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Volumn 5, Issue 8, 1996, Pages 1648-1654

Role of the divalent metal ion in the NAD:malic enzyme reaction: An ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex

Author keywords

decarboxylation; EPR spectroscopy; malic enzyme; substrate conformation

Indexed keywords

MALATE DEHYDROGENASE (DECARBOXYLATING); NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 0030037042     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050818     Document Type: Article
Times cited : (7)

References (44)
  • 1
    • 0019556812 scopus 로고
    • Purification of malic enzyme from Ascaris suum using NAD+-agarose
    • Allen BL, Harris BG. 1981. Purification of malic enzyme from Ascaris suum using NAD+-agarose. Mol Biochem Parisitol 2:367-372.
    • (1981) Mol Biochem Parisitol , vol.2 , pp. 367-372
    • Allen, B.L.1    Harris, B.G.2
  • 2
    • 0019157471 scopus 로고
    • Use of isotope effects to deduce the chemical mechanism of fumarase
    • Blanchard JS, Cleland WW. 1980. Use of isotope effects to deduce the chemical mechanism of fumarase. Biochemistry 19:4506-4513.
    • (1980) Biochemistry , vol.19 , pp. 4506-4513
    • Blanchard, J.S.1    Cleland, W.W.2
  • 3
    • 0024284768 scopus 로고
    • Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism
    • Chen CY, Harris BG, Cook PF. 1988. Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism. Biochemistry 27:212-219.
    • (1988) Biochemistry , vol.27 , pp. 212-219
    • Chen, C.Y.1    Harris, B.G.2    Cook, P.F.3
  • 4
    • 0000915570 scopus 로고
    • Nuclear modulation effects in high spin electron systems with small zero-field splittings
    • Coffino AR, Peisach J. 1992. Nuclear modulation effects in high spin electron systems with small zero-field splittings. J Chem Phys 97:3072-3091.
    • (1992) J Chem Phys , vol.97 , pp. 3072-3091
    • Coffino, A.R.1    Peisach, J.2
  • 5
    • 0001423719 scopus 로고
    • A study of manganous complexes by paramagnetic resonance absorption
    • Cohn M, Townsend J. 1954. A study of manganous complexes by paramagnetic resonance absorption. Nature 173:1090-1091.
    • (1954) Nature , vol.173 , pp. 1090-1091
    • Cohn, M.1    Townsend, J.2
  • 6
    • 0022423889 scopus 로고
    • Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme
    • Grissom CB, Cleland WW. 1985. Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme. Biochemistry 24:944-948.
    • (1985) Biochemistry , vol.24 , pp. 944-948
    • Grissom, C.B.1    Cleland, W.W.2
  • 7
    • 0001626995 scopus 로고
    • Carbon isotope effects on the metal ion catalyzed decarboxylation of oxalacetate
    • Grissom CB, Cleland WW. 1986. Carbon isotope effects on the metal ion catalyzed decarboxylation of oxalacetate. J Am Chem Soc 108:5582-5583.
    • (1986) J Am Chem Soc , vol.108 , pp. 5582-5583
    • Grissom, C.B.1    Cleland, W.W.2
  • 8
    • 0024291649 scopus 로고
    • Isotope effect studies of chicken liver NADP malic enzyme: Role of the metal ion and viscosity dependence
    • Grissom CB, Cleland WW. 1988. Isotope effect studies of chicken liver NADP malic enzyme: Role of the metal ion and viscosity dependence. Biochemisiry 27:2921-2934.
    • (1988) Biochemisiry , vol.27 , pp. 2921-2934
    • Grissom, C.B.1    Cleland, W.W.2
  • 9
    • 0020492976 scopus 로고
    • Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-ohosphate dehydrogenase
    • Hermes JD, Roeske CA, O'Leary MH, Cleland WW. 1982. Use of multiple isotope effects to determine enzyme mechanisms and intrinsic isotope effects. Malic enzyme and glucose-6-ohosphate dehydrogenase. Biochemistry 27:5106-5114.
    • (1982) Biochemistry , vol.27 , pp. 5106-5114
    • Hermes, J.D.1    Roeske, C.A.2    O'Leary, M.H.3    Cleland, W.W.4
  • 10
    • 0014963061 scopus 로고
    • Mechanism of pigeon liver malic enzyme
    • Hsu RY. 1970. Mechanism of pigeon liver malic enzyme. J Biol Chem 245:6675-6682.
    • (1970) J Biol Chem , vol.245 , pp. 6675-6682
