메뉴 건너뛰기




Volumn 366, Issue 4, 2008, Pages 994-1000

Interaction of human 3-phosphoglycerate kinase with l-ADP, the mirror image of d-ADP

Author keywords

Enantioselectivity; Enzyme kinetic analysis; Human 3 phosphoglycerate kinase; Microcalorimetry; Nucleotide substrates; Small angle X ray scattering

Indexed keywords

ADENOSINE; ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE MAGNESIUM; PHOSPHOGLYCERATE KINASE;

EID: 37749046016     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.12.061     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 0037085269 scopus 로고    scopus 로고
    • Phosphorylation of pyrimidine deoxynucleoside analog diphosphates: selective phosphorylation of l-nucleoside analog diphosphates by 3-phosphoglycerate kinase
    • Krishnan P., Fu Q., Lam W., Liou J.Y., Dutschman G., and Cheng Y.C. Phosphorylation of pyrimidine deoxynucleoside analog diphosphates: selective phosphorylation of l-nucleoside analog diphosphates by 3-phosphoglycerate kinase. J. Biol. Chem. 277 (2002) 5453-5459
    • (2002) J. Biol. Chem. , vol.277 , pp. 5453-5459
    • Krishnan, P.1    Fu, Q.2    Lam, W.3    Liou, J.Y.4    Dutschman, G.5    Cheng, Y.C.6
  • 3
    • 33747158845 scopus 로고    scopus 로고
    • l-nucleoside enantiomers as antivirals drugs: a mini-review
    • Mathé C., and Gosselin G. l-nucleoside enantiomers as antivirals drugs: a mini-review. Antiviral Res. 71 (2006) 276-281
    • (2006) Antiviral Res. , vol.71 , pp. 276-281
    • Mathé, C.1    Gosselin, G.2
  • 4
    • 0026536746 scopus 로고
    • Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-d-glycerate
    • Harlos K., Vas M., and Blake C.C.F. Crystal structure of the binary complex of pig muscle phosphoglycerate kinase and its substrate 3-phospho-d-glycerate. Proteins 12 (1992) 133-144
    • (1992) Proteins , vol.12 , pp. 133-144
    • Harlos, K.1    Vas, M.2    Blake, C.C.F.3
  • 5
  • 6
    • 0031573453 scopus 로고    scopus 로고
    • Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability
    • Auerbach G., Huber R., Grattinger M., Zaiss K., Schurig H., Jaenicke R., and Jacob U. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure 5 (1997) 1475-1483
    • (1997) Structure , vol.5 , pp. 1475-1483
    • Auerbach, G.1    Huber, R.2    Grattinger, M.3    Zaiss, K.4    Schurig, H.5    Jaenicke, R.6    Jacob, U.7
  • 7
    • 0032584315 scopus 로고    scopus 로고
    • Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism
    • Bernstein B.E., and Hol W.G. Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism. Biochemistry 37 (1998) 4429-4436
    • (1998) Biochemistry , vol.37 , pp. 4429-4436
    • Bernstein, B.E.1    Hol, W.G.2
  • 8
    • 0037118690 scopus 로고    scopus 로고
    • Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: correlation between nucleotide binding mode and helix flexibility
    • Kovári Z., Flachner B., Náray-Szabó G., and Vas M. Crystallographic and thiol-reactivity studies on the complex of pig muscle phosphoglycerate kinase with ATP analogues: correlation between nucleotide binding mode and helix flexibility. Biochemistry 41 (2002) 8796-8806
    • (2002) Biochemistry , vol.41 , pp. 8796-8806
    • Kovári, Z.1    Flachner, B.2    Náray-Szabó, G.3    Vas, M.4
  • 9
    • 12144285772 scopus 로고    scopus 로고
    • Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP
    • Flachner B., Kovári Z., Varga A., Gugolya Z., Vonderviszt F., Náray-Szabó G., and Vas M. Role of phosphate chain mobility of MgATP in completing the 3-phosphoglycerate kinase catalytic site: binding, kinetic, and crystallographic studies with ATP and MgATP. Biochemistry 43 (2004) 3436-3449
    • (2004) Biochemistry , vol.43 , pp. 3436-3449
    • Flachner, B.1    Kovári, Z.2    Varga, A.3    Gugolya, Z.4    Vonderviszt, F.5    Náray-Szabó, G.6    Vas, M.7
  • 10
    • 33747099931 scopus 로고    scopus 로고
    • Overcoming HIV drug resistance through rational drug design based on molecular, biochemical, and structural profiles of HIV resistance
    • Yin P.D., Das D., and Mitsuya H. Overcoming HIV drug resistance through rational drug design based on molecular, biochemical, and structural profiles of HIV resistance. Cell Mol. Life Sci. 63 (2006) 1706-1724
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 1706-1724
