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Volumn 334, Issue 2, 2005, Pages 613-618

Erratum: Crystal structure of NAD-dependent malate dehydrogenase complexed with NADP(H) (Biochemical and Biophysical Research Communications (2005) 334 (613-618) DOI: 10.1016/j.bbrc.2005.06.133);Crystal structure of NAD-dependent malate dehydrogenase complexed with NADP(H)

Author keywords

Coenzyme specificity; Crystal structure; Malate dehydrogenase; Tricarboxylic acid cycle

Indexed keywords

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 22144480963     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.170     Document Type: Erratum
Times cited : (15)

References (25)
  • 1
    • 0001667972 scopus 로고
    • Physicochemical properties of pig and horse heart mitochondrial malate dehydrogenase
    • C.J. Throrne, and N.O. Kaplan Physicochemical properties of pig and horse heart mitochondrial malate dehydrogenase J. Biol. Chem. 238 1963 1861 1868
    • (1963) J. Biol. Chem. , vol.238 , pp. 1861-1868
    • Throrne, C.J.1    Kaplan, N.O.2
  • 2
    • 0016656718 scopus 로고
    • Kinetic studies on pig heart cytoplasmic malate dehydrogenase
    • C. Frieden, and J. Fernandez-Sousa Kinetic studies on pig heart cytoplasmic malate dehydrogenase J. Biol. Chem. 250 1975 2106 2113
    • (1975) J. Biol. Chem. , vol.250 , pp. 2106-2113
    • Frieden, C.1    Fernandez-Sousa, J.2
  • 4
    • 0023664596 scopus 로고
    • Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase
    • L. McAlister-Henn, M. Blaber, and R.A. Bradshaw Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase Nucleic Acids Res. 15 1987 4993
    • (1987) Nucleic Acids Res. , vol.15 , pp. 4993
    • McAlister-Henn, L.1    Blaber, M.2    Bradshaw, R.A.3
  • 5
    • 0023057044 scopus 로고
    • Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity
    • M. Nishiyama, N. Matsubara, K. Yamamoto, S. Iijima, T. Uozumi, and T. Beppu Nucleotide sequence of the malate dehydrogenase gene of Thermus flavus and its mutation directing an increase in enzyme activity J. Biol. Chem. 261 1986 14178 14183
    • (1986) J. Biol. Chem. , vol.261 , pp. 14178-14183
    • Nishiyama, M.1    Matsubara, N.2    Yamamoto, K.3    Iijima, S.4    Uozumi, T.5    Beppu, T.6
  • 6
    • 0018966272 scopus 로고
    • Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile Thermus flavus AT-62
    • S. Iijima, T. Saiki, and T. Beppu Physicochemical and catalytic properties of thermostable malate dehydrogenase from an extreme thermophile Thermus flavus AT-62 Biochim. Biophys. Acta 613 1980 1 9
    • (1980) Biochim. Biophys. Acta , vol.613 , pp. 1-9
    • Iijima, S.1    Saiki, T.2    Beppu, T.3
  • 7
    • 84996270670 scopus 로고
    • Isolation and characterization of extremely thermophilic bacteria from hot springs
    • T. Saiki, R. Kimura, and K. Arima Isolation and characterization of extremely thermophilic bacteria from hot springs Agric. Biol. Chem. 36 1972 2357 2366
    • (1972) Agric. Biol. Chem. , vol.36 , pp. 2357-2366
    • Saiki, T.1    Kimura, R.2    Arima, K.3
  • 8
    • 0027415645 scopus 로고
    • Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis
    • M. Nishiyama, J.J. Birktoft, and T. Beppu Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis J. Biol. Chem. 268 1993 4656 4660
    • (1993) J. Biol. Chem. , vol.268 , pp. 4656-4660
    • Nishiyama, M.1    Birktoft, J.J.2    Beppu, T.3
  • 9
    • 0025778954 scopus 로고
    • Preliminary X-ray diffraction analysis of a crystallizable mutant of malate dehydrogenase from the thermophile Thermus flavus
    • C.A. Kelly, S. Sarfaty, M. Nishiyama, T. Beppu, and J.J. Birktoft Preliminary X-ray diffraction analysis of a crystallizable mutant of malate dehydrogenase from the thermophile Thermus flavus J. Mol. Biol. 221 1991 383 385
    • (1991) J. Mol. Biol. , vol.221 , pp. 383-385
    • Kelly, C.A.1    Sarfaty, S.2    Nishiyama, M.3    Beppu, T.4    Birktoft, J.J.5
  • 10
    • 0027156651 scopus 로고
    • Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus
    • C.A. Kelly, M. Nishiyama, Y. Ohnishi, T. Beppu, and J.J. Birktoft Determinants of protein thermostability observed in the 1.9-Å crystal structure of malate dehydrogenase from the thermophilic bacterium Thermus flavus Biochemistry 32 1993 3913 3922
