EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   3.1.1.96 | more |
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 |
Escherichia coli |
? |
- |
? |
| 3.1.1.96 | more |
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 |
Saccharomyces cerevisiae |
? |
- |
? |
| 3.1.1.96 | D-aminoacyl-tRNA + H2O |
- |
Escherichia coli |
D-amino acid + tRNA |
- |
? |
| 3.1.1.96 | D-aminoacyl-tRNA + H2O |
- |
Azotobacter vinelandii |
D-amino acid + tRNA |
- |
? |
| 3.1.1.96 | D-aminoacyl-tRNA + H2O |
- |
Haemophilus influenzae |
D-amino acid + tRNA |
- |
? |
| 3.1.1.96 | D-aminoacyl-tRNA + H2O |
the enzyme recognize almost all D-aminoacyl-tRNAs instead of only D-Tyr-tRNATyr |
Escherichia coli |
D-amino acid + tRNA |
- |
? |
| 3.1.1.96 | D-aspartyl-tRNAAsp + H2O |
initial rate of hydrolysis is very close to that obtained with D-tyrosyl-tRNATyr |
Arabidopsis thaliana |
D-aspartate + tRNAAsp |
- |
? |
| 3.1.1.96 | D-aspartyl-tRNAAsp + H2O |
no activity with L-aspartyl-tRNAAsp |
Escherichia coli |
D-aspartate + tRNAAsp |
- |
? |
| 3.1.1.96 | D-tryptophanyl-tRNATrp + H2O |
- |
Escherichia coli |
D-tryptophan + tRNATrp |
- |
? |
| 3.1.1.96 | D-Tyr-tRNA + H2O |
- |
Escherichia coli |
D-Tyr + tRNA |
- |
? |
