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Kinases guanylate kinase

Adaptor Proteins. Figure 1 Adaptor protein domains. A scheme of the domain structures of some well-characterized adaptor proteins is shown. Descriptions of domain characteristics are in main text except C2, binds to phospholipids GTPase activating protein (GAP) domain, inactivates small GTPases such as Ras Hect domain, enzymatic domain of ubiquitin ligases and GUK domain, guanylate kinase domain. For clarity, not all domains contained within these proteins are shown. [Pg.15]

Wu, Y., Dowbenko, D., Spencer, S., Laura, R., Lee, J., Gu Q., Lasky L.A. Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase 2000, J. Biol. Chem. 275 21477-21485... [Pg.333]

Fig. 16.11. Model of the association of Fyn kinase with the NMDA receptor The NMDA receptor is shown as a tetramer of NRl and NR2 subunits. The C-terminal tail of NR2 interacts with PDZ2 of PSD-95. The protein tyrosine kinase Fyn is assumed to bind to PDZ3 of PSD-95 via its SH2 domain. Fyn also is anchored to the ceU membrane via its myristoylated N-terminus. GK guanylate kinase domain of PSD-95. According to Sala and Sheng (1999), with permission. Fig. 16.11. Model of the association of Fyn kinase with the NMDA receptor The NMDA receptor is shown as a tetramer of NRl and NR2 subunits. The C-terminal tail of NR2 interacts with PDZ2 of PSD-95. The protein tyrosine kinase Fyn is assumed to bind to PDZ3 of PSD-95 via its SH2 domain. Fyn also is anchored to the ceU membrane via its myristoylated N-terminus. GK guanylate kinase domain of PSD-95. According to Sala and Sheng (1999), with permission.
Hall, S.W. Kiihn, H. Purification and properties of guanylate kinase from bovine retinas and rod outer segments. Eur. J. Biochem., 161, 551-556 (1986)... [Pg.512]

ATP GMP phosphotransferase GMP kinase deoxyguanylate kinase guanosine monophosphate kinase kinase, guanylate (phosphorylating)... [Pg.543]

GMP <2, 7> (<2> competitive inhibitor to dGMP [2] <7> non competitive with respect to MgATP because of the formation of an abortive complex guanylate kinase-MgATP "GMP [18]) [2, 18]... [Pg.546]

Oeschger, M. Guanylate kinase from Escherichia coli B. Methods EnzymoL, 51, 473-482 (1978)... [Pg.553]

Moriguchi, M. Kohno, H. Kamei, M. Tochikura, T. Purification and properties of guanylate kinase from bakers yeast. Biochim. Biophys. Acta, 662, 165-167 (1981)... [Pg.553]

Berger, A. Schiltz, E. Schultz, G.E. Guanylate kinase from Saccharomyces cerevisiae. Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases. Eur. J. Biochem., 184, 433-443 (1989)... [Pg.553]

Stehle, T. Schultz, G.E. Temperature-dependent space-group transitions in crystals of guanylate kinase from yeast. Acta Crystallogr. Sect. B Struct. Sci., B48, 546-548 (1992)... [Pg.553]

Le Floc h, F. Lafleuriel, J. Purification and properties of guanylate kinase of mitochondrias from tubers of Jerusalem artichoke. Plant Physiol. Biochem., 28, 191-201 (1990)... [Pg.553]

Agarwal, K.C. Parks, R.E. Inhibition of rat hepatic guanylate kinase by 6-thioguanosine-5-phosphate and 6-selenoguanosine-5-phosphate. Biochem. Pharmacol., 24, 791-795 (1975)... [Pg.553]

Nave, J.-F. Eschbach, A. Halazy, S. 9-(Phosphonoalkyl)guanine derivatives as substrates or inhibitors of guanylate kinase. Arch. Biochem. Biophys., 295, 253-257 (1992)... [Pg.553]

Boehme, R.E. Phosphorylation of the antiviral precursor 9-(l,3-dihydroxy-2-propoxymethyl)guanine monophosphate by guanylate kinase isozymes. J. Biol. Chem., 259, 12346-12349 (1984)... [Pg.553]

Prinz, H. Lavie, A. Scheidig, A.J. Spangenberg, O. Konrad, M. Binding of nucleotides to guanylate kinase, p21(ras), and nucleoside-diphosphate kinase studied by nano-electrospray mass spectrometry. J. Biol. Chem., 274, 35337-35342 (1999)... [Pg.554]

Blaszczyk, J. Li, Y Yan, H. Ji, X. Crystal structure of unligated guanylate kinase from yeast reveals GMP-induced conformational changes. J. Mol. Biol., 307, 247-257 (2001)... [Pg.554]

Stolworthy, T.S. Black, M.E. The mouse guanylate kinase double mutant E72Q/D103N is a functional adenylate kinase. Protein Eng., 14, 903-909 (2001)... [Pg.554]

This reaction is fully reversible, so after the intense demand for ATP ends, the enzyme can recycle AMP by converting it to ADP, which can then be phosphorylated to ATP in mitochondria A similar enzyme, guanylate kinase, converts GMP to GDP at the expense of ATP. By pathways such as these, energy conserved in the catabolic production of ATP is used to supply the cell with all required NTPs and dNTPs. [Pg.505]

See other pages where Kinases guanylate kinase is mentioned: [Pg.235]    [Pg.17]    [Pg.284]    [Pg.812]    [Pg.198]    [Pg.321]    [Pg.72]    [Pg.326]    [Pg.725]    [Pg.543]    [Pg.543]    [Pg.544]    [Pg.545]    [Pg.546]    [Pg.547]    [Pg.548]    [Pg.549]    [Pg.549]    [Pg.550]    [Pg.551]    [Pg.552]    [Pg.553]    [Pg.553]    [Pg.554]    [Pg.554]    [Pg.554]    [Pg.554]    [Pg.636]   
See also in sourсe #XX -- [ Pg.906 ]



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