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Protein methyltransferases

Trievel RC, Beach BM, Dirk LMA, Houtz RL, Hurley JH (2002) Structure and catalytic mechanism of a set domain protein methyltransferase. Cell 111 91—103... [Pg.350]

Fig. 13 DNA-protein CT reactions. The DNA-bound protein, methyltransferase Hhal (mutant Q237W), flips a base out of the DNA double helix and inserts a trytophan side chain leaving the /r-stack largely unperturbed. This intercalated trytophan moiety transfers an electron to [Ru(bpy )(dppz)(phen)]3+, generated by flash quench, over 50 A away. Adapted from [164]... [Pg.109]

Chen D, Ma H, Hong H, Koh SS, Huang SM, Schurter BT, Aswad DW, Stallcup MR (1999) Regulation of transcription by a protein methyltransferase. Science 284 2174-2177 Chubb JR, Boyle S, Perry P, Bickmore WA (2002) Chromatin motion is constrained by association with nuclear compartments in human cells. Curr Biol 12 439-445 Croston GE, Kadonaga JT (1993) Role of chromatin structure in the regulation of transcription by RNA polymerase II. Curr Opin Cell Biol 5 417-423... [Pg.24]

Mai, A., Valente, S., Cheng, D., Perrone, A., Ragno, R., Simeoni, S. et al. (2007) Synthesis and biological validation of novel synthetic histone/protein methyltransferase inhibitors. ChemMedChem, 3, 987-991. [Pg.85]

Fig. 10 SAM and clickable SAM analogs for labeling protein methyltransferase substrates... Fig. 10 SAM and clickable SAM analogs for labeling protein methyltransferase substrates...
Peters W, Willnow S, Duisken M et al (2010) Enzymatic site-specific functionalization of protein methyltransferase substrates with alkynes for click labeling. Angew Chem Int Ed Engl 49 5170-5173... [Pg.41]

Ma, Y.T., Shi, Y.Q., Lim, Y.H., McGrail, S.H., Ware, J.A., and Rando, R.R. (1994). Mechanistic studies on human platelet isoprenylated protein methyltransferase farnesyl-cysteine analogs block platelet aggregation without inhibiting the methyltransferase. Biochemistry 33 5414-5420. [Pg.89]

Gilbert, B.A.,Tan,E.W., Perez-Sala, D.,andRando, R.R. (1992). Structure activity studies on the retinal rod outer segment isoprenylated protein methyltransferase. J Am Chem Soc 114 3966-3973. [Pg.228]

Marciano, D., Aharonson, Z., Varsano, T., Haklai, R., and Kloog, Y. (1997). Novel inhibitors of the prenylated protein methyltransferase reveal distinctive structural requirements. Bioorg Med Chem Lett 7 1709-1714. [Pg.228]

An important structural difference between eliminases and mutases concerns the axial base coordinated to the cobalt, perpendicular to the plane of the corrin ring. Whereas in all the eliminases, the axial base is the dimethylbenzimidazole of the coenzyme itself (Fig. 1), the mutases use a conserved histidine residue of the enzyme for this purpose. On binding of the coenzyme to the apo-enzyme, the axial base is replaced by the histidine and moves into a distinct pocket of the protein. Methyltransferases (see below) also use a protein histidine as axial base, whose reactivity is fine tuned by protonation. Possibly the mutases and methyltransferases have a common evolutionary origin, whereas the eliminases evolved separately. [Pg.65]

Li, C. Clarke, S. (1992). A protein methyltransferase specific for altered aspartyl residues is important in Escherichia coli stationary-phase survival and heat-shock resistance. Proc. Natl. Acad. Sci. USA 89, 9885-9889. [Pg.301]

Pollack, B. P. et al. (1999). The human homologue of the yeast proteins Skbl and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J. Biol. Chem. 274(44), 31531-31542. [Pg.221]

Djordjevic, S. and Stock, A.M. (1998). Ghemotaxis receptor recognition by protein methyltransferase GheR. Nature Struct. Biol. 5, 446-450. [Pg.178]

Further insight into transcriptional regulation of the ST cluster has come from an A. nidulans mutant hunt. Complementation of a mutant unable to express aflR or stc genes - but otherwise near wild-type in appearance - revealed the laeA (loss of aflR expression) gene. This gene encodes a putative protein methyltransferase... [Pg.203]

Alignment of the MetH sequence between residues 366 and -610 with a methyltetrahydrofolate corrinoid iron-sulfur protein methyltransferase (AcsE) reveals 22% identity and 43% homology between these proteins (6) the same region of MetH is more distantly related to pteroate synthase (6, 31). Structures for pteroate synthase (52, 55) and the recently determined structure of AcsE (6) predict that the folate binding module will be a (Pa)g barrel. Model-building (6)... [Pg.191]

Willnow, S., Martin, M., Liischer, B., and Weinhold, E. (2012) A selenium-based click AdoMet analogue for versatile substrate labeling with wild-type protein methyltransferases. ChemBioChem, 13, 1167-1173. [Pg.422]

Copeland RA, Solomon ME, Richon VM (2009) Protein methyltransferases as a target class for drug discovery. Nat Rev Drug Discov 8 724-732... [Pg.147]

All the available evidence indicates that S-adenosyl-L-methi-onine is the sole biological methyl donor for the above protein methyltransferases, and the demethylated reaction product S-adeno-syl-L-homocysteine is a potent competitive inhibitor for the reaction (2,18,19). Thus, there have been a few attempts in the past to investigate the effect of modification of various regions of these compounds on the reaction of protein methyltransferases. These investigations are not only important in elucidation of the reaction mechanism, but also in practical application where only a desired methylation reaction can be selectively studied, while others are inhibited and/or modulated. [Pg.57]

In the present brief chapter, we review the effect of various derivatives and analogs of S-adenosyl-L-methionine and S-adenosyl-L-homocysteine on protein methyltransferases. In doing this, we first review protein methylase I and III reaction, and is followed by our recent data on protein methylase II reaction. [Pg.57]


See other pages where Protein methyltransferases is mentioned: [Pg.311]    [Pg.255]    [Pg.363]    [Pg.365]    [Pg.594]    [Pg.24]    [Pg.26]    [Pg.171]    [Pg.87]    [Pg.88]    [Pg.228]    [Pg.228]    [Pg.1099]    [Pg.341]    [Pg.594]    [Pg.288]    [Pg.347]    [Pg.311]    [Pg.219]    [Pg.222]    [Pg.456]    [Pg.68]    [Pg.148]    [Pg.374]    [Pg.390]   


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