IUBMB Enzyme Nomenclature


Accepted name: D-aminoacyl-tRNA deacylase

Reaction: (1) a D-aminoacyl-tRNA + H2O = a D-amino acid + tRNA
(2) glycyl-tRNAAla + H2O = glycine + tRNAAla

Other name(s): Dtd2; D-Tyr-tRNA(Tyr) deacylase; D-Tyr-tRNATyr deacylase; D-tyrosyl-tRNATyr aminoacylhydrolase; dtdA (gene name)

Systematic name: D-aminoacyl-tRNA aminoacylhydrolase

Comments: The enzyme, found in all domains of life, can cleave mischarged glycyl-tRNAAla [5]. The enzyme from Escherichia coli can cleave D-tyrosyl-tRNATyr, D-aspartyl-tRNAAsp and D-tryptophanyl-tRNATrp [1]. Whereas the enzyme from the archaeon Pyrococcus abyssi is a zinc protein, the enzyme from Escherichia coli does not carry any zinc [2].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:


1. Soutourina, J., Plateau, P. and Blanquet, S. Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells. J. Biol. Chem. 275 (2000) 32535-32542. [PMID: 10918062]

2. Ferri-Fioni, M.L., Schmitt, E., Soutourina, J., Plateau, P., Mechulam, Y. and Blanquet, S. Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases. J. Biol. Chem. 276 (2001) 47285-47290. [PMID: 11568181]

3. Ferri-Fioni, M.L., Fromant, M., Bouin, A.P., Aubard, C., Lazennec, C., Plateau, P. and Blanquet, S. Identification in archaea of a novel D-Tyr-tRNATyr deacylase. J. Biol. Chem. 281 (2006) 27575-27585. [PMID: 16844682]

4. Wydau, S., Ferri-Fioni, M.L., Blanquet, S. and Plateau, P. GEK1, a gene product of Arabidopsis thaliana involved in ethanol tolerance, is a D-aminoacyl-tRNA deacylase. Nucleic Acids Res. 35 (2007) 930-938. [PMID: 17251192]

5. Pawar, K.I., Suma, K., Seenivasan, A., Kuncha, S.K., Routh, S.B., Kruparani, S.P. and Sankaranarayanan, R. Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a cellular defense against glycine mischarging by AlaRS. Elife 6 (2017) . [PMID: 28362257]

[EC created 2014, modified 2019]

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