Methionyl tRNA synthetase

Ferguson, B., and Yang, D. (1986) Localization of noncovalently bound ethidium in free and methionyl-tRNA synthetase bound tRNA(fMet) by singlet - singlet energy transfer. Biochemistry 25, 5298. 

METHIONYL-tRNA SYNTHETASE METHIONYL-tRNA FORMYLTRANSFERASE METHIONYL-tRNA SYNTHETASE AMINO-ACYL tRNA SYNTHETASES Method of continuous variation,... 

METHIONINE ADENOSYLTRANSFERASE METHIONYL-tRNA SYNTHETASE NAD SYNTHETASE... 

Discrimination between some pairs of tRNAs depends entirely on the anticodon sequence. For example, tRNAMet contains the anticodon CAU. That for a minor tRNAIle is the same except that the cytosine has been posttranscriptionally modified by covalent linkage of a molecule of lysine via its e-amino group to C2 of the cytosine. The latter base (Iysidine) is correctly recognized by E. coli isoleucyl-tRNA synthetase but, if the cytosine is unmodified, it is aminoacylated by methionyl-tRNA synthetase.192 In most instances the acceptor specificity, or tRNA identity, is not determined solely by the anticodon sequence. Thus, when a methionine initiator tRNA was modified to contain a tryptophan anticodon, it was only partially charged with tryptophan in vivo. However, when A73 of the methionine tRNA was also converted to G73, only tryptophan was inserted.193 Nucleotide 73 (Fig. 

A similar editing process prevents isoleucyl-, leucyl-, and methionyl-tRNA synthetases from attaching L-homocysteine to tRNAs 260-263 In this case, instead of hydrolysis the editing site catalyzes conversion of the homocysteinyl-adenylate into homocysteine lactone. Naturally occurring mutations in tRNA molecules can sometimes have serious consequences. For example, a human mutation is responsible for a fragile mitochondrial isoleucine tRNA and serious cardiomyopathy and opthalmophegia (see also Box 18-B).263a... 

The methionyl-tRNA synthetase edits Tnisactivated homocysteine before the transfer to tRNAMet. The homocysteinyl adenylate complex is rapidly decomposed in the absence of tRNA. The reaction is, however, idiosyncratic, in that it invokes the cyclization of the intermediate to give the thiolactone.12... 

Biosynthetic processes Elongation of RNA or DNA chains Other synthetic routes RNA polymerase I DNA polymerase Poly(ADP-ribose)polymerase Carbamoyl phosphate synthetase Anthranilate synthase-phosphoribosyl transferase Glycogen synthetase Methionyl-tRNA synthetase ATP phosphoribosyl transferase Zn2+... 

Burnell, J.N. 1981. Methionyl-tRNA synthetase from Phaseolus aureus purification and properties. Plant Physiol. 67, 316-324. 

Jarvest, R.L. et al. 2002. Nanomolar inhibitors of Staphylococcus aureus methionyl tRNA synthetase with potent antibacterial activity against gram-positive pathogens. J. Med. Chem. 45, 1959-1962. 

Jarvest, R.L. et al. 2003. Optimisation of aryl substitution leading to potent methionyl tRNA synthetase inhibitors with excellent gram-positive antibacterial activity. Bioorg. Med. Chem. Lett. 13, 665-668. 

Experimental agents were assayed for their ability to inhibit the enzyme methionyl tRNA synthetase according to the method of Heischmann (1). Aminoacylation assay test results are provided in Table 1. 

Kiick KL, Tirrell DA. Protein engineering by in vivo incorporation of non-natural amino acids Control of incorporation of methionine analogues by methionyl-tRNA synthetase. Tetrahedron 2000 56 9487-9493. 

L. Serre, G. Verdon, T. Choinowski, N. Hervouet, J.L. Risler, and C. Zelwer. 2001. Ho v methionyl-tRNA synthetase creates its amino acid recognition pocket upon 1-methionine binding J. Mol. Biol. 306 863-876. (PubMed)... 

As mentioned, the mildness of NaBHaCN (coupled with its effectiveness and stability in aqueous media) has attracted considerable interest for applications in biochemical areas. Examples include the trapping of suspected imine intermediates produced in enzyme (mitochondrial monoamine oxidase) inactivation by amines, the establishment by reduction of the positions of imine-forming amines in 2-keto-3-deoxy-6-phosphogluconate aldolase, and the transfer labeling of methionyl-tRNA synthetase and methionyl-tRNA transformalase by treatment with periodate-treated tRNA. In fact, most biochemical applications of NaBHaCN have utilized in situ imine formation-reduction (i.e. reductive amination) conditions and will be further discussed in Section 1.2.2.3.1. 

Analyses of in situ DNA synthesis of Euglena gracilis identify zinc-dependent steps in the eukaryotic cell cycle and show that the derangements in RNA metabolism are critical determinants of the growth arrest associated with zinc deficiency. Combined use of microwave-induced emission spectrometry and micro gel emulsion chromatography shows the presence of stoichiometric amounts of zinc essential to the function of E. gracilis and yeast RNA polymerases, the reverse transcriptases" from avian myeloblastosis, murine leukemic and woolly type C viruses, and E. coli methionyl tRNA synthetase. These results stress the importance of zinc to both nucleic acid and protein metabolism. Transient-state kinetic studies of carboxypeptidase A show that zinc functions in the catalytic step of peptide hydrolysis and in the binding step of ester hydrolysis. 

Vaughan, M. D., Sampson, P. B., Daub, E. and Honek, J. F. (2005) Investigation of bioisosteric effects on the interaction of substrates inhibitors with the methionyl-tRNA synthetase from Escherichia coli. Med Chem., 1, 227-237. 

Crepin, T., Schmitt, E., Mechulam, Y., et al. (2003) Use of analogues of methionine and methio-nyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase. J. Mol. Biol., 332(1), 59-72. 

The initiator tRNA molecule in prokaryotes—tRNA — has several properties that distinguish it from all other tRNA molecules. One feature is that the tRNA is first acylated with methionine, and then the methionine is modified. Acylation is by methionyl tRNA synthetase, which also charges tRNA . However, the methionine of charged tRNA is immediately recognized by another enzyme, tRNA methionyl transformylase, which transfers a formyl group from N °-formyltetrahydrofolate (fTHF) to the amino group of the methionine to form... 

Serre, L.. Verdon, G.. Choinowski, T., Hervouct, N., Risler, J. L, and Zelwer, C. 2001. How methionyl-tRNA. synthetase creates its amino acid recognition pocket upon l,-methionine binding./. Mol Biol 306 863-876. 

Methionyl tRNA synthetase, (a) The enzyme specifically recognizes the amino acid methionine in one region of the active site and the methionyl tRNA in another, (b) The acylation reaction that results in a covalent linkage of the amino acid to the tRNA. 

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