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Volumn 59, Issue 4, 2011, Pages 445-455

The structure and allosteric regulation of glutamate dehydrogenase

Author keywords

Allostery; Glutamate dehydrogenase; Hyperinsulinism; Insulin

Indexed keywords

3 (3,5 DIBROMO 4 HYDROXYBENZYLIDENE) 1,3 DIHYDRO 5 IODO 2 INDOLONE; AMMONIA; AURINTRICARBOXYLIC ACID; BITHIONOL; EPIGALLOCATECHIN; EPIGALLOCATECHIN 3 MONOGALLATE; EPIGALLOCATECHIN GALLATE; GLUTAMATE DEHYDROGENASE; GUANOSINE TRIPHOSPHATE; HEXACHLOROPHENE; INSULIN; POLYPHENOL DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 80052271742     PISSN: 01970186     EISSN: 18729754     Source Type: Journal    
DOI: 10.1016/j.neuint.2010.10.017     Document Type: Review
Times cited : (53)

References (84)
  • 1
    • 8544270914 scopus 로고    scopus 로고
    • Evolution of glutamate dehydrogenase regulation of insulin homeostasis is an example of molecular exaptation
    • DOI 10.1021/bi048817i
    • A. Allen, J. Kwagh, J. Fang, C.A. Stanley, and T.J. Smith Evolution of glutamate dehydrogenase regulation of insulin homeostasis is an example of molecular exaptation Biochemistry 43 2004 14431 14443 (Pubitemid 39491978)
    • (2004) Biochemistry , vol.43 , Issue.45 , pp. 14431-14443
    • Allen, A.1    Kwagh, J.2    Fang, J.3    Stanley, C.A.4    Smith, T.J.5
  • 4
    • 0020490683 scopus 로고
    • Regulation of bovine glutamate dehydrogenase
    • J.S. Bailey, E.T. Bell, and J.E. Bell Regulation of bovine glutamate dehydrogenase J. Biol. Chem. 257 1982 5579 5583
    • (1982) J. Biol. Chem. , vol.257 , pp. 5579-5583
    • Bailey, J.S.1    Bell, E.T.2    Bell, J.E.3
  • 5
    • 0344837307 scopus 로고    scopus 로고
    • Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation
    • DOI 10.1021/bi0206917
    • S. Banerjee, T. Schmidt, J. Fang, C.A. Stanley, and T.J. Smith Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation Biochemistry 42 2003 3446 3456 (Pubitemid 36368638)
    • (2003) Biochemistry , vol.42 , Issue.12 , pp. 3446-3456
    • Banerjee, S.1    Schmidt, T.2    Fang, J.3    Stanley, C.A.4    Smith, T.J.5
  • 6
    • 0023051825 scopus 로고
    • Isolation and identification of cysteinyl peptide labeled by 6-[(4-bromo-2,3-dioxobutyl)thio]-6-deaminoadenosine 5'-diphosphate in the reduced diphosphopyridine nucleotide inhibitory site of glutamate dehydrogenase
    • S.P. Batra, and R.F. Colman Isolation and identification of cysteinyl peptide labeled by 6-[(4-bromo-2,3-dioxobutyl)thio]-6-deaminoadenosine 5'-diphosphate in the reduced diphosphopyridine nucleotide inhibitory site of glutamate dehydrogenase Biochemistry 25 1986 3508 3515
    • (1986) Biochemistry , vol.25 , pp. 3508-3515
    • Batra, S.P.1    Colman, R.F.2
  • 7
    • 30544433533 scopus 로고    scopus 로고
    • ATP citrate lyase is an important component of cell growth and transformation
    • DOI 10.1038/sj.onc.1208773, PII 1208773
    • D.E. Bauer, G. Hatzivassiliou, F. Zhao, C. Andreadis, and C.B. Thompson ATP citrate lyase is an important component of cell growth and transformation Oncogene 24 2005 6314 6322 (Pubitemid 43080054)
    • (2005) Oncogene , vol.24 , Issue.41 , pp. 6314-6322
    • Bauer, D.E.1    Hatzivassiliou, G.2    Zhao, F.3    Andreadis, C.4    Thompson, C.B.5
  • 8
    • 0021904143 scopus 로고
    • Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in the induction of conformational changes
    • E.T. Bell, C. LiMuti, C.L. Renz, and J.E. Bell Negative co-operativity in glutamate dehydrogenase. Involvement of the 2-position in the induction of conformational changes Biochem. J. 225 1985 209 217
    • (1985) Biochem. J. , vol.225 , pp. 209-217
    • Bell, E.T.1    Limuti, C.2    Renz, C.L.3    Bell, J.E.4
  • 10
