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Literature summary for 2.3.2.6 extracted from

  • Fung, A.W.; Fahlman, R.P.
    The molecular basis for the post-translational addition of amino acids by L/F transferase in the N-end rule pathway (2015), Curr. Protein Pept. Sci., 16, 163-180 .
    View publication on PubMed
Search for more literature for 2.3.2.6

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein] Escherichia coli
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 tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
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 ?
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein] Escherichia coli
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 tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
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 ?
additional information Escherichia coli in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein ?
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Organism

Organism UniProt Comment Textmining
Escherichia coli P0A8P1
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein]
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 Escherichia coli tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
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 ?
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein]
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 Escherichia coli tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
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 ?
L-phenylalanyl-tRNAPhe + N-terminal L-arginyl-[protein]
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 Escherichia coli tRNAPhe + N-terminal L-phenylalanyl-L-arginyl-[protein]
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 ?
L-phenylalanyl-tRNAPhe + N-terminal L-lysyl-[protein]
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 Escherichia coli tRNAPhe + N-terminal L-phenylalanyl-L-lysyl-[protein]
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 ?
additional information in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein Escherichia coli ?
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additional information in vitro, the L/F transferase catalyzes the transfer of Leu or Phe (1° destabilizing) or Met (2° destabilizing) from an aminoacyl-tRNA to the N-terminus of a substrate protein bearing an N-terminal Arg or Lys (2° destabilizing) or Met (1° destabilizing) residue, substrate recognition and proposed mechanism for the generation of N-end rule substrates, structure-function relationship, overview. Design of an improved aminoacyl-tRNA substrate analogue Escherichia coli ?
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Synonyms

Synonyms Comment Organism
AAT
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 Escherichia coli
aminoacyl transferase
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 Escherichia coli
aminoacyl tRNA protein transferase
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 Escherichia coli
L/F-transferase
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 Escherichia coli
leucyl/phenylalaninyl tRNA protein transferase
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 Escherichia coli
R/K-transferase
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 Escherichia coli

General Information

General Information Comment Organism
evolution the enzyme belongs to the Dupli-GNAT superfamily and contains a GNAT-like domain Escherichia coli
metabolism substrate specificity of aminoacyl tRNA protein transferase and Escherichia coli end rule, overview Escherichia coli
additional information molecular mechanism of catalysis and substrate recognition, overview. The acceptor peptide mainly interacts with the domain I, while domain II is responsible for tRNA recognition Escherichia coli
physiological function all Escherichia coli proteins initiate with formyl-methionine. Upon proteolytic cleavage by exo- and/or endopeptidases, a neo-N-terminus is exposed which is categorized into primary destabilizing (1°, including Leu, Phe, Trp, and Tyr) and secondary destabilizing (2°, including Arg and Lys) residues. 2° Degrons are recognized by the L/F transferase, which posttranslationally adds a Leu or Phe (1°) destabilizing residue from an aminoacyl-tRNA to the N-terminus of a protein having an Arg or Lys (2°). The adaptor ClpS recognizes and binds to proteins with a 1° N-degron and delivers the tagged protein to the proteasome-like complex ClpAP, where the protein is unfolded by the AAA+ ATPase ClpA and degraded by the protease ClpP. Posttranslational non-ribosomal amino acid transfer mechanism of L/F transferase transferring the aminoacyl moiety of the 3' end of an aminoacyl-tRNA substrate to an acceptor substrate, overview. The alpha-amino group of the N-terminus of a substrate polypeptide acts as a nucleophile and attacks the amino acyl carbonyl group. Two catalytic residues, D186 and Q188, are actively involved in the catalytic transfer reaction. The general base Q188, first activated by D186 via an electron-relay system, attracts a proteon from the alpha-NH3+ group of the N-terminal Arg acceptor substrate peptide and facilitates the nucleophile attack on the carbonyl carbon of the aminoacyl-tRNA donor substrate Escherichia coli