madern D, Karlstrom M, Lien T, Ladenstein R, Birkeland NK. Comparison of isocitrate dehydrogenase from three hyperthermophiles reveals differences in thermostability, cofactor specificity, oligomeric state, and phylogenetic affiliation. J Biol Chem 2001;276:43924-43931.
    • (2001) J Biol Chem , vol.276 , pp. 43924-43931
    • Steen, I.H.1    Madern, D.2    Karlstrom, M.3    Lien, T.4    Ladenstein, R.5    Birkeland, N.K.6
  • 6
    • 0026334204 scopus 로고
    • Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus
    • Imada K, Sato M, Tanaka N, Katsube Y, Matsuura Y, Oshima T. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus. J Mol Biol 1991;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
  • 7
    • 0016345760 scopus 로고
    • Chemical and biological evolution of a nucleotide-binding protein
    • Rossmann MG, Moras D, Olsen KW. Chemical and biological evolution of a nucleotide-binding protein. Nature 1974;250:194-199.
    • (1974) Nature , vol.250 , pp. 194-199
    • Rossmann, M.G.1    Moras, D.2    Olsen, K.W.3
  • 8
    • 0029886080 scopus 로고    scopus 로고
    • Determinants of cofactor specificity in isocitrate dehydrogenase: Structure of an engineered NADP(+)->NAD(+) specificity-reversal mutant
    • Hurley JH, Chen R, Dean AM. Determinants of cofactor specificity in isocitrate dehydrogenase: structure of an engineered NADP(+)->NAD(+) specificity-reversal mutant. Biochemistry 1996;35:5670-5678.
    • (1996) Biochemistry , vol.35 , pp. 5670-5678
    • Hurley, J.H.1    Chen, R.2    Dean, A.M.3
  • 10
    • 0014134954 scopus 로고
    • Biochemical basis of obligate autotrophy in blue-green algae and thiobacilli
    • Smith AJ, London J, Stanier RY. Biochemical basis of obligate autotrophy in blue-green algae and thiobacilli. J Bacteriol 1967;94:972-983.
    • (1967) J Bacteriol , vol.94 , pp. 972-983
    • Smith, A.J.1    London, J.2    Stanier, R.Y.3
  • 11
    • 0014688630 scopus 로고
    • Regulation of isocitrate dehydrogenase from Thiobacullus thiooxidans and Pseudomonas fluorescens
    • Hampton ML, Hanson RS. Regulation of isocitrate dehydrogenase from Thiobacullus thiooxidans and Pseudomonas fluorescens. Biochem Biophys Res Commun 1969;36:296-305.
    • (1969) Biochem Biophys Res Commun , vol.36 , pp. 296-305
    • Hampton, M.L.1    Hanson, R.S.2
  • 12
    • 0021950232 scopus 로고
    • 2 assimilation via the reductive tricarboxylic-acid cycle in an obligately autotrophic, aerobic hydrogen-oxyidaizing bacterium, hydrogenobacter- thermophilus
    • 2 assimilation via the reductive tricarboxylic-acid cycle in an obligately autotrophic, aerobic hydrogen-oxyidaizing bacterium, hydrogenobacter- thermophilus. Arch Microbiol 1985;141:198-203.
    • (1985) Arch Microbiol , vol.141 , pp. 198-203
    • Shiba, H.1    Kawasumi, T.2    Igarashi, Y.3    Kodama, T.4    Minoda, Y.5
  • 13
    • 0027383273 scopus 로고
    • Kinetic mechanism of Escherichia coli isocitrate dehydrogenase
    • Dean AM, Koshland DE, Jr. Kinetic mechanism of Escherichia coli isocitrate dehydrogenase. Biochemistry 1993;32:9302-9309.
    • (1993) Biochemistry , vol.32 , pp. 9302-9309
    • Dean, A.M.1    Koshland Jr., D.E.2
  • 14
    • 0028774536 scopus 로고
    • +: Ligand-induced loop closing and mechanism for cofactor specificity
    • +: ligand-induced loop closing and mechanism for cofactor specificity. Structure 1994;2:1007-1016.
