메뉴 건너뛰기




Volumn 275, Issue 21, 2008, Pages 5383-5392

Influential factor contributing to the isoform-specific inhibition by ATP of human mitochondrial NAD(P)+-dependent malic enzyme: Functional roles of the nucleotide binding site Lys346

Author keywords

Allosteric regulation; ATP inhibition; Cofactor specificity; Cooperativity; Mutagenesis

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; ARGININE; FUMARIC ACID; LYSINE; MALATE DEHYDROGENASE (DECARBOXYLATING); MALIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SERINE;

EID: 53849147880     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06668.x     Document Type: Article
Times cited : (12)

References (45)
  • 1
    • 0019316309 scopus 로고
    • Kinetic studies of the malic enzyme of pigeon liver. 'Half-of-the-sites' behavior of the enzyme tetramer in catalysis and substrate inhibition
    • Hsu RY Pry RA (1980) Kinetic studies of the malic enzyme of pigeon liver. 'Half-of-the-sites' behavior of the enzyme tetramer in catalysis and substrate inhibition. Biochemistry 19, 962 968.
    • (1980) Biochemistry , vol.19 , pp. 962-968
    • Hsu, R.Y.1    Pry, R.A.2
  • 2
    • 0018823014 scopus 로고
    • Mitochondrial malic enzymes. Mitochondrial NAD(P)+-dependent malic enzyme activity and malate-dependent pyruvate formation are progression-linked in Morris hepatomas
    • Sauer LA, Dauchy RT, Nagel WO Morris HP (1980) Mitochondrial malic enzymes. Mitochondrial NAD(P)+-dependent malic enzyme activity and malate-dependent pyruvate formation are progression-linked in Morris hepatomas. J Biol Chem 255, 3844 3848.
    • (1980) J Biol Chem , vol.255 , pp. 3844-3848
    • Sauer, L.A.1    Dauchy, R.T.2    Nagel, W.O.3    Morris, H.P.4
  • 3
    • 0020475291 scopus 로고
    • Pigeon liver malic enzyme
    • Hsu RY (1982) Pigeon liver malic enzyme. Mol Cell Biochem 43, 3 26.
    • (1982) Mol Cell Biochem , vol.43 , pp. 3-26
    • Hsu, R.Y.1
  • 4
    • 0025286085 scopus 로고
    • Regulation of coenzyme utilization by mitochondrial NAD(P)-dependent malic enzyme
    • Skorkowski EF Storey KB (1990) Regulation of coenzyme utilization by mitochondrial NAD(P)-dependent malic enzyme. Int J Biochem 22, 471 475.
    • (1990) Int J Biochem , vol.22 , pp. 471-475
    • Skorkowski, E.F.1    Storey, K.B.2
  • 5
    • 0025757237 scopus 로고
    • Kinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation
    • Mallick S, Harris BG Cook PF (1991) Kinetic mechanism of NAD:malic enzyme from Ascaris suum in the direction of reductive carboxylation. J Biol Chem 266, 2732 2738.
    • (1991) J Biol Chem , vol.266 , pp. 2732-2738
    • Mallick, S.1    Harris, B.G.2    Cook, P.F.3
  • 6
    • 0025753268 scopus 로고
    • Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli
    • Loeber G, Infante AA, Maurer-Fogy I, Krystek E Dworkin MB (1991) Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning, primary structure, and expression in Escherichia coli. J Biol Chem 266, 3016 3021.
    • (1991) J Biol Chem , vol.266 , pp. 3016-3021
    • Loeber, G.1    Infante, A.A.2    Maurer-Fogy, I.3    Krystek, E.4    Dworkin, M.B.5
  • 7
    • 0037044306 scopus 로고    scopus 로고
    • Alternative substrates for malic enzyme: Oxidative decarboxylation of l-aspartate
    • Liu D, Hwang CC Cook PF (2002) Alternative substrates for malic enzyme: oxidative decarboxylation of l-aspartate. Biochemistry 41, 12200 12203.
    • (2002) Biochemistry , vol.41 , pp. 12200-12203
    • Liu, D.1    Hwang, C.C.2    Cook, P.F.3
  • 8
    • 0030037042 scopus 로고    scopus 로고
    • 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
    • Tipton PA, Quinn TP, Peisach J Cook PF (1996) 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. Protein Sci 5, 1648 1654.
