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Peptide acceptors in the arginine transfer reaction






Journal of Biological Chemistry 248(8): 2918-2921

Peptide acceptors in the arginine transfer reaction



Accession: 006079611

PMID: 4572514



Related references

Soffer, R.L., 1973: Peptide acceptors in the leucine, phenylalanine transfer reaction. Journal of Biological Chemistry 248(24): 8424-8428

Kotlova, E.K.; Levin, E.D.; Yusupova, M.P.; Rozynov, B.V.; Stepanov, V.M., 1994: Reaction of transformylation-transfer of N-formyl residue from the amino acid and peptide derivatives to nucleophilic groups as a side reaction in peptide synthesis. The formyl group transfer from N-formyl amino acids and their derivatives to other acceptors - amino acids esters and aniline, was studied. Formylamino acids with the free alpha-carboxyl group are more effective donors in transformylation than for...

Charlier, J.; Gerlo, E., 1976: Arginyl transfer rna synthetase ec 6.1.1.19 from escherichia coli influence of arginine biosynthetic precursors on the charging of arginine acceptor transfer rna with carbon 14 arginine. The behavior of arginyl-tRNA synthetase (EC 6.1.1.19) in the presence of the arginine biosynthetic precursors, argininosuccinate, ornithine and citrulline, was studied in several E. coli K12 strains and in E. coli W. The results of kinetic measure...

Urban, C.; Wang, Y.; Rodríguez-Fernández, J.; García, Rúl.; Herranz, M.Ángeles.; Alcamí, M.; Martín, N.; Martín, F.; Gallego, Jé.M.; Miranda, R.; Otero, R., 2013: Charge transfer-assisted self-limited decyanation reaction of TCNQ-type electron acceptors on Cu(100). TCNQ derivatives adsorbed on a metal surface undergo a self-limited decyanation reaction that only affects two out of the four cyano groups in the molecule. Combined Scanning Tunneling Microscopy/X-ray Photoelectron Spectroscopy experiments and De...

Chulanova, E.A.; Pritchina, E.A.; Malaspina, L.A.; Grabowsky, S.; Mostaghimi, F.; Beckmann, J.; Bagryanskaya, I.Yu.; Shakhova, M.V.; Konstantinova, L.S.; Rakitin, O.A.; Gritsan, N.P.; Zibarev, A.V., 2016: New Charge-Transfer Complexes with 1,2,5-Thiadiazoles as Both Electron Acceptors and Donors Featuring an Unprecedented Addition Reaction. NlmCategory="UNASSIGNED">The design and synthesis of novel charge-transfer (CT) complexes are of interest for fundamental chemistry and applications to materials science. In addition to the recently described first CT complex with bot...

Teleb, S.M.; Refat, M.S., 2004: Spectroscopic studies on charge-transfer complexes formed in the reaction of ferric(III) acetylacetonate with sigma- and pi-acceptors. The reaction of ferric(III) acetylacetonate (donor), Fe(acac)3, with iodine as a sigma-acceptor and with other different pi-acceptors have been studied spectrophotometrically at room temperature in chloroform. The pi-acceptors used in this investi...

Refat, M.S.; El-Korashy, S.A.; El-Deen, I.M.; El-Sayed, S.M., 2011: Experimental and spectroscopic studies of charge transfer reaction between sulfasalazine antibiotic drug with different types of acceptors. The charge-transfer (CT) interactions between the electron donor sulfasalazine (SS) and the acceptors 2,3-dichloro-5,6-dicyano-1,4-benzoquinone (DDQ), p-chloranil (CHL), picric acid (PA) and iodine have been studied spectrophotometrically in CHCl(...

Cerná, J.; Rychlík, I.; Zemlicka, J.; Chládek, S., 1970: Substrate specificity of ribosomal peptidyl transferase. II. 2'(3')-O-aminoacyl nucleosides as acceptors of the peptide chain in the fragment reaction. Biochimica et Biophysica Acta 204(1): 203-209

Freist, W.; Sternbach, H.; Cramer, F., 1989: Arginyl transfer rna synthetase from yeast discrimination between 20 amino acids in aminoacylation of arginine transfer rna c c a and arginine transfer rna c c a 3' amine. For discrimination between arginine and 19 other amino acids in aminoacylation of tRNAArg-C-C-A by arginyl-tRNA synthetase from baker's yeast, discrimination factors (D) have been determined from kcat and Km values. The lowest values were fou...

Fersht, A.R.; Gangloff, J.; Dirheimer, G., 1978: Reaction pathway and rate determining step in the amino acylation of arginine transfer rna catalyzed by the arginyl transfer rna synthetase from yeast. The arginyl-tRNA synthetase from Saccharomyces cerevisiae, which does not form an isolable aminoacyl adenylate complex or catalyze the pyrophosphate-exchange reaction in the absence of tRNA, is one of the strongest candidates for the concerted mec...