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D-aminoacyl-tRNA + H2O
D-amino acid + tRNA
D-aspartyl-tRNAAsp + H2O
D-aspartate + tRNAAsp
D-tryptophanyl-tRNATrp + H2O
D-tryptophan + tRNATrp
-
-
-
?
D-Tyr-tRNA + H2O
D-Tyr + tRNA
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
Gly-tRNAAla + H2O
Gly + tRNAAla
additional information
?
-
D-aminoacyl-tRNA + H2O
D-amino acid + tRNA
-
-
-
-
?
D-aminoacyl-tRNA + H2O
D-amino acid + tRNA
-
-
-
-
?
D-aminoacyl-tRNA + H2O
D-amino acid + tRNA
the enzyme recognize almost all D-aminoacyl-tRNAs instead of only D-Tyr-tRNATyr
-
-
?
D-aminoacyl-tRNA + H2O
D-amino acid + tRNA
-
-
-
?
D-aspartyl-tRNAAsp + H2O
D-aspartate + tRNAAsp
initial rate of hydrolysis is very close to that obtained with D-tyrosyl-tRNATyr
-
-
?
D-aspartyl-tRNAAsp + H2O
D-aspartate + tRNAAsp
no activity with L-aspartyl-tRNAAsp
-
-
?
D-Tyr-tRNA + H2O
D-Tyr + tRNA
-
-
-
-
?
D-Tyr-tRNA + H2O
D-Tyr + tRNA
-
-
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
no activity with L-tyrosyl-tRNATyr and diacetyl-L-Lys-tRNALys
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
-
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the enzyme can recycle misaminoacylated D-Tyr-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
-
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the enzyme is responsible for resistance to the non-canonical amino acid D-tyrosine
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
-
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the enzyme is responsible for resistance to the non-canonical amino acid D-tyrosine
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
-
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
no activity with L-tyrosyl-tRNATyr, N-acetyl-L-tyrosyl-tRNATyr and N-acetyl-D-tyrosyl-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the deacylase does not hydrolyze L-Trp-tRNATrp at a significant rate
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the enzyme can recycle misaminoacylated D-Tyr-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the initial rate of D-Tyr-tRNATyr deacylation is at least 200fold higher than that of L-Tyr-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the enzyme can recycle misaminoacylated D-Tyr-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the initial rate of D-Tyr-tRNATyr deacylation is at least 200fold higher than that of L-Tyr-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
-
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the enzyme can recycle misaminoacylated D-Tyr-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
-
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
the enzyme can recycle misaminoacylated D-Tyr-tRNATyr
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
-
-
-
?
D-tyrosyl-tRNATyr + H2O
D-tyrosine + tRNATyr
-
-
-
?
Gly-tRNAAla + H2O
Gly + tRNAAla
-
-
-
-
?
Gly-tRNAAla + H2O
Gly + tRNAAla
-
the enzyme has a crucial role in preventing the accumulation of mischarged Gly-tRNAAla species. The enzyme effectively decouples glycine mischarged on tRNAAla, key cellular role as a glycine deacylator
-
-
?
Gly-tRNAAla + H2O
Gly + tRNAAla
-
the enzyme hydrolyzes D-amino acids mistakenly attached to tRNAs and eliminates glycine that has been erroneously coupled to tRNAAla
-
-
?
additional information
?
-
comparison of the growth of wild-type and deletion mutant strains indicates protection against the toxicity of D-Trp, D-Asp, D-Ser, and D-Gln afforded by the D-Tyr-tRNATyr deacylase gene. The effect of the other D-amino acids on growth is similar for the wild-type and deletion mutant strains
-
-
?
additional information
?
-
-
comparison of the growth of wild-type and deletion mutant strains indicates protection against the toxicity of D-Trp, D-Asp, D-Ser, and D-Gln afforded by the D-Tyr-tRNATyr deacylase gene. The effect of the other D-amino acids on growth is similar for the wild-type and deletion mutant strains
-
-
?
additional information
?