    • Yin, P.D.1    Das, D.2    Mitsuya, H.3
  • 11
    • 29344443515 scopus 로고    scopus 로고
    • Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase
    • Flachner B., Varga A., Szabó J., Barna L., Hajdú I., Gyimesi G., Závodszky P., and Vas M. Substrate-assisted movement of the catalytic Lys 215 during domain closure: site-directed mutagenesis studies of human 3-phosphoglycerate kinase. Biochemistry 44 (2005) 16853-16865
    • (2005) Biochemistry , vol.44 , pp. 16853-16865
    • Flachner, B.1    Varga, A.2    Szabó, J.3    Barna, L.4    Hajdú, I.5    Gyimesi, G.6    Závodszky, P.7    Vas, M.8
  • 12
    • 17444400179 scopus 로고
    • Crystallisation and comparative studies of d-3-phosphoglyceraldehyde dehydrogenase from muscle of various mammals
    • Elo{combining double acute accent}di P., and Szörényi E. Crystallisation and comparative studies of d-3-phosphoglyceraldehyde dehydrogenase from muscle of various mammals. Acta Physiol. Hung. 9 (1956) 339-350
    • (1956) Acta Physiol. Hung. , vol.9 , pp. 339-350
    • Elodi, P.1    Szörényi, E.2
  • 14
    • 0001070572 scopus 로고
    • The acyl-enzyme intermediate and the kinetic mechanism of the glyceraldehyde 3-phosphate dehydrogenase reaction
    • Furfine C.S., and Velick S.F. The acyl-enzyme intermediate and the kinetic mechanism of the glyceraldehyde 3-phosphate dehydrogenase reaction. J. Biol. Chem. 240 (1965) 844-855
    • (1965) J. Biol. Chem. , vol.240 , pp. 844-855
    • Furfine, C.S.1    Velick, S.F.2
  • 15
    • 14644404369 scopus 로고    scopus 로고
    • The enantioselectivities of the active and allosteric sites of mammalian ribonucleotide reductase
    • He J., Roy B., Perigaud C., Kashlan O.B., and Cooperman B.S. The enantioselectivities of the active and allosteric sites of mammalian ribonucleotide reductase. FEBS J. 272 (2005) 1236-1242
    • (2005) FEBS J. , vol.272 , pp. 1236-1242
    • He, J.1    Roy, B.2    Perigaud, C.3    Kashlan, O.B.4    Cooperman, B.S.5
  • 16
    • 0021116194 scopus 로고
    • Measurement of the dissociation constant of MgATP at physiological nucleotide levels by a combination of 31P NMR and optical absorbance spectroscopy
    • Gupta R.K., Gupta P., Yashok W.P., and Rose Z.B. Measurement of the dissociation constant of MgATP at physiological nucleotide levels by a combination of 31P NMR and optical absorbance spectroscopy. Biochem. Biophys. Res. Commun. 117 (1983) 210-216
    • (1983) Biochem. Biophys. Res. Commun. , vol.117 , pp. 210-216
    • Gupta, R.K.1    Gupta, P.2    Yashok, W.P.3    Rose, Z.B.4
  • 17
    • 0031554720 scopus 로고    scopus 로고
    • 2+ macroelectrodes under conditions pertinent to 31P NMR ionized magnesium determinations
    • 2+ macroelectrodes under conditions pertinent to 31P NMR ionized magnesium determinations. Anal. Biochem. 251 (1997) 246-250
    • (1997) Anal. Biochem. , vol.251 , pp. 246-250
    • Zhang, W.1    Truttmann, A.C.2    Luthi, D.3    McGuigan, J.A.4
  • 18
    • 0014895743 scopus 로고
    • 3-Phosphoglycerate kinase from rabbit skeletal muscle and yeast
    • Krietsch W.K., and Bücher T. 3-Phosphoglycerate kinase from rabbit skeletal muscle and yeast. Eur. J. Biochem. 17 (1970) 568-580
    • (1970) Eur. J. Biochem. , vol.17 , pp. 568-580
    • Krietsch, W.K.1    Bücher, T.2
  • 19
    • 0022454691 scopus 로고
    • The phosphate group of 3-phosphoglycerate accounts for conformational changes occurring on binding to 3-phosphoglycerate kinase. Enzyme inhibition and thiol reactivity studies
    • Tompa P., Hong P.T., and Vas M. The phosphate group of 3-phosphoglycerate accounts for conformational changes occurring on binding to 3-phosphoglycerate kinase. Enzyme inhibition and thiol reactivity studies. Eur. J. Biochem. 154 (1986) 643-649
    • (1986) Eur. J. Biochem. , vol.154 , pp. 643-649
    • Tompa, P.1    Hong, P.T.2    Vas, M.3
  • 20
    • 0000957077 scopus 로고
    • Studies on liver alcohol dehydrogenase complexes. III. Multiple inhibition kinetics in the presence of two competitive inhibitors
    • Yonetani T., and Theorell H. Studies on liver alcohol dehydrogenase complexes. III. Multiple inhibition kinetics in the presence of two competitive inhibitors. Arch. Biochem. Biophys. 106 (1964) 243-351
