The Enzyme Database

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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
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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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:e24001 (2017). [DOI] [PMID: 28362257]
[EC created 2014, modified 2019]

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