The Enzyme Database

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Accepted name: peptidyl-tRNA hydrolase
Reaction: N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA
Other name(s): aminoacyl-transfer ribonucleate hydrolase; N-substituted aminoacyl transfer RNA hydrolase; aminoacyl-tRNA hydrolase; PTH1 (gene name); PTH2 (gene name); pth (gene name); spoVC (gene name); PTRH1 (gene name); PTRH2 (gene name)
Systematic name: peptidyl-tRNA peptidylhydrolase
Comments: The enzyme acts on premature protein synthesis products that dissociate from stalled ribosomes, cleaving the peptidyl chains and restoring functionality to the tRNA. In most organisms mutants with limited Pth activity accumulate peptidyl-tRNAs, reducing the availability of uncharged tRNAs below the limit that is necessary for protein synthesis and impairing cell growth. Two distinct classes of the enzyme, Pth and Pth2, have been identified. While most enzymes can recognize and cleave N-acylated aminoacyl-tRNAs, they are not able to act on N-formyl-methionyl-tRNA.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9054-98-2
1.  Cuzin, F., Kretchmer, N., Greenberg, R.E., Hurwitz, R. and Chapeville, F. Enzymatic hydrolysis of N-substituted aminoacyl-tRNA. Proc. Natl. Acad. Sci. USA 58 (1967) 2079–2086. [DOI] [PMID: 4866985]
2.  Kossel, H. and RajBhandary, U.L. Studies on polynucleotides. LXXXVI. Enzymic hydrolysis of N-acylaminoacyl-transfer RNA. J. Mol. Biol. 35 (1968) 539–560. [DOI] [PMID: 4877004]
3.  Jost, J.-P. and Bock, R.M. Enzymatic hydrolysis of N-substituted aminoacyl transfer ribonucleic acid in yeast. J. Biol. Chem. 244 (1969) 5866–5873. [DOI] [PMID: 4981785]
4.  Menninger, J.R. Accumulation of peptidyl tRNA is lethal to Escherichia coli. J. Bacteriol. 137 (1979) 694–696. [DOI] [PMID: 368041]
5.  Dutka, S., Meinnel, T., Lazennec, C., Mechulam, Y. and Blanquet, S. Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase. Nucleic Acids Res. 21 (1993) 4025–4030. [DOI] [PMID: 7690473]
6.  Menez, J., Buckingham, R.H., de Zamaroczy, M. and Campelli, C.K. Peptidyl-tRNA hydrolase in Bacillus subtilis, encoded by spoVC, is essential to vegetative growth, whereas the homologous enzyme in Saccharomyces cerevisiae is dispensable. Mol. Microbiol. 45 (2002) 123–129. [DOI] [PMID: 12100553]
7.  Rosas-Sandoval, G., Ambrogelly, A., Rinehart, J., Wei, D., Cruz-Vera, L.R., Graham, D.E., Stetter, K.O., Guarneros, G. and Soll, D. Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase are nonessential in yeast. Proc. Natl. Acad. Sci. USA 99 (2002) 16707–16712. [DOI] [PMID: 12475929]
8.  De Pereda, J.M., Waas, W.F., Jan, Y., Ruoslahti, E., Schimmel, P. and Pascual, J. Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity. J. Biol. Chem. 279 (2004) 8111–8115. [DOI] [PMID: 14660562]
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