Structural highlights
Function
SYDND_PSEAE Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over tRNA(Asn). Reaction proceeds in two steps: aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).[1]
See Also
References
- ↑ Bernard D, Akochy PM, Beaulieu D, Lapointe J, Roy PH. Two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase from Pseudomonas aeruginosa are individually implicated in the recognition of tRNAAsn. J Bacteriol. 2006 Jan;188(1):269-74. PMID:16352843 doi:http://dx.doi.org/10.1128/JB.188.1.269-274.2006