    • (1964) Arch. Biochem. Biophys. , vol.106 , pp. 243-351
    • Yonetani, T.1    Theorell, H.2
  • 21
    • 34248347847 scopus 로고    scopus 로고
    • Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg
    • Roessle M.W., et al. Upgrade of the small-angle X-ray scattering beamline X33 at the European Molecular Biology Laboratory, Hamburg. J. Appl. Cryst. 40 (2007) s190-s194
    • (2007) J. Appl. Cryst. , vol.40
    • Roessle, M.W.1
  • 22
    • 33646174431 scopus 로고    scopus 로고
    • Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase
    • Varga A., Flachner B., Konarev P., Gráczer E., Szabó J., Svergun D., Závodszky P., and Vas M. Substrate-induced double sided H-bond network as a means of domain closure in 3-phosphoglycerate kinase. FEBS Lett. 580 (2006) 2698-2706
    • (2006) FEBS Lett. , vol.580 , pp. 2698-2706
    • Varga, A.1    Flachner, B.2    Konarev, P.3    Gráczer, E.4    Szabó, J.5    Svergun, D.6    Závodszky, P.7    Vas, M.8
  • 23
    • 33645214738 scopus 로고    scopus 로고
    • ATSAS 2.1, a program package for small-angle scattering data analysis
    • Konarev P.V., Volkov V.V., Petoukhov M.V., and Svergun D.I. ATSAS 2.1, a program package for small-angle scattering data analysis. J. Appl. Cryst. 39 (2006) 277-286
    • (2006) J. Appl. Cryst. , vol.39 , pp. 277-286
    • Konarev, P.V.1    Volkov, V.V.2    Petoukhov, M.V.3    Svergun, D.I.4
  • 24
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D.I., Barberato C., and Koch M.H.J. CRYSOL-a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28 (1995) 768-773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 25
    • 0027234028 scopus 로고
    • 2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium dialysis binding and enzyme kinetic data
    • 2+ affects the binding of ADP but not ATP to 3-phosphoglycerate kinase. Correlation between equilibrium dialysis binding and enzyme kinetic data. Biochem. J. 293 (1993) 595-599
    • (1993) Biochem. J. , vol.293 , pp. 595-599
    • Molnár, M.1    Vas, M.2
  • 26
    • 0037039416 scopus 로고    scopus 로고
    • Nucleotide binding to pig muscle 3-phosphoglycerate kinase in the crystal and in solution: relationship between substrate antagonism and interdomain communication
    • Merli A., Szilágyi A.N., Flachner B., Rossi G.L., and Vas M. Nucleotide binding to pig muscle 3-phosphoglycerate kinase in the crystal and in solution: relationship between substrate antagonism and interdomain communication. Biochemistry 41 (2002) 111-119
    • (2002) Biochemistry , vol.41 , pp. 111-119
    • Merli, A.1    Szilágyi, A.N.2    Flachner, B.3    Rossi, G.L.4    Vas, M.5
  • 27
    • 17444381136 scopus 로고    scopus 로고
    • Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase
    • Varga A., Flachner B., Gráczer E., Osváth S., Szilágyi A.N., and Vas M. Correlation between conformational stability of the ternary enzyme-substrate complex and domain closure of 3-phosphoglycerate kinase. FEBS J. 272 (2005) 1867-1885
    • (2005) FEBS J. , vol.272 , pp. 1867-1885
    • Varga, A.1    Flachner, B.2    Gráczer, E.3    Osváth, S.4    Szilágyi, A.N.5    Vas, M.6
  • 28
    • 0018276904 scopus 로고
    • 31P NMR study of bound reactants and products of yeast 3-phosphoglycerate kinase at equilibrium and the effect of sulfate ion
    • Nageswara-Rao B.D., Cohn M., and Scopes R.K. 31P NMR study of bound reactants and products of yeast 3-phosphoglycerate kinase at equilibrium and the effect of sulfate ion. J. Biol. Chem. 253 (1978) 8056-8060
    • (1978) J. Biol. Chem. , vol.253 , pp. 8056-8060
    • Nageswara-Rao, B.D.1    Cohn, M.2    Scopes, R.K.3
  • 29
    • 0028968241 scopus 로고
    • Transient and equilibrium kinetic studies on yeast 3-phosphoglycerate kinase. Evidence that an intermediate containing 1,3-bisphosphoglycerate accumulates in the steady state
    • Schmidt P.P., Travers F., and Barman T. Transient and equilibrium kinetic studies on yeast 3-phosphoglycerate kinase. Evidence that an intermediate containing 1,3-bisphosphoglycerate accumulates in the steady state. Biochemistry 34 (1995) 824-832
    • (1995) Biochemistry , vol.34 , pp. 824-832
    • Schmidt, P.P.1    Travers, F.2    Barman, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.