Warning: The NCBI web site requires JavaScript to function. more...
An official website of the United States government
The .gov means it's official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you're on a federal government site.
The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.
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.
Filter your results:
Your browsing activity is empty.
Activity recording is turned off.
Turn recording back on