-
comparison of the growth of wild-type and deletion mutant strains indicates protection against toxicity by D-leucine afforded by the D-Tyr-tRNATyr deacylase gene. Full inhibition of the growth of the Ddtd1 strain is reached at 0.1 mM D-tyrosine. With the DTD1 strain, identical growth inhibition required 0.3 mM D-amino acid. The effect of the other D-amino acids on growth is similar for the wild-type and deletion mutant strains
-
-
?
additional information
?
-
-
comparison of the growth of wild-type and deletion mutant strains indicates protection against toxicity by D-leucine afforded by the D-Tyr-tRNATyr deacylase gene. Full inhibition of the growth of the Ddtd1 strain is reached at 0.1 mM D-tyrosine. With the DTD1 strain, identical growth inhibition required 0.3 mM D-amino acid. The effect of the other D-amino acids on growth is similar for the wild-type and deletion mutant strains
-
-
?
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malfunction
inactivation of the corresponding gene (dtd3) renders the growth of Synechocystis sp. hypersensitive to the presence of D-tyrosine
malfunction
-
inactivation of the gene dtd increases the toxicity of several D-amino acids including D-tyrosine, D-tryptophan, and D-aspartic acid
malfunction
-
DTD knockout in AlaRS editing-defective background causes pronounced toxicity in Escherichia coli even at low-glycine levels which is alleviated by alanine supplementation
malfunction
-
inactivation of the gene dtd increases the toxicity of several D-amino acids including D-tyrosine, D-tryptophan, and D-aspartic acid
-
metabolism
-
the enzym effectively decouples glycine mischarged on tRNAAla, key cellular role as a glycine deacylator
metabolism
-
the enzyme hydrolyzes D-amino acids mistakenly attached to tRNAs and eliminates glycine that has been erroneously coupled to tRNAAla
metabolism
the enzyme is responsible for resistance to the non-canonical amino acid D-tyrosine
metabolism
-
the enzyme is responsible for resistance to the non-canonical amino acid D-tyrosine
-
physiological function
-
the enzyme contributes to the resistance of the cell to D-amino acids by deacylating D-aminoacyl tRNAs at the nuclear pore
physiological function
-
the enzyme contributes to the resistance of the cell to D-amino acids by deacylating D-aminoacyl tRNAs at the nuclear pore
physiological function
the enzyme helps maintain the fidelity of protein synthesis
physiological function
-
the enzyme helps maintain the fidelity of protein synthesis
-
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Rigden, D.J.
Archaea recruited D-Tyr-tRNATyr deacylase for editing in Thr-tRNA synthetase
RNA
10
1845-1851
2004
Azotobacter vinelandii, Escherichia coli, Haemophilus influenzae (P44814)
brenda
Zheng, G.; Liu, W.; Gong, Y.; Yang, H.; Yin, B.; Zhu, J.; Xie, Y.; Peng, X.; Qiang, B.; Yuan, J.
Human D-Tyr-tRNA(Tyr) deacylase contributes to the resistance of the cell to D-amino acids
Biochem. J.
417
85-94
2009
Homo sapiens, Mus musculus
brenda
Soutourina, J.; Plateau, P.; Delort, F.; Peirotes, A.; Blanquet, S.
Functional characterization of the D-Tyr-tRNATyr deacylase from Escherichia coli
J. Biol. Chem.
274
19109-19114
1999
Escherichia coli (P0A6M4), Escherichia coli
brenda
Soutourina, J.; Plateau, P.; Blanquet, S.
Metabolism of D-aminoacyl-tRNAs in Escherichia coli and Saccharomyces cerevisiae cells
J. Biol. Chem.
275
32535-32542
2000
Escherichia coli (P0A6M4), Escherichia coli, Saccharomyces cerevisiae (Q07648), Saccharomyces cerevisiae
brenda
Ferri-Fioni, M.L.; Schmitt, E.; Soutourina, J.; Plateau, P.; Mechulam, Y.; Blanquet, S.
Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases
J. Biol. Chem.
276
47285-47290
2001
Escherichia coli (P0A6M4), Escherichia coli
brenda
Lim, K.; Tempczyk, A.; Bonander, N.; Toedt, J.; Howard, A.; Eisenstein, E.; Herzberg, O.
A catalytic mechanism for D-Tyr-tRNATyr deacylase based on the crystal structure of Hemophilus influenzae HI0670
J. Biol. Chem.
278
13496-13502
2003
Haemophilus influenzae (P44814), Haemophilus influenzae, Haemophilus influenzae DSM 11121 (P44814)
brenda
Ferri-Fioni, M.L.; Fromant, M.; Bouin, A.P.; Aubard, C.; Lazennec, C.; Plateau, P.; Blanquet, S.
Identification in archaea of a novel D-Tyr-tRNATyr deacylase
J. Biol. Chem.
281
27575-27585
2006
Archaeoglobus fulgidus (O29630), Archaeoglobus fulgidus, Saccharolobus solfataricus (Q97WI2), Saccharolobus solfataricus, Pyrococcus abyssi (Q9V2R8), Pyrococcus abyssi, Saccharolobus solfataricus P2 (Q97WI2), Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 (Q9V2R8)
brenda
Wydau, S.; van der Rest, G.; Aubard, C.; Plateau, P.; Blanquet, S.
Widespread distribution of cell defense against D-aminoacyl-tRNAs
J. Biol. Chem.
284
14096-14104
2009
Synechocystis sp. (P73335), Synechocystis sp.
brenda
Wydau, S.; Ferri-Fioni, M.L.; Blanquet, S.; Plateau, P.
GEK1, a gene product of Arabidopsis thaliana involved in ethanol tolerance, is a D-aminoacyl-tRNA deacylase
Nucleic Acids Res.
35
930-938
2007
Arabidopsis thaliana (Q9ZPQ3), Arabidopsis thaliana
brenda
Yang, H.; Zheng, G.; Peng, X.; Qiang, B.; Yuan, J.
D-Amino acids and D-Tyr-tRNA(Tyr) deacylase: stereospecificity of the translation machine revisited
FEBS Lett.
552
95-98
2003
Escherichia coli (P0A6M4)
brenda
Soutourina, O.; Soutourina, J.; Blanquet, S.; Plateau, P.
Formation of D-tyrosyl-tRNATyr accounts for the toxicity of D-tyrosine toward Escherichia coli
J. Biol. Chem.
279
42560-42565
2004
Escherichia coli, Escherichia coli K-37
brenda
Rybak, M.; Kovalenko, O.; Kryklyvyi, I.; Tukalo, M.
Cloning, expression and purification of D-Tyr-tRNATyr-deacylase from Thermus thermophilus
Biopolym. Cell
31
179-186
2015
Thermus thermophilus (Q5SJQ9), Thermus thermophilus (Q72K35)
-
brenda
Pawar, K.I.; Suma, K.; Seenivasan, A.; Kuncha, S.K.; Routh, S.B.; Kruparani, S.P.; Sankaranarayanan, R.
Role of D-aminoacyl-tRNA deacylase beyond chiral proofreading as a cellular defense against glycine mischarging by AlaRS
eLife
6
e24001
2017
Escherichia coli
brenda
Geraskina, N.; Butov, I.; Yomantas, Y.; Stoynova, N.
The dtd gene from Bacillus amyloliquefaciens encodes a putative D-tyrosyl-tRNATyr deacylase and is a selectable marker for Bacillus subtilis
Microbiol. Res.
171
90-96
2015
Bacillus amyloliquefaciens (A0A023W421), Bacillus amyloliquefaciens, Bacillus amyloliquefaciens A50 (A0A023W421)
brenda
Calendar, R.
D-Tyrosyl-tRNA deacylase A new function
Trends Biochem. Sci.
42
684-686
2017
Escherichia coli
brenda