    • (1994) Structure , vol.2 , pp. 1007-1016
    • Hurley, J.H.1    Dean, A.M.2
  • 15
    • 0032528935 scopus 로고    scopus 로고
    • Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 Å resolution: The role of Glu88 in the unique substrate-recognition mechanism
    • Imada K, Inagaki K, Matsunami H, Kawaguchi H, Tanaka H, Tanaka N, Namba K. Structure of 3-isopropylmalate dehydrogenase in complex with 3-isopropylmalate at 2.0 Å resolution: the role of Glu88 in the unique substrate-recognition mechanism. Structure 1998;6:971-982.
    • (1998) Structure , vol.6 , pp. 971-982
    • Imada, K.1    Inagaki, K.2    Matsunami, H.3    Kawaguchi, H.4    Tanaka, H.5    Tanaka, N.6    Namba, K.7
  • 16
    • 0028853604 scopus 로고
    • Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophils
    • Kadono S, Sakurai M, Moriyama H, Sato M, Hayashi Y, Oshima T, Tanaka N. Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophils. J Biochem 1995;118:745-752.
    • (1995) J Biochem , vol.118 , pp. 745-752
    • Kadono, S.1    Sakurai, M.2    Moriyama, H.3    Sato, M.4    Hayashi, Y.5    Oshima, T.6    Tanaka, N.7
  • 18
    • 4043105583 scopus 로고    scopus 로고
    • Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity
    • Xu X, Zhao J, Xu Z, Peng B, Huang Q, Arnold E, Ding J. Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. J Biol Chem 2004;279:33946-33957.
    • (2004) J Biol Chem , vol.279 , pp. 33946-33957
    • Xu, X.1    Zhao, J.2    Xu, Z.3    Peng, B.4    Huang, Q.5    Arnold, E.6    Ding, J.7
  • 20
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW. Solvent content of protein crystals. J Mol Biol 1968;33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 21
    • 0003076963 scopus 로고
    • Recent changes to the MOSFLM package for processing film and image plate data. CCP4+ESF-EACMB Newslett
    • Leslie AGW. Recent changes to the MOSFLM package for processing film and image plate data. CCP4+ESF-EACMB Newslett Protein Crystallogr 1992;26:27-33.
    • (1992) Protein Crystallogr , vol.26 , pp. 27-33
    • Leslie, A.G.W.1
  • 22
    • 0028103275 scopus 로고
    • Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 1994;50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 24
    • 0032872798 scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan KD, Zhang KY. Density modification for macromolecular phase improvement. Prog Biophys Mol Biol 1994;72:245-270.
    • (1994) Prog Biophys Mol Biol , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zhou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 1997;53:240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 28
    • 24444468650 scopus 로고
    • Ground-states of molecules, 38. MNDO method - approximations and parameters
    • Dewar MJS, Thiel W. Ground-states of molecules, 38. MNDO method - approximations and parameters. J Am Chem Soc 1977;99:4899-4907.
    • (1977) J Am Chem Soc , vol.99 , pp. 4899-4907
    • Dewar, M.J.S.1    Thiel, W.2
  • 29
    • 0842341771 scopus 로고
    • The development and use of quantum-mechanical molecular-models, 76. AM1 - a new general-purpose quantum-mechanical molecular-model
    • Dewar MJS, Zoebisch EG, Healy EF, Stewart JJP. The development and use of quantum-mechanical molecular-models, 76. AM1 - a new general-purpose quantum-mechanical molecular-model. J Am Chem Soc 1985;107:3902-3909.
    • (1985) J Am Chem Soc , vol.107 , pp. 3902-3909
    • Dewar, M.J.S.1    Zoebisch, E.G.2    Healy, E.F.3    Stewart, J.J.P.4
  • 30
    • 84988129057 scopus 로고    scopus 로고
    • Stewart JJP. Optimization of parameters for semiempirical methods. I. Method. J Comput Chem 1989;10:209-220.