    • (1993) Biochemistry , vol.32 , pp. 3913-3922
    • Kelly, C.A.1    Nishiyama, M.2    Ohnishi, Y.3    Beppu, T.4    Birktoft, J.J.5
  • 11
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 12
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • A. Vagin, and A. Teplyakov MOLREP: an automated program for molecular replacement J. Appl. Crystallogr. 30 1997 1022 1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • N. Collaborative Computational Project, The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D 50 (1994) 760-763.
    • (1994) Acta Crystallogr. , vol.50 D , pp. 760-763
  • 14
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 16
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1998 505 524
    • (1998) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2
  • 17
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • W.W. Cleland Statistical analysis of enzyme kinetic data Methods Enzymol. 63 1979 103 138
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 18
    • 0027302991 scopus 로고
    • Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 Å resolution
    • M.D. Hall, and L.J. Banaszak Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 Å resolution J. Mol. Biol. 232 1993 213 222
    • (1993) J. Mol. Biol. , vol.232 , pp. 213-222
    • Hall, M.D.1    Banaszak, L.J.2
  • 19
    • 0033561407 scopus 로고    scopus 로고
    • Chloroplast NADP-malate dehydrogenase: Structural basis of light-dependent regulation of activity by thiol oxidation and reduction
    • P.D. Carr, D. Verger, A.R. Ashton, and D.L. Ollis Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction Struct. Fold Des. 7 1999 461 475
    • (1999) Struct. Fold Des. , vol.7 , pp. 461-475
    • Carr, P.D.1    Verger, D.2    Ashton, A.R.3    Ollis, D.L.4
  • 20
    • 0028403259 scopus 로고
    • T and R states in the crystals of bacterial l-lactate dehydrogenase reveal the mechanism for allosteric control
    • S. Iwata, K. Kamata, S. Yoshida, T. Minowa, and T. Ohta T and R states in the crystals of bacterial l-lactate dehydrogenase reveal the mechanism for allosteric control Nat. Struct. Biol. 1 1994 176 185
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 176-185
    • Iwata, S.1    Kamata, K.2    Yoshida, S.3    Minowa, T.4    Ohta, T.5
  • 21
    • 0023644310 scopus 로고
    • Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution
    • T. Skarzynski, P.C. Moody, and A.J. Wonacott Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 Å resolution J. Mol. Biol. 193 1987 171 187
    • (1987) J. Mol. Biol. , vol.193 , pp. 171-187
    • Skarzynski, T.1    Moody, P.C.2    Wonacott, A.J.3
  • 22
    • 0018214851 scopus 로고
    • Substrate inhibition of the mitochondrial and cytoplasmic malate dehydrogenases
    • L.H. Bernstein, M.B. Grisham, K.D. Cole, and J. Everse Substrate inhibition of the mitochondrial and cytoplasmic malate dehydrogenases J. Biol. Chem. 253 1978 8697 8701
    • (1978) J. Biol. Chem. , vol.253 , pp. 8697-8701
    • Bernstein, L.H.1    Grisham, M.B.2    Cole, K.D.3    Everse, J.4
  • 23
    • 0015239163 scopus 로고
    • Pyridine nucleotide metabolism in Escherichia coli I. Exponential growth
    • R. Lundquist, and B.M. Olivera Pyridine nucleotide metabolism in Escherichia coli I. Exponential growth J. Biol. Chem. 246 1971 1107 1116
    • (1971) J. Biol. Chem. , vol.246 , pp. 1107-1116
    • Lundquist, R.1    Olivera, B.M.2
  • 24
    • 0142042960 scopus 로고    scopus 로고
    • Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves
    • A.U. Igamberdiev, and P. Gardestrom Regulation of NAD- and NADP-dependent isocitrate dehydrogenases by reduction levels of pyridine nucleotides in mitochondria and cytosol of pea leaves Biochim. Biophys. Acta 1606 2003 117 125
    • (2003) Biochim. Biophys. Acta , vol.1606 , pp. 117-125
    • Igamberdiev, A.U.1    Gardestrom, P.2
  • 25
    • 0032537722 scopus 로고    scopus 로고
    • Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis
    • E.P. Carpenter, A.R. Hawkins, J.W. Frost, and K.A. Brown Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis Nature 394 1998 299 302
    • (1998) Nature , vol.394 , pp. 299-302
    • Carpenter, E.P.1    Hawkins, A.R.2    Frost, J.W.3    Brown, K.A.4


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