Order of substrate binding to tyrosyl‐tRNA synthetase of Escherichia coli B

No abstract is available for this paper.

• Publication year

  1971

• Venue

  FEBS Letters

• Publication date

  1971-03-05

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/0014-5793(71)80224-7PMID 11945656
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• References

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• References

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• Acetylation of acetyl-CoA synthetase from Mycobacterium tuberculosis leads to specific inactivation of the adenylation reaction.

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• Kinetic mechanism of threonyl-tRNA synthetase from human placenta.

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• Thermodynamic Analysis Reveals a Temperature-dependent Change in the Catalytic Mechanism of Bacillus stearothermophilus Tyrosyl-tRNA Synthetase*

  2009cites this paper
• Activation of d-Tyrosine by Bacillus stearothermophilus Tyrosyl-tRNA Synthetase

  2008cites this paper
• Aminoacyl-tRNA Synthetases: Some Recent Results and Achievements

  2006cites this paper
• The catalytic mechanism of glutamyl-tRNA synthetase of Escherichia coli. A steady-state kinetic investigation.

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• Author Index to Volume 13

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• Master author index

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• Proteins: Structure, Function, and Engineering

  1995cites this paper
• Aminoacyl-tRNA Synthetases: Occurrence, Structure, and Function

  1995cites this paper
• A family of RNA-binding enzymes. the aminoacyl-tRNA synthetases.

  1995cites this paper
• Possible control of transcript levels by chlorophyll precursors in Chlamydomonas.

  1988cites this paper
• Tyrosyl-tRNA synthetase from baker's yeast. Order of substrate addition, discrimination of 20 amino acids in aminoacylation of tRNATyr-C-C-A and tRNATyr-C-C-A(3'NH2).

  1988cites this paper
• Use of the inhibition of enzymatic antioxidant systems in order to evaluate their physiological importance.

  1988cites this paper
• Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. Study of the interactions with its substrates.

  1979cites this paper
• The 32PPi—ATP isotope‐exchange reaction catalyzed by the yeast valyl‐tRNA synthetase Order of substrate binding and effect of tRNA

  1979cites this paper
• Influence of Magnesium on the Steady‐State‐Derived Order of Substrate Addition and Product Release in tRNA Trp Aminoacylation by Beef Pancreas Tryptophan: tRNA Ligase

  1978cites this paper
• Influence of magnesium on the steady-state-derived order of substrate addition and product release in tRNATrp aminoacylation by beef pancreas tryptophan: tRNA ligase: significance of the deduced mechanism.

  1978cites this paper
• ATP-analogues as substrates for the leucyl-tRNA synthetase from Escherichia coli MRE 600.

  1976cites this paper
• Kinetic techniques for the investigation of amino acid: tRNA ligases (aminoacyl-tRNA synthetases, amino acid activating enzymes).

  1974cites this paper
• The effect of adenosine analogues on the ATP-pyrophosphate exchange reaction catalysed by methionyl-tRNA synthetase.

  1974cites this paper
• Human tryptophanyl transfer ribonucleic acid synthetase. Comparison of the kinetic mechanism to that of the Escherichia coli tryptophanyl transfer ribonucleic acid synthetase.

  1974cites this paper
• Aminoacyl-tRNA synthetases: sone recent results and achievements.

  1974cites this paper
• Beef pancreas tryptophanyl-tRNA synthetase. Order of substrate binding in ATP-(32-P)-pyrophosphate exchange reaction.

  1974cites this paper
• Studies on the interaction of tyrosyl-tRNA synthetase from Escherichia coli K12 with tyrosine and with tyrosyl-AMP.

  1973cites this paper
• Acylation of Escherichia coli tRNAtrp with 5-methyltryptophan by E. coli tryptophanyl-tRNA ligase.

  1973cites this paper
• CHAPTER 3 – Inhibitors of Amino Acid Activation

  1973cites this paper
• The mechanism of aminoacylation of transfer RNA.

  1972cites this paper
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  1972cites this paper
• Substrate-derived reversible and irreversible inhibitors of the multi-enzyme I of gramicidin S biosynthesis.

  1972cites this paper
• Phenylalanyl transfer ribonucleic acid synthetase from Escherichia coli. Reaction parameters and order of substrate addition.

  1971cites this paper
• Phenylalanyl transfer ribonucleic acid synthetase from Escherichia coli. Analysis of the adenosine triphosphate binding site.

  1971cites this paper