2 edition of Some properties of lysyl ribonucleic acid synthetase from Escherichia Coli. found in the catalog.
Some properties of lysyl ribonucleic acid synthetase from Escherichia Coli.
Written in English
Bibliography: p. 20.
|LC Classifications||QP601 .W16|
|The Physical Object|
|Number of Pages||20|
|LC Control Number||70471162|
The molecular weight of l‐phenylalanyl‐tRNA synthetase was redetermined. A new value of was obtained by high‐speed analytical ultracentrifugation and Sephadex G‐ gel chromatography. The. Samuel CE, Rabinowitz JC. Effect of formylation on the chromatographic behavior of methionyl transfer ribonucleic acid. Anal Biochem. May; 47 (1)– [Google Scholar] Schofield P. Isolation and some properties of methionine transfer ribonucleic acid from Escherichia coli. Biochemistry. Apr 14; 9 (8)–
The heat‐inducible lysyl‐tRNA synthetase from Escherichia coli (LysU; EC6/1/1/) converts ATP to diadenosine tri‐ and tetraphosphates (Ap 3 A/Ap 4 A) in the presence of l ‐lysine/Mg 2+ /Zn 2+.To understand LysU in more detail, 26 mutants were prepared: six of E, four of R and sixteen mutants by alanine‐scanning of the inner shell/motif 2 loop. This work was supported by Grant GM from the National Institutes of Health and by a Biomical Research Support grant (2-SRR) for the video densitometer. REFERENCES ARCHIBALD, E. T., and WILLIAMS, L. S. (). Regulation of methio- nyl-transfer ribonucleic acid synthetase formation in Escherichia coli and Salmonella typhimurium. J.
Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase Article (PDF Available) in Biochemical Journal (2) September with 9 Reads. Prolyl transfer ribonucleic acid synthetase of Escherichia coli. J Biol Chem – Analysis of the amino acid binding to the proline transfer ribonucleic acid synthetase of Escherichia coli. J Biol Chem – Partial purification and some properties of Δ 1-pyrrolinecarboxylate reductase from Escherichia coli.
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Eur J Biochem. Jul;5(2) Some properties of lysyl ribonucleic acid synthetase from Escherichia coli. Waldenström J. PMID: Cited by: 1. Eur J Biochem. Feb;3(4) Purification and some properties of lysyl ribonucleic acid synthetase from Escherichia coli.
Waldenström by: Tryptophanyl transfer ribonucleic acid synthetase of Escherichia coli. Purification of the enzyme and of tryptrophan transfer ribonucleic acid. Joseph DR, Muench KH. J Biol Chem, (24), 01 Dec Cited by: 51 articles | PMID: Cited by: Lysyl transfer ribonucleic acid synthetase (L-lysine: tRNA ligase (AMP), EC ) was pursed to a state of apparent homogeneity from bakers’ yeast.
For each of two different preparation procedures, a to fold purika- tion of the enzyme was obtained, and the final purification. Purification and some Properties of Lysyl Ribonucleic Acid Synthetase from Escherichia coli. European Journal of Biochemistry3 (4), DOI: / by: Two modes of metabolic regulation of lysyl-transfer ribonucleic acid synthetase in Escherichia coli K J Bacteriol.
Aug; (2)– [PMC free article] Hirshfield IN, Yeh FM. An in vivo effect of the metabolites L-alanine and glycyl-L-leucine on the properties of the lysyl-tRNA synthetase from Escherichia coli K II. Neidhardt FC () Multiple forms of lysyl-transfer ribonucleic acid synthetase in Escherichia toll.
J Bacteriol5 Hirshfield IN, Yeh FM, Sawyer LE () Metabolites influence control of lysine transfer ribonucleic acid synthetase formation in Escherichia toll K The lysyl-RNA synthetase from E. coli recognized about 70% of the lysine specific chains of yeast transferRNA, while the yeast enzyme recognized about 80% of the lysine specific chains of E.
coli. Transient rates of synthesis of five aminoacyl transfer ribonucleic acid synthetases during a shift up of Escherichia coli Article (PDF Available) in Journal of Bacteriology (2) March. Lizin-tRNK ligaza (EClizil-tRNK sintetaza, lizil-transfer ribonukleat sintetaza, lizil-transfer RNK sintetaza, L-lizin-transfer RNK ligaza, lizin-tRNK sintetaza, lizinska translaza) je enzim sa sistematskim imenom L-lizin:tRNKLis ligaza (formira AMP).