    • 0015713701 scopus 로고
    • Localization of some enzymes of ß-oxidation of fatty acids in the peroxisomes of Tetrahymena
    • J.J. Blum Localization of some enzymes of ß-oxidation of fatty acids in the peroxisomes of Tetrahymena J. Protozool. 20 1973 688 692
    • (1973) J. Protozool. , vol.20 , pp. 688-692
    • Blum, J.J.1
  • 11
    • 20544449673 scopus 로고    scopus 로고
    • The glucose dependence of Akt-transformed cells can be reversed by pharmacologic activation of fatty acid β-oxidation
    • DOI 10.1038/sj.onc.1208622
    • M. Buzzai, D.E. Bauer, R.G. Jones, R.J. Deberardinis, G. Hatzivassiliou, R.L. Elstrom, and C.B. Thompson The glucose dependence of Akt-transformed cells can be reversed by pharmacologic activation of fatty acid ß-oxidation Oncogene 24 2005 4165 4173 (Pubitemid 40961771)
    • (2005) Oncogene , vol.24 , Issue.26 , pp. 4165-4173
    • Buzzai, M.1    Bauer, D.E.2    Jones, R.G.3    DeBerardinis, R.J.4    Hatzivassiliou, G.5    Elstrom, R.L.6    Thompson, C.B.7
  • 12
    • 77952562382 scopus 로고    scopus 로고
    • Glucose addiction of TSC null cells Is caused by failed mTORC1-dependent balancing of metabolic demand with supply
    • A.Y. Choo, S.G. Kim, M.G. Vander Heiden, S.J. Mahoney, H. Vu, S.-O. Yoon, L.C. Cantley, and J. Blenis Glucose addiction of TSC null cells Is caused by failed mTORC1-dependent balancing of metabolic demand with supply Mol. Cell 38 2010 487 499
    • (2010) Mol. Cell , vol.38 , pp. 487-499
    • Choo, A.Y.1    Kim, S.G.2    Vander Heiden, M.G.3    Mahoney, S.J.4    Vu, H.5    Yoon, S.-O.6    Cantley, L.C.7    Blenis, J.8
  • 13
    • 0000459625 scopus 로고
    • Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase
    • K. Dalziel, and P.C. Engel Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase FEBS Lett. 1 1968 349 352
    • (1968) FEBS Lett. , vol.1 , pp. 349-352
    • Dalziel, K.1    Engel, P.C.2
  • 15
    • 0019882489 scopus 로고
    • Studies of glutamate dehydrogenase. The interaction of ADP, GTP, and NADPH in complexes with glutamate dehydrogenase
    • H. Dieter, R. Koberstein, and H. Sund Studies of glutamate dehydrogenase. The interaction of ADP, GTP, and NADPH in complexes with glutamate dehydrogenase Eur. J. Biochem. 115 1981 217 226
    • (1981) Eur. J. Biochem. , vol.115 , pp. 217-226
    • Dieter, H.1    Koberstein, R.2    Sund, H.3
  • 16
    • 0016236510 scopus 로고
    • Reaction mechanism of glutamate dehydrogenase. Transient complexes in the oxidative deamination of l-glutamate catalyzed by N∼D(P)-dependent l-glutamate dehydrogenase
    • A. diFranco Reaction mechanism of glutamate dehydrogenase. Transient complexes in the oxidative deamination of l-glutamate catalyzed by N∼D(P)-dependent l-glutamate dehydrogenase Eur. J. Biochem. 45 1974 407 424
    • (1974) Eur. J. Biochem. , vol.45 , pp. 407-424
    • Difranco, A.1
  • 17
    • 0026652145 scopus 로고
    • Identification of amino acids modified by the bifunctional affinity label 5′-(p-fluorosulfonyl)benzoyl-8-azidoadenosine in the reduced coenzyme regulatory site of bovine liver glutamate dehydrogenase
    • K.E. Dombrowski, Y.-C. Huang, and R.F. Colman Identification of amino acids modified by the bifunctional affinity label 5′-(p-fluorosulfonyl) benzoyl-8-azidoadenosine in the reduced coenzyme regulatory site of bovine liver glutamate dehydrogenase Biochemistry 31 1992 3785 3793
    • (1992) Biochemistry , vol.31 , pp. 3785-3793
    • Dombrowski, K.E.1    Huang, Y.-C.2    Colman, R.F.3
  • 19
    • 0014619159 scopus 로고
    • Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates
    • P. Engel, and K. Dalziel Kinetic studies of glutamate dehydrogenase with glutamate and norvaline as substrates Biochem. J. 115 1969 621 631