    • Hsu, R.Y.1
  • 13
    • 0028230767 scopus 로고
    • Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: A reinvestigation
    • Karsten WE, Cook PF. 1994. Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: A reinvestigation. Biochemistry 33: 2096-2103.
    • (1994) Biochemistry , vol.33 , pp. 2096-2103
    • Karsten, W.E.1    Cook, P.F.2
  • 14
    • 0028916268 scopus 로고
    • Metal ion activator effects on intrinsic isotope effects for hydride transfer and decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum
    • Karsten WE, Gavva SR, Park SH, Cook PF. 1995. Metal ion activator effects on intrinsic isotope effects for hydride transfer and decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum. Biochemistry 54:3253-3260.
    • (1995) Biochemistry , vol.54 , pp. 3253-3260
    • Karsten, W.E.1    Gavva, S.R.2    Park, S.H.3    Cook, P.F.4
  • 15
    • 0023048290 scopus 로고
    • Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinudeotide-malic enzyme reaction from isotope effect and pH studies
    • Kiick DM, Harris BG, Cook PF. 1986. Protonation mechanism and location of rate-determining steps for the Ascaris suum nicotinamide adenine dinudeotide-malic enzyme reaction from isotope effect and pH studies. Biochemistry 25:227-236.
    • (1986) Biochemistry , vol.25 , pp. 227-236
    • Kiick, D.M.1    Harris, B.G.2    Cook, P.F.3
  • 18
    • 33845281044 scopus 로고
    • Cu(H) coordination chemistry of amine oxidases: Pulsed EPR studies of histidine imidazole, water, and exogenous ligand coordination
    • McCracken J, Peisach J, Dooley DM. 1987. Cu(H) coordination chemistry of amine oxidases: Pulsed EPR studies of histidine imidazole, water, and exogenous ligand coordination. J Am Chem Soc 109:4064-4072.
    • (1987) J Am Chem Soc , vol.109 , pp. 4064-4072
    • McCracken, J.1    Peisach, J.2    Dooley, D.M.3
  • 19
    • 9344233297 scopus 로고
    • 1H ENDOR investigations in tris-sarcosine-calcium chloride doped with manganese
    • Metz H, Kùchler J, Böttcher R, Windsch W. 1982. 1H ENDOR investigations in tris-sarcosine-calcium chloride doped with manganese. Chem Phys Lett 89:351-355.
    • (1982) Chem Phys Lett , vol.89 , pp. 351-355
    • Metz, H.1    Kùchler, J.2    Böttcher, R.3    Windsch, W.4
  • 20
    • 0016312321 scopus 로고
    • Measurement of the linear electric field effect in EPR using the spin echo method
    • Mims WB. 1974. Measurement of the linear electric field effect in EPR using the spin echo method. Rev Sci Instrum 45:1583-1591.
    • (1974) Rev Sci Instrum , vol.45 , pp. 1583-1591
    • Mims, W.B.1
  • 21
    • 0000352268 scopus 로고
    • Elimination of the dead-time artifact in electron spin-echo envelope spectra
    • Mims WB. 1984. Elimination of the dead-time artifact in electron spin-echo envelope spectra. J Magn Reson 59:291-306.
    • (1984) J Magn Reson , vol.59 , pp. 291-306
    • Mims, W.B.1
  • 22
    • 0021413732 scopus 로고
    • The accessibility of type I Cu(II) centers in laccase, azurin, and stellacyanin to exchangeable hydrogen and ambient water
    • Mims WB, Davis JL, Peisach J. 1984. The accessibility of type I Cu(II) centers in laccase, azurin, and stellacyanin to exchangeable hydrogen and ambient water. Biophys J 45:755-766.
    • (1984) Biophys J , vol.45 , pp. 755-766
    • Mims, W.B.1    Davis, J.L.2    Peisach, J.3
  • 23
    • 0000567659 scopus 로고
    • The exchange of hydrogen ions and of water molecules near the active site of cytochrome c
    • Mims WB, Davis J, Peisach J. 1990. The exchange of hydrogen ions and of water molecules near the active site of cytochrome c. J Magn Res 86: 273-292.
    • (1990) J Magn Res , vol.86 , pp. 273-292
    • Mims, W.B.1    Davis, J.2    Peisach, J.3
  • 24
    • 0000537404 scopus 로고
    • Electron spin echo spectroscopy and the study of metalloproteins
    • Berliner LJ, Reuben J, eds. New York: Plenum Press