    • (1996) Protein Sci , vol.5 , pp. 1648-1654
    • Tipton, P.A.1    Quinn, T.P.2    Peisach, J.3    Cook, P.F.4
  • 9
    • 0034700281 scopus 로고    scopus 로고
    • Slow binding of metal ions to pigeon liver malic enzyme: A general case
    • Hung HC, Chang GG, Yang Z Tong L (2000) Slow binding of metal ions to pigeon liver malic enzyme: a general case. Biochemistry 39, 14095 14102.
    • (2000) Biochemistry , vol.39 , pp. 14095-14102
    • Hung, H.C.1    Chang, G.G.2    Yang, Z.3    Tong, L.4
  • 10
    • 0037085299 scopus 로고    scopus 로고
    • Effect of metal binding on the structural stability of pigeon liver malic enzyme
    • Chang HC, Chou WY Chang GG (2002) Effect of metal binding on the structural stability of pigeon liver malic enzyme. J Biol Chem 277, 4663 4671.
    • (2002) J Biol Chem , vol.277 , pp. 4663-4671
    • Chang, H.C.1    Chou, W.Y.2    Chang, G.G.3
  • 11
    • 0037018948 scopus 로고    scopus 로고
    • Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 Å resolution
    • Coleman DE, Rao GS, Goldsmith EJ, Cook PF Harris BG (2002) Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 Å resolution. Biochemistry 41, 6928 6938.
    • (2002) Biochemistry , vol.41 , pp. 6928-6938
    • Coleman, D.E.1    Rao, G.S.2    Goldsmith, E.J.3    Cook, P.F.4    Harris, B.G.5
  • 13
    • 0042835774 scopus 로고    scopus 로고
    • Crystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanism
    • Tao X, Yang Z Tong L (2003) Crystal structures of substrate complexes of malic enzyme and insights into the catalytic mechanism. Structure 11, 1141 1150.
    • (2003) Structure , vol.11 , pp. 1141-1150
    • Tao, X.1    Yang, Z.2    Tong, L.3
  • 14
    • 0033566912 scopus 로고    scopus 로고
    • Crystal structure of human mitochondrial NAD(P)+dependent malic enzyme: A new class of oxidative decarboxylases
    • Xu Y, Bhargava G, Wu H, Loeber G Tong L (1999) Crystal structure of human mitochondrial NAD(P)+dependent malic enzyme: a new class of oxidative decarboxylases. Structure 7, R877 R889.
    • (1999) Structure , vol.7
    • Xu, Y.1    Bhargava, G.2    Wu, H.3    Loeber, G.4    Tong, L.5
  • 15
    • 0034049525 scopus 로고    scopus 로고
    • Structure of a closed form of human malic enzyme and implications for catalytic mechanism
    • Yang Z, Floyd DL, Loeber G Tong L (2000) Structure of a closed form of human malic enzyme and implications for catalytic mechanism. Nat Struct Biol 7, 251 257.
    • (2000) Nat Struct Biol , vol.7 , pp. 251-257
    • Yang, Z.1    Floyd, D.L.2    Loeber, G.3    Tong, L.4
  • 16
    • 0036065620 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate
    • Yang Z, Lanks CW Tong L (2002) Molecular mechanism for the regulation of human mitochondrial NAD(P)+-dependent malic enzyme by ATP and fumarate. Structure 10, 951 960.
    • (2002) Structure , vol.10 , pp. 951-960
    • Yang, Z.1    Lanks, C.W.2    Tong, L.3
  • 17
    • 0242507497 scopus 로고    scopus 로고
    • Structure and function of malic enzymes, a new class of oxidative decarboxylases
    • Chang GG Tong L (2003) Structure and function of malic enzymes, a new class of oxidative decarboxylases. Biochemistry 42, 12721 12733.
    • (2003) Biochemistry , vol.42 , pp. 12721-12733
    • Chang, G.G.1    Tong, L.2
  • 18
    • 0141621040 scopus 로고    scopus 로고
    • Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site
    • Rao GS, Coleman DE, Karsten WE, Cook PF Harris BG (2003) Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site. J Biol Chem 278, 38051 38058.
