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Literature summary for 3.1.1.29 extracted from

  • Ito, K.; Murakami, R.; Mochizuki, M.; Qi, H.; Shimizu, Y.; Miura, K.; Ueda, T.; Uchiumi, T.
    Structural basis for the substrate recognition and catalysis of peptidyl-tRNA hydrolase (2012), Nucleic Acids Res., 40, 10521-10531.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with the tRNA CCA-acceptor-TpsiC domain of tRNAAla, sitting drop vapor diffusion method, using 100 mM sodium acetate buffer (pH 5.2), 20% (w/v) 1,4-butanediol and 30 mM glycyl-glycylglycine, at 20°C Escherichia coli

Protein Variants

Protein Variants Comment Organism
H188A the mutation results in a 5.4fold decrease in the kcat/Km value compared to the wild type enzyme Escherichia coli
N185A the mutation results in a 5.7fold decrease in the kcat/Km value compared to the wild type enzyme Escherichia coli
N185A/H188A the mutation results in a 7.7fold decrease in the kcat/Km value compared to the wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00471
-
N-acetyl-Ala-tRNA(Ala) wild type enzyme, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C Escherichia coli
0.0134
-
N-acetyl-Ala-tRNA(Ala) mutant enzyme N185A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C Escherichia coli
0.0171
-
N-acetyl-Ala-tRNA(Ala) mutant enzyme H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C Escherichia coli
0.0269
-
N-acetyl-Ala-tRNA(Ala) mutant enzyme N185A/H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C Escherichia coli

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
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A7D1
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-chelating column chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-Ala-tRNA(Ala) + H2O
-
Escherichia coli N-acetyl-Ala + tRNA(Ala)
-
?
N-substituted aminoacyl-tRNA + H2O
-
Escherichia coli N-substituted amino acid + tRNA
-
?

Synonyms

Synonyms Comment Organism
peptidyl-tRNA hydrolase
-
Escherichia coli
PTH
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.8
-
N-acetyl-Ala-tRNA(Ala) mutant enzyme N185A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C Escherichia coli
7.93
-
N-acetyl-Ala-tRNA(Ala) mutant enzyme H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C Escherichia coli
8.7
-
N-acetyl-Ala-tRNA(Ala) mutant enzyme N185A/H188A, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C Escherichia coli
11.7
-
N-acetyl-Ala-tRNA(Ala) wild type enzyme, in 20 mM HEPES-KOH (pH 7.6), 10 mM MgCl2, at 28°C Escherichia coli