Ovaj enzim katalizuje sledeću hemijsku reakciju. ATP + L-lizin + tRNK Lys ⇌ AMP + difosfat + L-lizil-tRNK Lys. Seryl transfer ribonucleic acid synthetase of Escherichia coli B.
Enzyme-substrate interactions. Biochemistry12 (13), DOI: /bia Daniel V. Santi and Peter V. Danenberg. Phenylalanyl transfer ribonucleic acid synthetase from Escherichia coli.
Analysis of the phenylalanine binding site. Multiple forms of lysyl-transfer ribonucleic acid synthetase in Escherichia coli. J Bacteriol. Apr; (1)– [Europe PMC free article] [Google Scholar] Hirshfield IN, Tenreiro R, Vanbogelen RA, Neidhardt FC.
Escherichia coli K lysyl-tRNA synthetase mutant with a novel reversion pattern. J Bacteriol. May; (2)– Biochemistry All Publications/Website.
OR SEARCH CITATIONS. The crystal structure of the lysyl-tRNA synthetase (LysU) from Escherichia coli Silvia Onesti l*t, Andrew D Miller2 and Peter Brick1 1Blackett Laboratory and 2Department of Chemistry, Imperial College, London SW7 2BZ, UK Background: Lysyl-tRNA synthetase catalyzes the attachment of the amino acid lysine to the cognate tRNA.
The substrate specificity of a purified lysyl-ribonucleic acid synthetase of Escherichia coli has been studied by determining the effects of a group of lysine analogs upon (a) the enzymic transfer of lysine C to soluble ribonucleic acid and (b) lysine-dependent ATP-pyrophosphate relatively high levels, 4-oxalysine, 2,6-diaminohexynoic acid, and transdehydrolysine (but.
Lysyl-transfer ribonucleic acid (tRNA) synthetase activity was compared in three independently isolated Escherichia coli K mutants of the enzyme S-adenosyl-L-methionine synthetase (metK mutants) and their isogenic parents. In all three cases the activity of the lysyl-tRNA synthetase was elevated two- to fourfold in the mutant strains.
Purification and some Properties of Leucyl-tRNA Synthetase from Bacillus stearothermophilus. European Journal of Biochemistry10 (2), DOI: /jtbx. Yaniv, F. Gros. Studies on valyl-tRNA synthetase and tRNAVal from Escherichia coli. Purification and some properties of lysyl ribonucleic acid synthetase from Escherichia coli.
Waldenström J Eur J Biochem, 3(4), 01 Feb The induction of the inducible lysyl-tRNA synthetase, LysU, and the inducible lysine and arginine decarboxylases of Escherichia coli K grown in AC broth to a pH of or less is temperature.
Waldenström J. Purification and some properties of lysyl ribonucleic acid synthetase from Escherichia coli. Eur J Biochem. Feb; 3 (4)– Kendall FE. STUDIES ON SERUM PROTEINS. IDENTIFICATION OF A SINGLE SERUM GLOBULIN BY IMMUNOLOGICAL MEANS. The 3 substrates of this enzyme are ATP, L-lysine, and tRNA(Lys), whereas its 3 products are AMP, diphosphate, and L-lysyl-tRNA(Lys).
This enzyme participates in 3 metabolic pathways: lysine biosynthesis, aminoacyl-trna biosynthesis, and amyotrophic lateral sclerosis (als).Tyr of the Escherichia coli asparaginyl-tRNA synthetase, an amino acid in a C-terminal conserved motif, is involved in ATP binding.
FEBS Lett. – 7.Chlumecka V, Von Tigerstrom M, D'Obrenan P, Smith CJ (). “Purification and properties of lysyl transfer ribonucleic acid synthetase from bakers' yeast”. J. Biol. Chem. (20): –8. PMID Lagerkvist U, Rymo L, Lindqvist O, Andersson E ().
“Some properties of crystals of lysine transfer ribonucleic acid ligase from.