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Literature summary extracted from

  • Sharma, S.; Kaushik, S.; Sinha, M.; Kushwaha, G.S.; Singh, A.; Sikarwar, J.; Chaudhary, A.; Gupta, A.; Kaur, P.; Singh, T.P.
    Structural and functional insights into peptidyl-tRNA hydrolase (2014), Biochim. Biophys. Acta, 1844, 1279-1288.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Escherichia coli
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Mycolicibacterium smegmatis
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Pseudomonas aeruginosa
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Mycobacterium tuberculosis
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Saccharolobus solfataricus
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Francisella tularensis
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Acinetobacter baumannii
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Pyrococcus horikoshii
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Methanocaldococcus jannaschii
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Saccharolobus solfataricus P2
-
 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O Pyrococcus horikoshii OT-3
-
 N-substituted amino acid + tRNA
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.29 Acinetobacter baumannii
-
-
-
3.1.1.29 Escherichia coli
-
-
-
3.1.1.29 Francisella tularensis
-
-
-
3.1.1.29 Methanocaldococcus jannaschii Q60363
-
-
3.1.1.29 Mycobacterium tuberculosis
-
-
-
3.1.1.29 Mycolicibacterium smegmatis
-
-
-
3.1.1.29 Pseudomonas aeruginosa
-
-
-
3.1.1.29 Pyrococcus horikoshii O74017
-
-
3.1.1.29 Pyrococcus horikoshii OT-3 O74017
-
-
3.1.1.29 Saccharolobus solfataricus
-
-
-
3.1.1.29 Saccharolobus solfataricus P2
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Escherichia coli ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Mycolicibacterium smegmatis ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Pseudomonas aeruginosa ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Mycobacterium tuberculosis ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Saccharolobus solfataricus ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Francisella tularensis ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Acinetobacter baumannii ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Pyrococcus horikoshii ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Methanocaldococcus jannaschii ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Saccharolobus solfataricus P2 ?
-
 ?
3.1.1.29 additional information no activity with N-formyl-methionyl-tRNA Pyrococcus horikoshii OT-3 ?
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Escherichia coli N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Mycolicibacterium smegmatis N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Pseudomonas aeruginosa N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Mycobacterium tuberculosis N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Saccharolobus solfataricus N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Francisella tularensis N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Acinetobacter baumannii N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Pyrococcus horikoshii N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Methanocaldococcus jannaschii N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Saccharolobus solfataricus P2 N-substituted amino acid + tRNA
-
 ?
3.1.1.29 N-substituted aminoacyl-tRNA + H2O
-
 Pyrococcus horikoshii OT-3 N-substituted amino acid + tRNA
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.29 monomer
-
 Escherichia coli
3.1.1.29 monomer
-
 Mycolicibacterium smegmatis
3.1.1.29 monomer
-
 Pseudomonas aeruginosa
3.1.1.29 monomer
-
 Mycobacterium tuberculosis
3.1.1.29 monomer
-
 Saccharolobus solfataricus
3.1.1.29 monomer
-
 Francisella tularensis
3.1.1.29 monomer
-
 Acinetobacter baumannii
3.1.1.29 monomer
-
 Pyrococcus horikoshii
3.1.1.29 monomer
-
 Methanocaldococcus jannaschii

Synonyms

EC Number Synonyms Comment Organism
3.1.1.29 MJ0051 locus name Methanocaldococcus jannaschii
3.1.1.29 peptidyl-tRNA hydrolase
-
 Escherichia coli
3.1.1.29 peptidyl-tRNA hydrolase
-
 Mycolicibacterium smegmatis
3.1.1.29 peptidyl-tRNA hydrolase
-
 Pseudomonas aeruginosa
3.1.1.29 peptidyl-tRNA hydrolase
-
 Mycobacterium tuberculosis
3.1.1.29 peptidyl-tRNA hydrolase
-
 Saccharolobus solfataricus
3.1.1.29 peptidyl-tRNA hydrolase
-
 Francisella tularensis
3.1.1.29 peptidyl-tRNA hydrolase
-
 Acinetobacter baumannii
3.1.1.29 peptidyl-tRNA hydrolase
-
 Pyrococcus horikoshii
3.1.1.29 peptidyl-tRNA hydrolase
-
 Methanocaldococcus jannaschii
3.1.1.29 PH1539 locus name Pyrococcus horikoshii
3.1.1.29 Pth1 isoform Escherichia coli
3.1.1.29 Pth1 isoform Mycolicibacterium smegmatis
3.1.1.29 Pth1 isoform Pseudomonas aeruginosa
3.1.1.29 Pth1 isoform Mycobacterium tuberculosis
3.1.1.29 Pth1 isoform Francisella tularensis
3.1.1.29 Pth1 isoform Acinetobacter baumannii
3.1.1.29 Pth2 isoform Escherichia coli
3.1.1.29 Pth2 isoform Mycolicibacterium smegmatis
3.1.1.29 Pth2 isoform Pseudomonas aeruginosa
3.1.1.29 Pth2 isoform Mycobacterium tuberculosis
3.1.1.29 Pth2 isoform Francisella tularensis
3.1.1.29 Pth2 isoform Acinetobacter baumannii
3.1.1.29 SSO0175 locus name Saccharolobus solfataricus

General Information

EC Number General Information Comment Organism
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Escherichia coli
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Mycolicibacterium smegmatis
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Pseudomonas aeruginosa
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Mycobacterium tuberculosis
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Saccharolobus solfataricus
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Francisella tularensis
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Acinetobacter baumannii
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzyme which acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Methanocaldococcus jannaschii
3.1.1.29 physiological function peptidyl-tRNA hydrolase is an essential enzymewhich acts as one of the rescue factors of the stalled ribosomes. This enzyme is required for rapid clearing of the peptidyl-tRNAs, the accumulation of which in the cell leads to cell death Pyrococcus horikoshii