    • (1969) Biochem. J. , vol.115 , pp. 621-631
    • Engel, P.1    Dalziel, K.2
  • 20
    • 0030870711 scopus 로고    scopus 로고
    • Peroxisomes: Organelles at the crossroads
    • DOI 10.1016/S0962-8924(97)01126-4, PII S0962892497011264
    • R. Erdmann, M. Veenhuis, and W.H. Kunau Peroxisomes: organelles at the crossroads Trends Cell Biol. 7 1997 400 407 (Pubitemid 27417633)
    • (1997) Trends in Cell Biology , vol.7 , Issue.10 , pp. 400-407
    • Erdmann, R.1    Veenhuis, M.2    Kunau, W.-H.3
  • 21
    • 0019809137 scopus 로고
    • Regulation of glutamate dehydrogenase by palmitoyl-coenzyme A
    • L.A. Fahien, and E. Kmiotek Regulation of glutamate dehydrogenase by palmitoyl-coenzyme A Arch. Biochem. Biophys. 212 1981 247 253 (Pubitemid 12221836)
    • (1981) Archives of Biochemistry and Biophysics , vol.212 , Issue.1 , pp. 247-253
    • Fahien, L.A.1    Kmiotek, E.2
  • 22
    • 0023695196 scopus 로고
    • Regulation of insulin release by factors that also modify glutamate dehydrogenase
    • L.A. Fahien, M.J. MacDonald, E.H. Kmiotek, R.J. Mertz, and C.M. Fahien Regulation of insulin release by factors that also modify glutamate dehydrogenase J. Biol. Chem. 263 1988 13610 13614
    • (1988) J. Biol. Chem. , vol.263 , pp. 13610-13614
    • Fahien, L.A.1    MacDonald, M.J.2    Kmiotek, E.H.3    Mertz, R.J.4    Fahien, C.M.5
  • 23
    • 0028153795 scopus 로고
    • Planar stacking interactions of arginine and aromatic side-chains in proteins
    • DOI 10.1006/jmbi.1994.1022
    • M.M. Flocco, and S.L. Mowbray Planar stacking interactions of arginine and aromatic side-chains in proteins J. Mol. Biol. 235 1994 709 717 (Pubitemid 24063588)
    • (1994) Journal of Molecular Biology , vol.235 , Issue.2 , pp. 709-717
    • Flocco, M.M.1    Mowbray, S.L.2
  • 24
    • 0001697553 scopus 로고
    • The dissociation of glutamate dehydrogenase by reduced diphosphopyridine nucleotide (DPNH)
    • C. Frieden The dissociation of glutamate dehydrogenase by reduced diphosphopyridine nucleotide (DPNH) Biochim. Biophys. Acta 27 1958 431 432
    • (1958) Biochim. Biophys. Acta , vol.27 , pp. 431-432
    • Frieden, C.1
  • 25
    • 0000950097 scopus 로고
    • Glutamic dehydrogenase I. The effect of coenzyme on the sedimentation velocity and kinetic mechanism
    • C. Frieden Glutamic dehydrogenase I. The effect of coenzyme on the sedimentation velocity and kinetic mechanism J. Biol. Chem. 234 1959 809 814
    • (1959) J. Biol. Chem. , vol.234 , pp. 809-814
    • Frieden, C.1
  • 26
    • 84965094263 scopus 로고
    • Glutamic dehydrogenase II. The effect of various nucleotides on the association-disassociation and kinetic properties
    • C. Frieden Glutamic dehydrogenase II. The effect of various nucleotides on the association-disassociation and kinetic properties J. Biol. Chem. 234 1959 815 819
    • (1959) J. Biol. Chem. , vol.234 , pp. 815-819
    • Frieden, C.1
  • 27
    • 0001280072 scopus 로고
    • Glutamate dehydrogenase VI. Survey of purine nucleotides and other effects on the enzyme from various sources
    • C. Frieden Glutamate dehydrogenase VI. Survey of purine nucleotides and other effects on the enzyme from various sources J. Biol. Chem. 240 1965 2028 2037
    • (1965) J. Biol. Chem. , vol.240 , pp. 2028-2037
    • Frieden, C.1
  • 29
    • 0026478927 scopus 로고
    • Fatty acid degradation in plants
    • B. Gerhardt Fatty acid degradation in plants Prog. Lipid Res. 31 1992 417 446
    • (1992) Prog. Lipid Res. , vol.31 , pp. 417-446
    • Gerhardt, B.1
  • 30
    • 0015223343 scopus 로고
    • Effect of trinitrophenylation of specific lysyl residues on the catalytic, regulatory, and molecular properties of bovine liver glutamate dehydrogenase
