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Kinase guanylate

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]

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]

Figure 2 Synthesis of nucleoside triphosphates (1) Adenylate kinase (EC 2.1 A3, N = A,C,U) or guanylate kinase (EC 2.7.4.8, N = G), or nucleoside monophosphate kinase (EC 2.7.4.4, N = U). (2) Pyruvate kinase (EC 2.7.1.40). NMP, nucleoside monophosphate NDP, nucleoside diphosphate NTP, nucleoside triphosphate. (From Ref. 12.)... Figure 2 Synthesis of nucleoside triphosphates (1) Adenylate kinase (EC 2.1 A3, N = A,C,U) or guanylate kinase (EC 2.7.4.8, N = G), or nucleoside monophosphate kinase (EC 2.7.4.4, N = U). (2) Pyruvate kinase (EC 2.7.1.40). NMP, nucleoside monophosphate NDP, nucleoside diphosphate NTP, nucleoside triphosphate. (From Ref. 12.)...
Acyclovir (ACV) is not a true nucleoside, because the guanine residue is attached to an open-chain structure, but it mimics deoxyribose well enough for the compound to be accepted as a substrate by a thymidine kinase specified by certain herpes-type viruses. The normal thymidine kinase in mammalian cells does not recognize ACV as a substrate, however, so only virus-infected cells convert ACV to its monophosphate. Once the first phosphate has been added, the second phosphate is added by cellular guanylate kinase several other cellular kinases can add the third phosphate. The triphosphate is a more potent inhibitor of the viral DNA polymerases than of cellular DNA polymerases and also inactivates the former but not the latter. The net result is that ACV has been an effective treatment of, and prophylaxis for, genital herpes. Also it can result in dramatic relief of pain associated with shingles caused by reactivation of latent varicella-zoster virus, and has been successful in many patients with herpes encephalitis. [Pg.552]

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See also in sourсe #XX -- [ Pg.906 ]

See also in sourсe #XX -- [ Pg.67 ]



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Guanylate

Guanylate kinase, inhibitors

Guanylate kinase, structure

Guanylation

Kinases guanylate kinase

Kinases guanylate kinase

Membrane-associated guanylate kinase

Membrane-associated guanylate kinase inverted-2 (MAGI

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