    • Mims WB, Peisach J. 1981. Electron spin echo spectroscopy and the study of metalloproteins. In: Berliner LJ, Reuben J, eds. Biological magnetic resonance, vol 3. New York: Plenum Press. pp. 213-263.
    • (1981) Biological Magnetic Resonance , vol.3 , pp. 213-263
    • Mims, W.B.1    Peisach, J.2
  • 25
    • 22944440943 scopus 로고
    • Nuclear modulation of the electron spin echo envelope in glassy materials
    • Mims WB, Peisach J, Davis JL. 1977. Nuclear modulation of the electron spin echo envelope in glassy materials. J Chem Phys 66:5536-5550.
    • (1977) J Chem Phys , vol.66 , pp. 5536-5550
    • Mims, W.B.1    Peisach, J.2    Davis, J.L.3
  • 26
    • 0022742485 scopus 로고
    • pH Dependence of kinetic parameters for oxalacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme
    • Park SH, Harris BG, Cook PF. 1986. pH Dependence of kinetic parameters for oxalacetate decarboxylation and pyruvate reduction reactions catalyzed by malic enzyme. Biochemistry 25:3752-3759.
    • (1986) Biochemistry , vol.25 , pp. 3752-3759
    • Park, S.H.1    Harris, B.G.2    Cook, P.F.3
  • 27
    • 0021756507 scopus 로고
    • Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum
    • Park SH, Kiick, DM, Harris BG, Cook PF. 1984. Kinetic mechanism in the direction of oxidative decarboxylation for NAD-malic enzyme from Ascaris suum. Biochemistry 23:5446-5453.
    • (1984) Biochemistry , vol.23 , pp. 5446-5453
    • Park, S.H.1    Kiick, D.M.2    Harris, B.G.3    Cook, P.F.4
  • 28
    • 0018801615 scopus 로고
    • 14N in cytochrome P-450 and in a series of low spin heme compounds
    • 14N in cytochrome P-450 and in a series of low spin heme compounds. J Biol Chem 254:12379-12389.
    • (1979) J Biol Chem , vol.254 , pp. 12379-12389
    • Peisach, J.1    Mims, W.B.2    Davis, J.3
  • 29
    • 0021357243 scopus 로고
    • Water coordination by heme iron in metmyoglobin
    • Peisach J, Mims WB, Davis J. 1984. Water coordination by heme iron in metmyoglobin. J Biol Chem 259:2704-2706.
    • (1984) J Biol Chem , vol.259 , pp. 2704-2706
    • Peisach, J.1    Mims, W.B.2    Davis, J.3
  • 30
    • 0004076812 scopus 로고
    • Decarboxyladons of β-keto acids and related compounds
    • Candour RD, Schowen RL, eds. New York: Plenum Press
    • Pollack RM, 1978. Decarboxyladons of β-keto acids and related compounds. In: Candour RD, Schowen RL, eds. Transition states of biochemical processes. New York: Plenum Press. pp 467-492.
    • (1978) Transition States of Biochemical Processes , pp. 467-492
    • Pollack, R.M.1
  • 31
    • 0024835968 scopus 로고
    • Ligand conformations and ligand-enzyme interactions as studied by the nuclear Overhauser effect
    • Rosevear PR, Mildvan AS. 1989. Ligand conformations and ligand-enzyme interactions as studied by the nuclear Overhauser effect. Methods Enzymol 177:333-358.
    • (1989) Methods Enzymol , vol.177 , pp. 333-358
    • Rosevear, P.R.1    Mildvan, A.S.2
  • 32
    • 0017580411 scopus 로고
    • Determination of the rate-limiting steps for malic enzyme by the use of isotope effects and other kinetic studies
    • Schimerlik MI, Grimshaw CE, Cleland WW. 1977. Determination of the rate-limiting steps for malic enzyme by the use of isotope effects and other kinetic studies. Biochemistry 16:571-576.
    • (1977) Biochemistry , vol.16 , pp. 571-576
    • Schimerlik, M.I.1    Grimshaw, C.E.2    Cleland, W.W.3
  • 33
    • 0024291330 scopus 로고
    • Electron spin echo modulation and nuclear relaxation studies of staphylococcal nuclease and its metal-coordinating mutants
    • Serpersu EH, McCracken J, Peisach J, Mildvan AS. 1988. Electron spin echo modulation and nuclear relaxation studies of staphylococcal nuclease and its metal-coordinating mutants. Biochemistry 27:8034-8044.
    • (1988) Biochemistry , vol.27 , pp. 8034-8044
    • Serpersu, E.H.1    McCracken, J.2    Peisach, J.3    Mildvan, A.S.4
  • 34
    • 0007753531 scopus 로고
    • Electron spin echo envelope modulation studies of natural abundance carbon-13 and alummum-27 in two disordered systems
