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Literature summary for 3.1.1.29 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)

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

Organism

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

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

General Information

General Information Comment Organism
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
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
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
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
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
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
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
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
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