Aminoacyl-tRNA hydrolase
| aminoacyl-tRNA hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.1.29 | ||||||||
| CAS no. | 9054-98-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, an aminoacyl-tRNA hydrolase (EC 3.1.1.29) is an enzyme that catalyzes the chemical reaction
- N-Substituted aminoacyl-tRNA + H2O N-substituted amino acid + tRNA
Thus, the two substrates of this enzyme are N-Substituted aminoacyl-tRNA and H2O, whereas its two products are N-substituted amino acid and tRNA.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is aminoacyl-tRNA aminoacylhydrolase. Other names in common use include aminoacyl-transfer ribonucleate hydrolase, N-substituted aminoacyl transfer RNA hydrolase, and peptidyl-tRNA hydrolase.
Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1RYB, 1WN2, 1XTY, 2D3K, 2E1B, 2PTH, 2Z2I, 2Z2J, and 2Z2K.
References
- Jost JP, Bock RM (1969). "Enzymatic hydrolysis of N-substituted aminoacyl transfer ribonucleic acid in yeast". J. Biol. Chem. 244 (21): 5866–73. PMID 4981785.