    • (2003) J Biol Chem , vol.278 , pp. 38051-38058
    • Rao, G.S.1    Coleman, D.E.2    Karsten, W.E.3    Cook, P.F.4    Harris, B.G.5
  • 19
    • 0025932524 scopus 로고
    • Purification and characterization of the cytosolic NADP(+)-dependent malic enzyme from human breast cancer cell line
    • Chang GG, Wang JK, Huang TM, Lee HJ, Chou WY Meng CL (1991) Purification and characterization of the cytosolic NADP(+)-dependent malic enzyme from human breast cancer cell line. Eur J Biochem 202, 681 688.
    • (1991) Eur J Biochem , vol.202 , pp. 681-688
    • Chang, G.G.1    Wang, J.K.2    Huang, T.M.3    Lee, H.J.4    Chou, W.Y.5    Meng, C.L.6
  • 21
    • 0028352978 scopus 로고
    • Characterization of cytosolic malic enzyme in human tumor cells
    • Loeber G, Dworkin MB, Infante A Ahorn H (1994) Characterization of cytosolic malic enzyme in human tumor cells. FEBS Lett 344, 181 186.
    • (1994) FEBS Lett , vol.344 , pp. 181-186
    • Loeber, G.1    Dworkin, M.B.2    Infante, A.3    Ahorn, H.4
  • 22
    • 0028358224 scopus 로고
    • Cloning and expression of pigeon liver cytosolic NADP(+)-dependent malic enzyme cDNA and some of its abortive mutants
    • Chou WY, Huang SM, Liu YH Chang GG (1994) Cloning and expression of pigeon liver cytosolic NADP(+)-dependent malic enzyme cDNA and some of its abortive mutants. Arch Biochem Biophys 310, 158 166.
    • (1994) Arch Biochem Biophys , vol.310 , pp. 158-166
    • Chou, W.Y.1    Huang, S.M.2    Liu, Y.H.3    Chang, G.G.4
  • 23
    • 0020519141 scopus 로고
    • Skeletal muscle NAD+(P) and NADP+-dependent malic enzyme in Friedreich's ataxia
    • Bottacchi E Di Donato S (1983) Skeletal muscle NAD+(P) and NADP+-dependent malic enzyme in Friedreich's ataxia. Neurology 33, 712 716.
    • (1983) Neurology , vol.33 , pp. 712-716
    • Bottacchi, E.1    Di Donato, S.2
  • 24
    • 0023607745 scopus 로고
    • Evidence for two distinct mitochondrial malic enzymes in human skeletal muscle: Purification and properties of the NAD(P)+-dependent enzyme
    • Taroni F, Gellera C Di Donato S (1987) Evidence for two distinct mitochondrial malic enzymes in human skeletal muscle: purification and properties of the NAD(P)+-dependent enzyme. Biochim Biophys Acta 916, 446 454.
    • (1987) Biochim Biophys Acta , vol.916 , pp. 446-454
    • Taroni, F.1    Gellera, C.2    Di Donato, S.3
  • 25
    • 0023083783 scopus 로고
    • Mitochondrial NADP-dependent malic enzyme of cod heart. Rate of forward and reverse reaction
    • Biegniewska A Skorkowski EF (1987) Mitochondrial NADP-dependent malic enzyme of cod heart. Rate of forward and reverse reaction. Comp Biochem Physiol B 86, 731 735.
    • (1987) Comp Biochem Physiol B , vol.86 , pp. 731-735
    • Biegniewska, A.1    Skorkowski, E.F.2
  • 26
    • 0021248051 scopus 로고
    • The pathways of glutamate and glutamine oxidation by tumor cell mitochondria. Role of mitochondrial NAD(P)+-dependent malic enzyme
    • Moreadith RW Lehninger AL (1984) The pathways of glutamate and glutamine oxidation by tumor cell mitochondria. Role of mitochondrial NAD(P)+-dependent malic enzyme. J Biol Chem 259, 6215 6221.
    • (1984) J Biol Chem , vol.259 , pp. 6215-6221
    • Moreadith, R.W.1    Lehninger, A.L.2
  • 27
    • 0026660577 scopus 로고
    • Kinetics and regulation of hepatoma mitochondrial NAD(P) malic enzyme
    • Teller JK, Fahien LA Davis JW (1992) Kinetics and regulation of hepatoma mitochondrial NAD(P) malic enzyme. J Biol Chem 267, 10423 10432.