    • Snetsinger PA, Cornelius JB, Clarkson RB, Bowman MK, Belford RL. 1988. Electron spin echo envelope modulation studies of natural abundance carbon-13 and alummum-27 in two disordered systems. J Phys Chem 92:3696-3698.
    • (1988) J Phys Chem , vol.92 , pp. 3696-3698
    • Snetsinger, P.A.1    Cornelius, J.B.2    Clarkson, R.B.3    Bowman, M.K.4    Belford, R.L.5
  • 35
    • 0000996934 scopus 로고
    • Metal ion-catalyzed decarboxylation: A model for an enzyme system
    • Steinberger R, Westheimer FH. 1951. Metal ion-catalyzed decarboxylation: A model for an enzyme system. J Am Chem Soc 73:429-435.
    • (1951) J Am Chem Soc , vol.73 , pp. 429-435
    • Steinberger, R.1    Westheimer, F.H.2
  • 36
    • 84988073214 scopus 로고
    • Optimization of parameters for semiempirical methods II. Applications
    • Stewart JJP. 1989. Optimization of parameters for semiempirical methods II. Applications. J Comput Chem 10:221-264.
    • (1989) J Comput Chem , vol.10 , pp. 221-264
    • Stewart, J.J.P.1
  • 37
    • 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. 1993. Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, 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.2    Koshland, D.E.3
  • 38
    • 0015896972 scopus 로고
    • Reduction of α-oxo carboxylic acids by pigeon liver "malic$ enzyme
    • Tang CL, Hsu RY. 1973. Reduction of α-oxo carboxylic acids by pigeon liver "malic$ enzyme. Biochem J:287-291.
    • (1973) Biochem J , pp. 287-291
    • Tang, C.L.1    Hsu, R.Y.2
  • 39
    • 0039681277 scopus 로고
    • Scope and limitations of the concept of the transition state
    • Gandour RD, Schowen RL, eds. New York: Plenum Press
    • Thornton EK, Thornton ER. 1978. Scope and limitations of the concept of the transition state. In: Gandour RD, Schowen RL, eds. Transition states of biochemical processes. New York: Plenum Press. pp 1-76.
    • (1978) Transition States of Biochemical Processes , pp. 1-76
    • Thornton, E.K.1    Thornton, E.R.2
  • 40
    • 0027517031 scopus 로고
    • Intermediate partitioning in the tartrate dehydrogenase-catalyzed oxidative decarboxylation of D-malate
    • Tipton PA. 1993. Intermediate partitioning in the tartrate dehydrogenase-catalyzed oxidative decarboxylation of D-malate. Biochemistry 32:2822-2827.
    • (1993) Biochemistry , vol.32 , pp. 2822-2827
    • Tipton, P.A.1
  • 41
    • 0004696495 scopus 로고
    • Structure of manganese(II) trihydrate and comparison with other malates
    • Van Havere W, Lenstra ATH, Geise HJ. 1980. Structure of manganese(II) trihydrate and comparison with other malates. Acta Crystallogr B 36: 3117-3120.
    • (1980) Acta Crystallogr B , vol.36 , pp. 3117-3120
    • Van Havere, W.1    Lenstra, A.T.H.2    Geise, H.J.3
  • 42
    • 76549255287 scopus 로고
    • Biosynthesis of dicarboxylic acids by carbon dioxide fixation
    • Viega Salles JB, Ochoa S. 1950. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. J Biol Chem 187:849-861.
    • (1950) J Biol Chem , vol.187 , pp. 849-861
    • Viega Salles, J.B.1    Ochoa, S.2
  • 43
    • 0025837657 scopus 로고
    • Multiple isotope effects with alternative dinucleotide substrate as a probe of the malic enzyme reaction
    • Weiss PM, Gavva SR, Harris BG, Urbauer JC, Cleland WW, Cook PF. 1991. Multiple isotope effects with alternative dinucleotide substrate as a probe of the malic enzyme reaction. Biochemistry 30:5755-5763.
    • (1991) Biochemistry , vol.30 , pp. 5755-5763
    • Weiss, P.M.1    Gavva, S.R.2    Harris, B.G.3    Urbauer, J.C.4    Cleland, W.W.5    Cook, P.F.6
  • 44
    • 0028901535 scopus 로고
    • Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase
    • Zhang T, Koshland DE. 1995. Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase. Protein Sci 4:84-92.
    • (1995) Protein Sci , vol.4 , pp. 84-92
    • Zhang, T.1    Koshland, D.E.2


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