    • B.R. Goldin, and C. Frieden Effect of trinitrophenylation of specific lysyl residues on the catalytic, regulatory, and molecular properties of bovine liver glutamate dehydrogenase Biochemistry 10 1971 3527 3534
    • (1971) Biochemistry , vol.10 , pp. 3527-3534
    • Goldin, B.R.1    Frieden, C.2
  • 32
    • 0032918215 scopus 로고    scopus 로고
    • Peroxisomal beta-oxidation enzymes
    • T. Hashimoto Peroxisomal beta-oxidation enzymes Neurochem. Res. 24 1999 551 563
    • (1999) Neurochem. Res. , vol.24 , pp. 551-563
    • Hashimoto, T.1
  • 33
    • 0023681148 scopus 로고
    • Physiological roles of nicotinamide nucleotide transhydrogenase
    • J.B. Hoek, and J. Rydström Physiological roles of nicotinamide nucleotide transhydrogenase Biochem. J. 254 1988 1 10
    • (1988) Biochem. J. , vol.254 , pp. 1-10
    • Hoek, J.B.1    Rydström, J.2
  • 34
    • 0035091975 scopus 로고    scopus 로고
    • Protein-sensitive and fasting hypoglycemia in children with the hyperinsulinism/hyperammonemia syndrome
    • DOI 10.1067/mpd.2001.111818
    • B.Y. Hsu, A. Kelly, P.S. Thornton, C.R. Greenberg, L.A. Dilling, and C.A. Stanley Protein-sensitive and fasting hypoglycemia in children with the hyperinsulinism/hyperammonemia syndrome J. Pediatr. 138 2001 383 389 (Pubitemid 32207142)
    • (2001) Journal of Pediatrics , vol.138 , Issue.3 , pp. 383-389
    • Hsu, B.Y.L.1    Kelly, A.2    Thornton, P.S.3    Greenberg, C.R.4    Dilling, L.A.5    Stanley, C.A.6
  • 35
    • 0027333040 scopus 로고
    • L-Glutamate dehydrogenases: Distribution, properties and mechanism
    • R.C. Hudson, and R.M. Daniel l-Glutamate dehydrogenases: distribution, properties and mechanism Comp. Biochem. Physiol. 106B 1993 767 792
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 767-792
    • Hudson, R.C.1    Daniel, R.M.2
  • 36
    • 0014210666 scopus 로고
    • Regulation de l' Activite' de la glutamate dehydrogenase par les effecteurs GTP et ADP: ETUDE par "stopped flow"
    • M. Iwatsubo, and D. Pantaloni Regulation De L' Activite' De La glutamate dehydrogenase par les effecteurs GTP et ADP: ETUDE par "stopped flow" Bull. Soc. Chem. Biol. 49 1967 1563 1572
    • (1967) Bull. Soc. Chem. Biol. , vol.49 , pp. 1563-1572
    • Iwatsubo, M.1    Pantaloni, D.2
  • 37
    • 0023432852 scopus 로고
    • Role of glutamate dehydrogenase in ammonia assimilation in nitrogen-fixing Bacillus macerans
    • K. Kanamori, R.L. Weiss, and J.D. Roberts Role of glutamate dehydrogenase in ammonia assimilation in nitrogen-fixing Bacillus macerans J. Bacteriol. 169 1987 4692 4695
    • (1987) J. Bacteriol. , vol.169 , pp. 4692-4695
    • Kanamori, K.1    Weiss, R.L.2    Roberts, J.D.3
  • 38
    • 67650221414 scopus 로고    scopus 로고
    • 3-Hydroxyacyl-coenzyme A dehydrogenase deficiency and hyperinsulinemic hypoglycemia: Characterization of a novel mutation and severe dietary protein sensitivity
    • R.R. Kapoor, C. James, S.E. Flanagan, S. Ellard, S. Eaton, and K. Hussain 3-Hydroxyacyl-coenzyme A dehydrogenase deficiency and hyperinsulinemic hypoglycemia: characterization of a novel mutation and severe dietary protein sensitivity J. Clin. Endocrinol. Metab. 94 2009 2221 2225
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , pp. 2221-2225
    • Kapoor, R.R.1    James, C.2    Flanagan, S.E.3    Ellard, S.4    Eaton, S.5    Hussain, K.6
  • 39
    • 33947592820 scopus 로고    scopus 로고
    • Mitochondrial GTP Regulates Glucose-Stimulated Insulin Secretion
    • DOI 10.1016/j.cmet.2007.02.008, PII S155041310700040X
    • R.G. Kibbey, R.L. Pongratz, A.J. Romanelli, C.B. Wollheim, G.W. Cline, and G.I. Shulman Mitochondrial GTP regulates glucose-stimulated insulin secretion Cell Metab. 5 2007 253 264 (Pubitemid 46477853)