    • Stewart JJP. Optimization of parameters for semiempirical methods. I. Method. J Comput Chem 1989;10:209-220.
  • 31
    • 84961980743 scopus 로고
    • COSMO - a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient
    • Klamt A, Schuemann G. COSMO - a new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient. J Chem Soc Perkin Trans 1993;2:799-805.
    • (1993) J Chem Soc Perkin Trans , vol.2 , pp. 799-805
    • Klamt, A.1    Schuemann, G.2
  • 32
    • 0035854744 scopus 로고    scopus 로고
    • Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 Å. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase
    • Singh SK, Matsuno K, LaPorte DC, Banaszak J. Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 Å. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase. J Biol Chem 2001;276:26154-26163.
    • (2001) J Biol Chem , vol.276 , pp. 26154-26163
    • Singh, S.K.1    Matsuno, K.2    LaPorte, D.C.3    Banaszak, J.4
  • 33
    • 0030879888 scopus 로고    scopus 로고
    • Orbital steering in the catalytic power of enzymes: Small structural changes with large catalytic consequences
    • Mesecar AD, Stoddard B, Koshland DE, Jr. Orbital steering in the catalytic power of enzymes: small structural changes with large catalytic consequences. Science 1997;277:202-206.
    • (1997) Science , vol.277 , pp. 202-206
    • Mesecar, A.D.1    Stoddard, B.2    Koshland Jr., D.E.3
  • 34
    • 0034641677 scopus 로고    scopus 로고
    • Crystal structures of adrenodoxin reductase in complex with NADP(+) and NADPH suggesting a mechanism for the electron transfer of an enzyme family
    • Ziegler GA, Schulz GE. Crystal structures of adrenodoxin reductase in complex with NADP(+) and NADPH suggesting a mechanism for the electron transfer of an enzyme family. Biochemistry 2000;39:10986-10995.
    • (2000) Biochemistry , vol.39 , pp. 10986-10995
    • Ziegler, G.A.1    Schulz, G.E.2
  • 35
    • 0034644773 scopus 로고    scopus 로고
    • Probing the catalytic mechanism of GDP-4-keto-6-deoxy-d-mannose epimerase/reductase by kinetic and crystallographic characterization of site-specific mutants
    • Rosano C, Bisso A, Izzo G, Tonetti M, Sturla L, Flora AD, Bolognesi M. Probing the catalytic mechanism of GDP-4-keto-6-deoxy-d-mannose epimerase/reductase by kinetic and crystallographic characterization of site-specific mutants. J Mol Biol 2000;303:77-91.
    • (2000) J Mol Biol , vol.303 , pp. 77-91
    • Rosano, C.1    Bisso, A.2    Izzo, G.3    Tonetti, M.4    Sturla, L.5    Flora, A.D.6    Bolognesi, M.7
  • 36
    • 10944270383 scopus 로고    scopus 로고
    • Theoretical study of the electron density distributions of glycyl-L-threonine dihydrate
    • Yu N, Merz KM. Theoretical study of the electron density distributions of glycyl-L-threonine dihydrate. Mol Phys 2004;102:2545-2557.
    • (2004) Mol Phys , vol.102 , pp. 2545-2557
    • Yu, N.1    Merz, K.M.2
  • 37
    • 5244245983 scopus 로고
    • A correlation of reaction rates
    • Hammond GS. A correlation of reaction rates. J Am Chem Soc 1955;77:334-338.
    • (1955) J Am Chem Soc , vol.77 , pp. 334-338
    • Hammond, G.S.1
  • 38
    • 0000500410 scopus 로고
    • Evaluation of the factors influencing reactivity and stereospecificity in NAD(P)H dependent dehydrogenase enzymes
    • Almarsson O, Bruice TC. Evaluation of the factors influencing reactivity and stereospecificity in NAD(P)H dependent dehydrogenase enzymes. J Am Chem Soc 1993;115:2125-2138.
    • (1993) J Am Chem Soc , vol.115 , pp. 2125-2138
    • Almarsson, O.1    Bruice, T.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.