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D-aminoacyl-tRNA deacylase
This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. Cell growth inhibition by several d-amino acids can be explained by an in vivo production of d-aminoacyl-tRNA molecules. Escherichia coli and yeast cells express an enzyme, d-Tyr-tRNA(Tyr) deacylase, capable of recycling such d-aminoacyl-tRNA molecules into free tRNA and d-amino acid. Accordingly, upon inactivation of the genes of the above deacylases, the toxicity of d-amino acids increases. Orthologues of the deacylase are found in many cells [1].The D-aminoacyl-tRNA deacylase (DTD) enzyme is homodimeric with two active sites located at the dimeric interface. Each active site carries an invariant Gly-cisPro dipeptide motif in each monomer. The interaction between the dipeptide motifs from each monomer ensures substrate stereospecificity. This family also includes a subclass of DTDs which is present in Chordata and harbors a Gly-transPro motif. The cis to trans switch is the key to Animal DTDs (ATD) gaining of L-chiral selectivity. This 'gain of function' through relaxation of substrate chiral specificity underlies ATD's capability of correcting the error in tRNA selection [2]. [1]. 11568181. Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A. representative of a new class of tRNA-dependent hydrolases.. Ferri-Fioni ML, Schmitt E, Soutourina J, Plateau P, Mechulam Y,. Blanquet S;. J Biol Chem 2001;276:47285-47290.. [2]. 29410408. A chiral selectivity relaxed paralog of DTD for proofreading. tRNA mischarging in Animalia.. Kuncha SK, Mazeed M, Singh R, Kattula B, Routh SB,. Sankaranarayanan R;. Nat Commun. 2018;9:511. (from Pfam)
D-aminoacyl-tRNA deacylase hydrolyzes D-aminoacyl-tRNA into D-amino acids and free tRNA which may be a defense mechanism against harmful effects of incorporating D-amino acids
This homodimeric enzyme, D-aminoacyl-tRNA deacylase, appears able to cleave any D-amino acid (and glycine, which does not have distinct D/L forms) from mis-charged tRNA molecules. The old name D-tyrosyl-tRNA(Tyr) deacylase reflects characterization with respect to D-Tyr on tRNA(Tyr) as established in the literature, but substrate specificity seems much broader.
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