    • (1992) J Biol Chem , vol.267 , pp. 10423-10432
    • Teller, J.K.1    Fahien, L.A.2    Davis, J.W.3
  • 28
    • 33747369870 scopus 로고    scopus 로고
    • Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial NAD(P)+-dependent malic enzyme: Functional roles of glutamine 362
    • Hsieh JY, Liu GY, Chang GG Hung HC (2006) Determinants of the dual cofactor specificity and substrate cooperativity of the human mitochondrial NAD(P)+-dependent malic enzyme: functional roles of glutamine 362. J Biol Chem 281, 23237 23245.
    • (2006) J Biol Chem , vol.281 , pp. 23237-23245
    • Hsieh, J.Y.1    Liu, G.Y.2    Chang, G.G.3    Hung, H.C.4
  • 29
    • 0019849889 scopus 로고
    • Glucose and triiodothyronine both induce malic enzyme in the rat hepatocyte culture: Evidence that triiodothyronine multiplies a primary glucose-generated signal
    • Mariash CN, McSwigan CR, Towle HC, Schwartz HL Oppenheimer JH (1981) Glucose and triiodothyronine both induce malic enzyme in the rat hepatocyte culture: evidence that triiodothyronine multiplies a primary glucose-generated signal. J Clin Invest 68, 1485 1490.
    • (1981) J Clin Invest , vol.68 , pp. 1485-1490
    • Mariash, C.N.1    McSwigan, C.R.2    Towle, H.C.3    Schwartz, H.L.4    Oppenheimer, J.H.5
  • 30
    • 0021264219 scopus 로고
    • Purification, kinetic behavior, and regulation of NAD(P)+ malic enzyme of tumor mitochondria
    • Moreadith RW Lehninger AL (1984) Purification, kinetic behavior, and regulation of NAD(P)+ malic enzyme of tumor mitochondria. J Biol Chem 259, 6222 6227.
    • (1984) J Biol Chem , vol.259 , pp. 6222-6227
    • Moreadith, R.W.1    Lehninger, A.L.2
  • 31
    • 0022354491 scopus 로고
    • Malic enzyme and malate dehydrogenase activities in rat tracheal epithelial cells during the progression of neoplasia
    • Wasilenko WJ Marchok AC (1985) Malic enzyme and malate dehydrogenase activities in rat tracheal epithelial cells during the progression of neoplasia. Cancer Lett 28, 35 42.
    • (1985) Cancer Lett , vol.28 , pp. 35-42
    • Wasilenko, W.J.1    Marchok, A.C.2
  • 32
    • 35348875299 scopus 로고    scopus 로고
    • Dietary nitrogen intake regulates hepatic malic enzyme messenger ribonucleic acid expression
    • Chendrimada TP, Freeman ME Davis AJ (2007) Dietary nitrogen intake regulates hepatic malic enzyme messenger ribonucleic acid expression. Poult Sci 86, 1980 1987.
    • (2007) Poult Sci , vol.86 , pp. 1980-1987
    • Chendrimada, T.P.1    Freeman, M.E.2    Davis, A.J.3
  • 33
    • 28044469286 scopus 로고    scopus 로고
    • Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human mitochondrial NAD(P)+-dependent malate dehydrogenase (malic enzyme)
    • Hung HC, Kuo MW, Chang GG Liu GY (2005) Characterization of the functional role of allosteric site residue Asp102 in the regulatory mechanism of human mitochondrial NAD(P)+-dependent malate dehydrogenase (malic enzyme). Biochem J 392, 39 45.
    • (2005) Biochem J , vol.392 , pp. 39-45
    • Hung, H.C.1    Kuo, M.W.2    Chang, G.G.3    Liu, G.Y.4
  • 34
    • 0016816729 scopus 로고
    • The mitochondrial malic enzymes. I. Submitochondrial localization and purification and properties of the NAD(P)+-dependent enzyme from adrenal cortex
    • Mandella RD Sauer LA (1975) The mitochondrial malic enzymes. I. Submitochondrial localization and purification and properties of the NAD(P)+-dependent enzyme from adrenal cortex. J Biol Chem 250, 5877 5884.