    • (2007) Cell Metabolism , vol.5 , Issue.4 , pp. 253-264
    • Kibbey, R.G.1    Pongratz, R.L.2    Romanelli, A.J.3    Wollheim, C.B.4    Cline, G.W.5    Shulman, G.I.6
  • 40
    • 33749478922 scopus 로고    scopus 로고
    • Cancer's molecular sweet tooth and the warburg effect
    • DOI 10.1158/0008-5472.CAN-06-1501
    • J.W. Kim, and C.V. Dang Cancer's molecular sweet tooth and the Warburg effect Cancer Res. 66 2006 8927 8930 (Pubitemid 44521105)
    • (2006) Cancer Research , vol.66 , Issue.18 , pp. 8927-8930
    • Kim, J.-W.1    Dang, C.V.2
  • 41
    • 0015782265 scopus 로고
    • The influence of ADP, GTP and l-glutamate on the binding of the reduced coenzyme to beef-liver glutamate dehydrogenase
    • R. Koberstein, and H. Sund The influence of ADP, GTP and l-glutamate on the binding of the reduced coenzyme to beef-liver glutamate dehydrogenase Eur. J. Biochem. 36 1973 545 552
    • (1973) Eur. J. Biochem. , vol.36 , pp. 545-552
    • Koberstein, R.1    Sund, H.2
  • 42
    • 0011434964 scopus 로고
    • On the effect of green tea for diabettes mellitus
    • Kyoto University
    • S. Konayagi, and M. Minowada On the effect of green tea for diabettes mellitus Study of Physiology vol. 10 1933 Kyoto University pp. 449-454
    • (1933) Study of Physiology , vol.10 , pp. 449-454
    • Konayagi, S.1    Minowada, M.2
  • 43
    • 0030444789 scopus 로고    scopus 로고
    • The structural basis of negative cooperativity: Receptors and enzymes
    • D.E.J. Koshland The structural basis of negative cooperativity: receptors and enzymes Cur. Opin. Struc. Biol. 6 1996 757 761
    • (1996) Cur. Opin. Struc. Biol. , vol.6 , pp. 757-761
    • Koshland, D.E.J.1
  • 44
    • 0025608884 scopus 로고
    • A complex effet of arsenite on the formation of a-ketoglutarate in rate liver mitochondria
    • E. Lenartowicz A complex effet of arsenite on the formation of a-ketoglutarate in rate liver mitochondria Arch. Biochem. Biophys. 283 1990 388 396
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 388-396
    • Lenartowicz, E.1
  • 49
    • 37349039359 scopus 로고    scopus 로고
    • High throughput screening reveals several new classes of glutamate dehydrogenase inhibitors
    • DOI 10.1021/bi7018783
    • M. Li, A. Allen, and T.J. Smith High throughput screening reveals several new classes of glutamate dehydrogenase inhibitors Biochemistry 46 2007 15089 15102 (Pubitemid 350308900)
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 15089-15102
    • Li, M.1    Allen, A.2    Smith, T.J.3
  • 50
    • 69249158109 scopus 로고    scopus 로고
    • Novel inhibitors complexed with glutamate dehydrogenase: Allosteric regulation by control of protein dynamics
    • M. Li, C.J. Smith, M.T. Walker, and T.J. Smith Novel inhibitors complexed with glutamate dehydrogenase: allosteric regulation by control of protein dynamics J. Biol. Chem. 284 2009 22988 23000
    • (2009) J. Biol. Chem. , vol.284 , pp. 22988-23000
    • Li, M.1    Smith, C.J.2    Walker, M.T.3    Smith, T.J.4
  • 53
    • 0015509464 scopus 로고
    • Kinetic studies on the mechanism of the action of ADP on the glutamate dehydrogenase reaction
    • K. Markau, J. Schneider, and H. Sund Kinetic studies on the mechanism of the action of ADP on the glutamate dehydrogenase reaction FEBS Lett. 24 1972 32 36
    • (1972) FEBS Lett. , vol.24 , pp. 32-36
    • Markau, K.1    Schneider, J.2    Sund, H.3
  • 54
    • 0015429145 scopus 로고
    • Negative cooperativity in glutamate dehydrogenase. Coenzyme binding studies
    • G. Melzi-D'eril, and K. Dalziel Negative cooperativity in glutamate dehydrogenase. Coenzyme binding studies Biochem. J. 130 1973 3P
    • (1973) Biochem. J. , vol.130
    • Melzi-D'Eril, G.1    Dalziel, K.2
  • 55
