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Seryl-tRNA synthetases (SerRSs) fall into two distinct evolutionary groups of enzymes, bacterial and methanogenic. These two types of SerRSs display only minimal sequence similarity, primarily within the class II conserved motifs, and possess distinct modes of tRNA(Ser) recognition. In order to determine whether the two types of SerRSs also differ in their recognition of the serine substrate, we compared the sensitivity of the representative methanogenic and bacterial-type SerRSs to serine hydroxamate and two previously unidentified inhibitors, serinamide and serine methyl ester. Our kinetic data showed selective inhibition of the methanogenic SerRS by serinamide, suggesting a lack of mechanistic uniformity in serine recognition between the evolutionarily distinct SerRSs.

Original publication

DOI

10.1016/j.febslet.2005.06.073

Type

Journal article

Journal

FEBS Lett

Publication Date

15/08/2005

Volume

579

Pages

4344 - 4348

Keywords

Amino Acid Sequence, Archaeal Proteins, Bacterial Proteins, Enzyme Inhibitors, Escherichia coli, Methanosarcina barkeri, Molecular Sequence Data, Phylogeny, Serine, Serine-tRNA Ligase, Substrate Specificity