    • (1975) J Biol Chem , vol.250 , pp. 5877-5884
    • Mandella, R.D.1    Sauer, L.A.2
  • 35
    • 0023943545 scopus 로고
    • Purification and properties of the NAD(P)-dependent malic enzyme from human placental mitochondria
    • Zolnierowicz S, Swierczynski J Zelewski L (1988) Purification and properties of the NAD(P)-dependent malic enzyme from human placental mitochondria. Biochem Med Metab Biol 39, 208 216.
    • (1988) Biochem Med Metab Biol , vol.39 , pp. 208-216
    • Zolnierowicz, S.1    Swierczynski, J.2    Zelewski, L.3
  • 36
    • 25444513960 scopus 로고    scopus 로고
    • Functional roles of ATP-binding residues in the catalytic site of human mitochondrial NAD(P)+-dependent malic enzyme
    • Hung HC, Chien YC, Hsieh JY, Chang GG Liu GY (2005) Functional roles of ATP-binding residues in the catalytic site of human mitochondrial NAD(P)+-dependent malic enzyme. Biochemistry 44, 12737 12745.
    • (2005) Biochemistry , vol.44 , pp. 12737-12745
    • Hung, H.C.1    Chien, Y.C.2    Hsieh, J.Y.3    Chang, G.G.4    Liu, G.Y.5
  • 37
    • 0018194638 scopus 로고
    • Identification and properties of the nicotinamide adenine dinucleotide (phosphate)+-dependent malic enzyme in mouse ascites tumor mitochondria
    • Sauer LA Dauchy RT (1978) Identification and properties of the nicotinamide adenine dinucleotide (phosphate)+-dependent malic enzyme in mouse ascites tumor mitochondria. Cancer Res 38, 1751 1756.
    • (1978) Cancer Res , vol.38 , pp. 1751-1756
    • Sauer, L.A.1    Dauchy, R.T.2
  • 38
    • 2942563996 scopus 로고    scopus 로고
    • Dual functional roles of ATP in the human mitochondrial malic enzyme
    • Hsu WC, Hung HC, Tong L Chang GG (2004) Dual functional roles of ATP in the human mitochondrial malic enzyme. Biochemistry 43, 7382 7390.
    • (2004) Biochemistry , vol.43 , pp. 7382-7390
    • Hsu, W.C.1    Hung, H.C.2    Tong, L.3    Chang, G.G.4
  • 39
    • 0032867426 scopus 로고    scopus 로고
    • Preliminary crystallographic studies of human mitochondrial NAD(P)(+)-dependent malic enzyme
    • Bhargava G, Mui S, Pav S, Wu H, Loeber G Tong L (1999) Preliminary crystallographic studies of human mitochondrial NAD(P)(+)-dependent malic enzyme. J Struct Biol 127, 72 75.
    • (1999) J Struct Biol , vol.127 , pp. 72-75
    • Bhargava, G.1    Mui, S.2    Pav, S.3    Wu, H.4    Loeber, G.5    Tong, L.6
  • 40
    • 0042026574 scopus 로고    scopus 로고
    • Ascaris suum NAD-malic enzyme is activated by l-malate and fumarate binding to separate allosteric sites
    • Karsten WE, Pais JE, Rao GS, Harris BG Cook PF (2003) Ascaris suum NAD-malic enzyme is activated by l-malate and fumarate binding to separate allosteric sites. Biochemistry 42, 9712 9721.
    • (2003) Biochemistry , vol.42 , pp. 9712-9721
    • Karsten, W.E.1    Pais, J.E.2    Rao, G.S.3    Harris, B.G.4    Cook, P.F.5
  • 41
    • 0034696783 scopus 로고    scopus 로고
    • Lysine residues 162 and 340 are involved in the catalysis and coenzyme binding of NADP(+)-dependent malic enzyme from pigeon
    • Kuo CC, Tsai LC, Chin TY, Chang GG Chou WY (2000) Lysine residues 162 and 340 are involved in the catalysis and coenzyme binding of NADP(+)-dependent malic enzyme from pigeon. Biochem Biophys Res Commun 270, 821 825.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 821-825
    • Kuo, C.C.1    Tsai, L.C.2    Chin, T.Y.3    Chang, G.G.4    Chou, W.Y.5
  • 42
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 44
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673 4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 45
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace AC, Laskowski RA Thornton JM (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng 8, 127 134.
    • (1995) Protein Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.