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • DOI 10.1091/mbc.E05-01-0033
    • E. Michishita, J.Y. Park, J.M. Burneskis, J.C. Barrett, and I. Horikawa Evolutionarily conserved an nonconserved cellular localizaitons and functions of human SIRT proteins Mol. Biol. Cell 16 2005 4623 4635 (Pubitemid 41416446)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 56
    • 0014430073 scopus 로고
    • Distribution of tricarboxylic acid cycle enzymes and glyoxylate cycle enzymes between mitochondria and peroxisomes in Tetrahymena pyriformis
    • M. Muller, J.F. Hogg, and C. De Duve Distribution of tricarboxylic acid cycle enzymes and glyoxylate cycle enzymes between mitochondria and peroxisomes in Tetrahymena pyriformis J. Biol. Chem. 243 1968 5385 5395
    • (1968) J. Biol. Chem. , vol.243 , pp. 5385-5395
    • Muller, M.1    Hogg, J.F.2    De Duve, C.3
  • 57
    • 0016608730 scopus 로고
    • Affinity labeling of a regulatory site of bovine liver glutamate dehydrogenase
    • P.K. Pal, W.J. Wechter, and R.F. Colman Affinity labeling of a regulatory site of bovine liver glutamate dehydrogenase Biochemistry 14 1975 707 715
    • (1975) Biochemistry , vol.14 , pp. 707-715
    • Pal, P.K.1    Wechter, W.J.2    Colman, R.F.3
  • 58
    • 0033565447 scopus 로고    scopus 로고
    • The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery
    • DOI 10.1016/S0969-2126(99)80101-4
    • P.E. Peterson, and T.J. Smith The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery Struct. Fold Des. 7 1999 769 782 (Pubitemid 29329848)
    • (1999) Structure , vol.7 , Issue.7 , pp. 769-782
    • Peterson, P.E.1    Smith, T.J.2
  • 59
    • 0015237763 scopus 로고
    • Bovine liver glutamate dehydrogenase. Equilibria and kinetics of inactivation by pyridoxal
    • D. Piszkiewicz, and E.L. Smith Bovine liver glutamate dehydrogenase. Equilibria and kinetics of inactivation by pyridoxal Biochemistry 10 1971 4538 4544
    • (1971) Biochemistry , vol.10 , pp. 4538-4544
    • Piszkiewicz, D.1    Smith, E.L.2
  • 60
    • 0015721891 scopus 로고
    • The mechanism of activation of glutamate dehydrogenase-catalyzed reactions by two different, cooperatively bound activators
    • R.A. Prough, J.M. Culver, and H.F. Fisher The mechanism of activation of glutamate dehydrogenase-catalyzed reactions by two different, cooperatively bound activators J. Biol. Chem. 248 1973 8528 8533
    • (1973) J. Biol. Chem. , vol.248 , pp. 8528-8533
    • Prough, R.A.1    Culver, J.M.2    Fisher, H.F.3
  • 61
    • 0017187697 scopus 로고
    • The asymmetric distribution of enzymic activity between the six subunits of bovine liver glutamate dehydrogenase. Use of d- and l-glutamyl alpha-chloromethyl ketones 4-amino-6-chloro-5-oxohexanoic acid
    • C.G. Rasool, S. Nicolaidis, and M. Akhtar The asymmetric distribution of enzymic activity between the six subunits of bovine liver glutamate dehydrogenase. Use of d- and l-glutamyl alpha-chloromethyl ketones 4-amino-6-chloro-5-oxohexanoic acid Biochem. J. 157 1976 675 686
    • (1976) Biochem. J. , vol.157 , pp. 675-686
    • Rasool, C.G.1    Nicolaidis, S.2    Akhtar, M.3
  • 63
    • 0014874160 scopus 로고
    • Factors governing the kinetics and steady state of the mitochondrial nicotinamide nucleotide transhydrogenase system
    • J. Rydström, A. Teixeira da Cruz, and L. Ernster Factors governing the kinetics and steady state of the mitochondrial nicotinamide nucleotide transhydrogenase system Eur. J. Biochem. 17 1970 56 62
    • (1970) Eur. J. Biochem. , vol.17 , pp. 56-62
    • Rydström, J.1    Teixeira Da Cruz, A.2    Ernster, L.3
  • 64
    • 0021679087 scopus 로고
    • Identification of the lysine and tyrosine peptides labeled by 5'-p-fluorosulfonylbenzoyladenosine in the NADH inhibitory site of glutamate dehydrogenase
