Aug 2, 2005

Selective inhibition of divergent seryl-tRNA synthetases by serine analogues

FEBS Letters
Dragana AhelIvana Weygand-Durasevic

Abstract

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.

  • References17
  • Citations11

Citations

Mentioned in this Paper

SARS2 gene
Bacterial Proteins
Phosphoserine
Alkalescens-Dispar Group
Carboxy-Terminal Amino Acid
Hydroxamate
Enzymes, antithrombotic
Amino Acids, I.V. solution additive
MT-TA gene
Triplet Codon-amino Acid Adaptor Activity

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