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Literature summary for 3.1.1.29 extracted from

  • Kaushik, S.; Singh, N.; Yamini, S.; Singh, A.; Sinha, M.; Arora, A.; Kaur, P.; Sharma, S.; Singh, T.P.
    The mode of inhibitor binding to peptidyl-tRNA hydrolase: binding studies and structure determination of unbound and bound peptidyl-tRNA hydrolase from Acinetobacter baumannii (2013), PLoS ONE, 8, e67547.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.29

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
native enzyme and in complex with cytidine or uridine, hanging drop vapor diffusion method, using 25% (w/v) PEG 10000, 0.3 M MgCl2 and 0.1 M HEPES buffer at pH 6.0 Acinetobacter baumannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-substituted aminoacyl-tRNA + H2O Acinetobacter baumannii
-
 N-substituted amino acid + tRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii D0C9L6
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA affinity resin column chromatography and Superdex G50 gel filtration Acinetobacter baumannii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-acetyl-Lys-tRNA + H2O
-
 Acinetobacter baumannii N-acetyl-Lys + tRNA
-
 ?
N-substituted aminoacyl-tRNA + H2O
-
 Acinetobacter baumannii N-substituted amino acid + tRNA
-
 ?

Synonyms

Synonyms Comment Organism
peptidyl-tRNA hydrolase
-
 Acinetobacter baumannii
PTH
-
 Acinetobacter baumannii