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Literature summary for 2.3.2.6 extracted from

  • Watanabe, K.; Toh, Y.; Suto, K.; Shimizu, Y.; Oka, N.; Wada, T.; Tomita, K.
    Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase (2007), Nature, 449, 867-871.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of the Escherichia coli LF-transferase complex with phenyalanyl adenosine (rA-Phe), with or without a short peptide bearing an N-terminal Arg residue. In the presence of both the donor and acceptor substrates, the peptide formation proceedes within the crystals, and the product peptide bearing Phe at the N terminus is retained on the LF-transferase Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A8P1
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Reaction

Reaction Comment Organism Reaction ID
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein] = tRNALeu + N-terminal L-leucyl-L-lysyl-[protein] the electron relay from Asp 186 to Gln 188 helps Gln 188 to attract a proton from the a-amino group of the N-terminal Arg of the acceptor peptide. This generates the attacking nucleophile for the carbonyl carbon of the aminoacyl bond of the aminoacyl-tRNA, thus facilitating peptide-bond formation Escherichia coli

Synonyms

Synonyms Comment Organism
leucyl/phenylalanyl-tRNA protein transferase
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Escherichia coli
LF-transferase
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Escherichia coli