Disease relevance of O-Methyltyrosine

• When introduced into E. coli, this pair leads to the in vivo incorporation of the synthetic amino acid O-methyl-l-tyrosine into protein in response to an amber nonsense codon [1].
• Examinations of the radiation-absorbed dose by O-[11C]methyl-L-tyrosine and the acute toxicity and mutagenicity of O-methyl-L-tyrosine showed suitability of the tracer for clinical use [2].

High impact information on O-Methyltyrosine

• Frameshift suppression with L-homoglutamine (hGln) does not significantly affect protein yields or cell growth rates and is mutually orthogonal with amber suppression, permitting the simultaneous incorporation of two unnatural amino acids, hGln and O-methyl-L-tyrosine, at distinct positions within myoglobin [3].
• Structure-based design of mutant Methanococcus jannaschii tyrosyl-tRNA synthetase for incorporation of O-methyl-L-tyrosine [4].
• Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for O-methyl-L-tyrosine [5].
• Two model membranes have been used to study the permeability changes induced by iturin A and O-methyltyrosine iturin A [6].
• An AM-toxin analog, cyclotetradepsipeptide, containing an O-methyl-L-tyrosine residue in place of an L-2-amino-5-arylpentanoic acid residue in AM-toxins has been prepared by a conventional method [7].

References