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Chemical Compound Review:

AR-1G9206 [(2S)-2-amino-3-(4- hydroxyphenyl)propoxy]...

Synonyms: AC1L52Y3, AC1Q6S60, TYA, Tyrosinyl-5'-AMP, Adenylyl-tyrosine, ...

Grosse, F. et al., Kleeman, T.A. et al., Bedouelle, H. et al., Chow, C.M. et al., Kuratani, M. et al., et al.

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Disease relevance of Tyrosyl adenylate

However, many of the residues known to line the tyrosyl-adenylate-binding pocket of the Bacillus stearothermophilus enzyme can be aligned in the yeast sequence [1].
Point mutations in tyrS that prevent interaction between its product, tyrosyl-tRNA synthetase, and tRNA(Tyr) but do not alter the rate of formation of tyrosyl-adenylate abolished the toxicity [2].

High impact information on Tyrosyl adenylate

Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase [3].
Nine of fifteen amino acids known to be involved in the formation of the tyrosyl-adenylate complex in B. stearothermophilus are conserved across all of the organisms, whereas amino acids involved in the recognition of tRNATyr are not conserved [4].
The binding of tyrosinyl-5'-AMP to tyrosyl-tRNA synthetase (E.coli) [5].
The binding sites for tRNATyr and tyrosinyl-5'-AMP are independent of each other, the anticooperative mode of tRNA binding being preserved in the presence of tyrosinyl-5-AMP [5].
TyrRS has the "HIGH" and "KMSKS" motifs, which play essential roles in the formation of the tyrosyl-adenylate from tyrosine and ATP [6].

Analytical, diagnostic and therapeutic context of Tyrosyl adenylate

The binding between tyrosyl-tRNA synthetase (E.coli) and the alkylanalogue of the aminoacyladenylate, tyrosinyl-5'-AMP, has been investigated by fluorescence titrations and rapid mixing experiments [5].

References

Saccharomyces cerevisiae cytoplasmic tyrosyl-tRNA synthetase gene. Isolation by complementation of a mutant Escherichia coli suppressor tRNA defective in aminoacylation and sequence analysis. Chow, C.M., RajBhandary, U.L. J. Biol. Chem. (1993) [Pubmed]
Overproduction of tyrosyl-tRNA synthetase is toxic to Escherichia coli: a genetic analysis. Bedouelle, H., Guez, V., Vidal-Cros, A., Hermann, M. J. Bacteriol. (1990) [Pubmed]
Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase. Austin, J., First, E.A. J. Biol. Chem. (2002) [Pubmed]
Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine. Kleeman, T.A., Wei, D., Simpson, K.L., First, E.A. J. Biol. Chem. (1997) [Pubmed]
The binding of tyrosinyl-5'-AMP to tyrosyl-tRNA synthetase (E.coli). Grosse, F., Krauss, G., Kownatzki, R., Maass, G. Nucleic Acids Res. (1979) [Pubmed]
Crystal structures of tyrosyl-tRNA synthetases from Archaea. Kuratani, M., Sakai, H., Takahashi, M., Yanagisawa, T., Kobayashi, T., Murayama, K., Chen, L., Liu, Z.J., Wang, B.C., Kuroishi, C., Kuramitsu, S., Terada, T., Bessho, Y., Shirouzu, M., Sekine, S., Yokoyama, S. J. Mol. Biol. (2006) [Pubmed]

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