2.3.2.6: lysine/arginine leucyltransferase
This is an abbreviated version!
For detailed information about lysine/arginine leucyltransferase, go to the full flat file.
Word Map on EC 2.3.2.6
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2.3.2.6
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aminoacyl-trnas
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diphtheria
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toxin
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aa
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eubacterial
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ribosylation
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n-termini
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peptidoglycan
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trna-dependent
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cycloaddition
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non-ribosomal
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puromycin
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n-degrons
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alkyne
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transferase-mediated
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toxin-dependent
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leu-trnaleu
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synthesis
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analysis
- 2.3.2.6
- aminoacyl-trnas
- diphtheria
- toxin
- aa
-
eubacterial
-
ribosylation
-
n-termini
- peptidoglycan
-
trna-dependent
-
cycloaddition
-
non-ribosomal
- puromycin
-
n-degrons
-
alkyne
-
transferase-mediated
-
toxin-dependent
- leu-trnaleu
- synthesis
- analysis
Reaction
Synonyms
AAT, aminoacyl transferase, aminoacyl tRNA protein transferase, L/F transferase, L/F-transferase, L/F-tRNA-protein transferase, leucyl, phenylalanine-tRNA-protein transferase, leucyl, phenylalanyl transfer ribonucleic acid-protein transferase, leucyl-phenylalanine-transfer ribonucleate-protein aminoacyltransferase, leucyl-phenylalanine-transfer ribonucleate-protein transferase, leucyl/phenylalaninyl tRNA protein transferase, leucyl/phenylalanyl tRNA protein transferase, leucyl/phenylalanyl-tRNA protein transferase, leucyl/phenylalanyl-tRNA-protein transferase, leucyltransferase, LF-transferase, LFTR, R/K-transferase
ECTree
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General Information on EC 2.3.2.6 - lysine/arginine leucyltransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
the enzyme belongs to the Dupli-GNAT superfamily and contains a GNAT-like domain
metabolism
substrate specificity of aminoacyl tRNA protein transferase and Escherichia coli end rule, overview
physiological function
additional information
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
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
additional information
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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
