Stereospecificity of the Escherichia coli valyl-RNA synthetase in the ATP-32PPi exchange reaction

Owens, Sally; Bell, Fred E.

doi:10.1016/0022-2836(68)90137-x

Cited by 19 publications

(7 citation statements)

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“…The same extent of tRNA Tyr aminoacylation could be reached with the L ‐ and the D ‐enantiomers of the amino acid [30,31]. D ‐Valine binding to valyl‐tRNA Val synthetase was reported by Owens and Bell [32,33]. In the work of Soutourina et al, production of D ‐Asp‐tRNA Asp and D ‐Trp‐tRNA Trp by aspartyl‐tRNA synthetase and tryptophanyl‐tRNA synthetase, respectively, was established in vitro [34].…”

Section: The Problem Of D/l‐amino Acid Discriminationsupporting

confidence: 54%

D‐Amino acids and D‐Tyr‐tRNA^Tyr deacylase: stereospecificity of the translation machine revisited

et al. 2003

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Until 30 years ago, it had been considered that D-amino acids were excluded from living systems except for D-amino acids in the cell wall of microorganisms. However, D-amino acids, in the form of free amino acids, peptides and proteins, were recently detected in various living organisms from bacteria to mammals. The extensive distribution of bio-functional D-amino acids challenges the current concept of protein synthesis: more attention should be paid to the stereospeci¢city of the translation machine. Besides aminoacyl-tRNA synthetases, elongation factor Tu and some other mechanisms, D-TyrtRNA Tyr deacylases provide a novel checkpoint since they speci¢cally recycle misaminoacylated D-Tyr-tRNA Tyr and some other D-aminoacyl-tRNAs. Their unique structure represents a new class of tRNA-dependent hydrolase. These unexpected ¢nd-ings have far-reaching implications for our understanding of protein synthesis and its origin.

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Section: The Problem Of D/l‐amino Acid Discriminationsupporting

confidence: 54%

D‐Amino acids and D‐Tyr‐tRNA^Tyr deacylase: stereospecificity of the translation machine revisited

et al. 2003

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“…In this context it is interesting to consider the investigations of Owens and Bell [2,3] with valyltRNA synthetase from Escherichia coli. These authors were concerned with the stereospecificity of this enzyme towards substrates and substrate analogues.…”

Section: Stereospecificity Of Bindingmentioning

confidence: 99%

Influence of Side‐Chain Structure of Aliphatic Amino Acids on Binding to Isoleucyl‐tRNA Synthetase from Escherichia coli MRE 600

Floßdorf

Prätorius

Kula

1976

European Journal of Biochemistry

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The binding of 10 isomeric a-amino-heptanoic acids, of two isomeric a-amino-octanoic acids, of isoleucinol and valinol, and of various a-hydroxy acids to isoleucyl-tRNA synthetase from Escherichiu coli MRE 600 has been investigated by an ultracentrifuge method. It was found that the enzyme requires a primary amino group together with a not-too-small side chain as prerequisites for ligand recognition. Though the enzyme is absolutely specific for the L isomers, it is fairly tolerant against replacement of the carboxyl group of the natural substrate by more or less hydrophobic substituents. These findings can be explained in terms of Ogston's three-point-attachment model, if it is additionally assumed that there is no further space available in the binding region normally occupied by the cc-hydrogen atom to accept other substituents which are as bulky as the carboxyl moiety.Similarly, the architecture of the binding region of the aliphatic side chain is discussed. Our measurements show that the free energy of binding strongly depends on the size and the structure of the remainder of the molecule. None of the isoleucine analogues employed is bound as tightly as the natural substrate itself, but there is a clear preference for side chains branched at the P-carbon atom. The functioning of the side-chain recognition site is best understood by imagining a two-finger glove, of which one finger is tailored to a methyl and the other to an ethyl group. Both these fingers, together with the binding region for the glycine moiety and a steric barrier against a fourth substituent bulkier than hydrogen, are responsible for a high steric specificity towards the one side chain over its Cb epimer.

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“…It causes the cleavage of bond formed between D-amino acids and tRNA thus making tRNA available to coalesce with L-amino acids (Wydau et al, 2009 ; Zheng et al, 2009 ). It was first reported in Escherichia coli and Bacillus subtilis that tRNA molecules are charged with D-tyrosine in the presence of Tyrosyl-tRNA synthetase (Owens and Bell, 1968 ). Later, a report of D-Valine, D-Aspartate, and D-Tryptophan coupling with their respective tRNA was published by different scientific groups (Soutourina et al, 2000 ).…”

Section: Introductionmentioning

confidence: 99%

Recent Updates on DTD (D-Tyr-tRNATyr Deacylase): An Enzyme Essential for Fidelity and Quality of Protein Synthesis

Bhatt

Soni

Sharma

2016

Front. Cell Dev. Biol.

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During protein synthesis, there are several checkpoints in the cell to ensure that the information encoded within genetic material is decoded correctly. Charging of tRNA with its cognate amino acid is one of the important steps in protein synthesis and is carried out by aminoacyl-tRNA synthetase (aaRS) with great accuracy. However, due to presence of D-amino acids in the cell, sometimes aaRS charges tRNA with D-amino acids resulting in the hampering of protein translational process, which is lethal to the cell. Every species has some mechanism in order to prevent the formation of D-amino acid-tRNA complex, for instance DTD (D-Tyr-tRNA deacylase) is an enzyme responsible for the cleavage of ester bond formed between D-amino acid and tRNA leading to error free translation process. In this review, structure, function, and enzymatic mechanism of DTD are discussed. The role of DTD as a drug target is also considered.

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Stereospecificity of the Escherichia coli valyl-RNA synthetase in the ATP-32PPi exchange reaction

Cited by 19 publications

References 5 publications

D‐Amino acids and D‐Tyr‐tRNA^Tyr deacylase: stereospecificity of the translation machine revisited

D‐Amino acids and D‐Tyr‐tRNA^Tyr deacylase: stereospecificity of the translation machine revisited

Influence of Side‐Chain Structure of Aliphatic Amino Acids on Binding to Isoleucyl‐tRNA Synthetase from Escherichia coli MRE 600

Recent Updates on DTD (D-Tyr-tRNATyr Deacylase): An Enzyme Essential for Fidelity and Quality of Protein Synthesis

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Stereospecificity of the Escherichia coli valyl-RNA synthetase in the ATP-32PPi exchange reaction

Cited by 19 publications

References 5 publications

D‐Amino acids and D‐Tyr‐tRNATyr deacylase: stereospecificity of the translation machine revisited

D‐Amino acids and D‐Tyr‐tRNATyr deacylase: stereospecificity of the translation machine revisited

Influence of Side‐Chain Structure of Aliphatic Amino Acids on Binding to Isoleucyl‐tRNA Synthetase from Escherichia coli MRE 600

Recent Updates on DTD (D-Tyr-tRNATyr Deacylase): An Enzyme Essential for Fidelity and Quality of Protein Synthesis

Contact Info

Product

Resources

About

D‐Amino acids and D‐Tyr‐tRNA^Tyr deacylase: stereospecificity of the translation machine revisited

D‐Amino acids and D‐Tyr‐tRNA^Tyr deacylase: stereospecificity of the translation machine revisited