    • J.A. Schmidt, and R.F. Colman Identification of the lysine and tyrosine peptides labeled by 5'-p-fluorosulfonylbenzoyladenosine in the NADH inhibitory site of glutamate dehydrogenase J. Biol. Chem. 259 1984 14515 14519 (Pubitemid 15222273)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.23 , pp. 14515-14519
    • Schmidt, J.A.1    Colman, R.F.2
  • 65
    • 0019133275 scopus 로고
    • L-Leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase
    • DOI 10.1038/288187a0
    • A. Sener, and W.J. Malaisse l-leucine and a nonmetabolized analogue activate pancreatic islet glutamate dehydrogenase Nature 288 1980 187 189 (Pubitemid 11212612)
    • (1980) Nature , vol.288 , Issue.5787 , pp. 187-189
    • Sener, A.1    Malaisse, W.J.2
  • 68
    • 33750619348 scopus 로고    scopus 로고
    • Glucose metabolism and cancer
    • DOI 10.1016/j.ceb.2006.10.005, PII S095506740600158X
    • R.J. Shaw Glucose metabolism and cancer Curr. Opin. Cell Biol. 18 2006 598 608 (Pubitemid 44692479)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.6 , pp. 598-608
    • Shaw, R.J.1
  • 69
    • 77956904836 scopus 로고
    • Glutamate dehydrogenases
    • P.D. Boyer, Academic Press New York
    • E.L. Smith, B.M. Austen, K.M. Blumenthal, and J.F. Nyc Glutamate dehydrogenases P.D. Boyer, The Enzymes Vol. 11 1975 Academic Press New York 293 367
    • (1975) The Enzymes , vol.11 , pp. 293-367
    • Smith, E.L.1    Austen, B.M.2    Blumenthal, K.M.3    Nyc, J.F.4
  • 70
    • 0035937256 scopus 로고    scopus 로고
    • Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation
    • DOI 10.1006/jmbi.2001.4499
    • T.J. Smith, P.E. Peterson, T. Schmidt, J. Fang, and C. Stanley Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation J. Mol. Biol. 307 2001 707 720 (Pubitemid 33027686)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.2 , pp. 707-720
    • Smith, T.J.1    Peterson, P.E.2    Schmidt, T.3    Fang, J.4    Stanley, C.A.5
  • 71
    • 0036304611 scopus 로고    scopus 로고
    • The structure of apo human glutamate dehydrogenase details subunit communication and allostery
    • DOI 10.1016/S0022-2836(02)00161-4
    • T.J. Smith, T. Schmidt, J. Fang, J. Wu, G. Siuzdak, and C.A. Stanley The structure of apo human glutamate dehydrogenase details subunit communication and allostery J. Mol. Biol. 318 2002 765 777 (Pubitemid 34729367)
    • (2002) Journal of Molecular Biology , vol.318 , Issue.3 , pp. 765-777
    • Smith, T.J.1    Schmidt, T.2    Fang, J.3    Wu, J.4    Siuzdak, G.5    Stanley, C.A.6
  • 72
    • 54249092318 scopus 로고    scopus 로고
    • Untangling the glutamate dehydrogenase allosteric nightmare
    • T.J. Smith, and C.A. Stanley Untangling the glutamate dehydrogenase allosteric nightmare Trends Biol. Chem. 33 2008 557 564
    • (2008) Trends Biol. Chem. , vol.33 , pp. 557-564
    • Smith, T.J.1    Stanley, C.A.2
  • 73
    • 84895303529 scopus 로고    scopus 로고
    • Disorders of mitochondrial fatty acid oxidation and related metabolic pathways
    • J. Fernandes, J.-M. Saudubray, G. van den Berg, J.H. Walter, fourth ed. Springer Heidelberg
    • C. Stanley, M.J. Bennett, and E. Mayatepek Disorders of mitochondrial fatty acid oxidation and related metabolic pathways J. Fernandes, J.-M. Saudubray, G. van den Berg, J.H. Walter, Inborn Metabolic Diseases fourth ed. 2006 Springer Heidelberg 177 188
    • (2006) Inborn Metabolic Diseases , pp. 177-188
    • Stanley, C.1    Bennett, M.J.2    Mayatepek, E.3
  • 74
    • 1642481536 scopus 로고    scopus 로고
    • The hyperinsulinism-hyperammonemia syndrome: Gain-of-function mutations of glutamate dehydrogenase
    • S. O'Rahilly, D.B. Dunger, BioScientifica, Ltd. Bristol
