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Literature summary for 3.1.1.29 extracted from

  • Singarapu, K.; Xiao, R.; Acton, T.; Rost, B.; Montelione, G.; Szyperski, T.
    NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors (2008), Proteins Struct. Funct. Genet., 71, 1027-1031.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 (DE3) pMGK cells with eight nonnative residues at the C-terminus (LEHHHHHH) to facilitate protein purification Pseudomonas syringae pv. tomato

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
12700
-
SDS-PAGE Pseudomonas syringae pv. tomato

Organism

Organism UniProt Comment Textmining
Pseudomonas syringae pv. tomato Q885L4
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas syringae pv. tomato

Subunits

Subunits Comment Organism
monomer gel-filtration followed by a combination of static light scattering and refractive index Pseudomonas syringae pv. tomato

Synonyms

Synonyms Comment Organism
peptidyl-tRNA hydrolase
-
Pseudomonas syringae pv. tomato
PTH
-
Pseudomonas syringae pv. tomato