    • C.A. Stanley The hyperinsulinism-hyperammonemia syndrome: gain-of-function mutations of glutamate dehydrogenase S. O'Rahilly, D.B. Dunger, Genetic Insights in Paediatric Endocrinology and Metabolism 2000 BioScientifica, Ltd. Bristol 23 30
    • (2000) Genetic Insights in Paediatric Endocrinology and Metabolism , pp. 23-30
    • Stanley, C.A.1
  • 75
    • 0034029974 scopus 로고    scopus 로고
    • Molecular basis and characterization of the hyperinsulinism/ hyperammonemia syndrome: Predominance of mutations in exons 11 and 12 of the glutamate dehydrogenase gene
    • C.A. Stanley, J. Fang, K. Kutyna, B.Y.L. Hsu, J.E. Ming, B. Glaser, and M. Poncz Molecular basis and characterization of the hyperinsulinism/ hyperammonemia syndrome of the glutamate dehydrogenase gene Diabetes 49 2000 667 673 (Pubitemid 30183758)
    • (2000) Diabetes , vol.49 , Issue.4 , pp. 667-673
    • Stanley, C.A.1    Fang, J.2    Kutyna, K.3    Hsu, B.Y.L.4    Ming, J.E.5    Glaser, B.6    Poncz, M.7
  • 77
    • 0021764142 scopus 로고
    • Ox liver glutamate dehydrogenase. The use of chemical modification to study the rlationship between catalytic sites for differeent amino acid substrates andthe question of kinetic non-equivalence of the subunits
    • S.-E.-H. Syed, and P.C. Engel Ox liver glutamate dehydrogenase. The use of chemical modification to study the rlationship between catalytic sites for differeent amino acid substrates andthe question of kinetic non-equivalence of the subunits Biochem. J. 222 1984 621 626
    • (1984) Biochem. J. , vol.222 , pp. 621-626
    • Syed, S.-E.-H.1    Engel, P.C.2
  • 78
    • 8544260615 scopus 로고
    • The influence of diethylstilbestrol and adenosine diphosphate on pyridine nucleotide coenzyme binding by glutamic dehydrogenase
    • G.M. Tomkins, K.L. Yielding, and J.F. Curran The influence of diethylstilbestrol and adenosine diphosphate on pyridine nucleotide coenzyme binding by glutamic dehydrogenase J. Biol. Chem. 237 1962 1704 1708
    • (1962) J. Biol. Chem. , vol.237 , pp. 1704-1708
    • Tomkins, G.M.1    Yielding, K.L.2    Curran, J.F.3
  • 80
    • 0028007435 scopus 로고
    • Activation of bovine liver glutamate dehydrogenase by covalent reaction of adenosine 5'-O-[S-(4-bromo-2,3-dioxobutyl)thiophosphate] with arginine-459 at an ADP regulatory site
    • DOI 10.1021/bi00204a017
    • K.O. Wrzeszczynski, and R.F. Colman Activation of bovine liver glutamate dehydrogenase by covalent reaction of adenosine 5′-O-[S-(4-bromo-2,3- dioxobutyl)thiophosphate] with arginine-459 at an ADP regulatory site Biochemistry 33 1994 11544 11553 (Pubitemid 24330088)
    • (1994) Biochemistry , vol.33 , Issue.38 , pp. 11544-11553
    • Wrzeszczynski, K.O.1    Colman, R.F.2
  • 81
    • 70350217425 scopus 로고    scopus 로고
    • Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling
    • C. Yang, J. Sudderth, T. Dang, R.G. Bachoo, J.G. McDonald, and R.J. DeBerardinis Glioblastoma cells require glutamate dehydrogenase to survive impairments of glucose metabolism or Akt signaling Cancer Res. 69 2009 7986 7993
    • (2009) Cancer Res. , vol.69 , pp. 7986-7993
    • Yang, C.1    Sudderth, J.2    Dang, T.3    Bachoo, R.G.4    McDonald, J.G.5    Deberardinis, R.J.6
  • 83
    • 0000941835 scopus 로고
    • An effect of l-leucine and other essential amino acids on the structure and activity of glutamate dehydrogenase
    • K.L. Yielding, and G.M. Tomkins An effect of l-leucine and other essential amino acids on the structure and activity of glutamate dehydrogenase Proc. Natl. Acad. Sci. 47 1961 983
    • (1961) Proc. Natl. Acad. Sci. , vol.47 , pp. 983
    • Yielding, K.L.1    Tomkins, G.M.2


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