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
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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
2.3.2.6 lysine/arginine leucyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.3.2.6 - lysine/arginine leucyltransferase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-naphthylalanyl-tRNA + L-Lys-SoCBM13
1-naphthylalanyl-L-Lys-SoCBM13 + tRNA
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a xylan binding domain with N-terminal Lys. Introduction of 1-naphthylalanine is more difficult than of 2-naphthylalanine
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-
?
2-naphthylalanyl-tRNA + L-Lys-SoCBM13
2-naphthylalanyl-L-Lys-SoCBM13 + tRNA
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a xylan binding domain with N-terminal Lys. Introduction of 1-naphthylalanine is more difficult than of 2-naphthylalanine
-
-
?
3-nitrotyrosyl-tRNA + L-Arg-casein
3-nitrotyrosyl-L-Arg-casein + tRNA
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-
-
-
?
3-nitrotyrosyl-tRNA + L-Lys-glutathione S-transferase
3-nitrotyrosyl-L-Lys-glutathione S-transferase + tRNA
-
-
-
-
?
3-nitrotyrosyl-tRNA + L-Lys-SoCBM13
3-nitrotyrosyl-L-Lys-SoCBM13 + tRNA
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a xylan binding domain with N-terminal Lys
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-
?
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein]
tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
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-
-
?
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein]
tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
-
-
-
?
L-leucyl-tRNALeu + putrescine aminotransferase
tRNALeu + L-leucyl-[putrescine aminotransferase]
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posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-phenylalanyl-tRNA + KAC-acrydonylalanine
tRNA + L-phenylalanyl-KAC-acrydonylalanine
-
-
-
-
?
L-phenylalanyl-tRNA + KPC-acrydonylalanine
tRNA + L-phenylalanyl-KPC-acrydonylalanine
-
-
-
-
?
L-phenylalanyl-tRNA + KQC-acrydonylalanine
tRNA + L-phenylalanyl-KQC-acrydonylalanine
-
-
-
-
?
L-phenylalanyl-tRNA + putrescine aminotransferase
tRNA + L-phenylalanyl-putrescine aminotransferase
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posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-phenylalanyl-tRNA + REPGLCTWQSLR
tRNA + FREPGLCTWQSLR
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substrate peptide
-
-
?
L-phenylalanyl-tRNA(Leu) + L-arginyl-peptide
tRNA(Leu) + L-phenylalanyl-L-arginyl-protein
-
-
-
?
L-phenylalanyl-tRNA(Phe) + L-arginyl-peptide
tRNA(Phe) + L-phenylalanyl-L-arginyl-protein
-
-
-
?
L-phenylalanyl-tRNAPhe + N-terminal L-arginyl-[protein]
tRNAPhe + N-terminal L-phenylalanyl-L-arginyl-[protein]
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-
-
?
L-phenylalanyl-tRNAPhe + N-terminal L-leucyl-[protein]
tRNAPhe + N-terminal L-phenylalanyl-L-leucyl-[protein]
-
-
-
?
L-phenylalanyl-tRNAPhe + N-terminal L-lysyl-[protein]
tRNAPhe + N-terminal L-phenylalanyl-L-lysyl-[protein]
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-
-
?
L-phenylalanyl-tRNAPhe + protein
tRNAPhe + L-phenylalanyl-[protein]
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-
-
-
?
L-Trp-tRNATrp + acceptor protein
tRNATrp + L-Trp-[acceptor protein]
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-
-
-
?
O-(2-fluoroethyl)- L-tyrosyl-tRNA + acceptor protein
tRNA + O-(2-fluoroethyl)-L-tyrosyl-protein
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-
-
-
?
O-(2-fluoromethyl)-L-tyrosinyl-tRNA + N-terminal L-leucyl-[protein]
tRNA + N-terminal O-(2-fluoromethyl)-L-tyrosinyl-L-leucyl-[protein]
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-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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acceptor protein: bovine serum albumin
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?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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acceptor protein: bovine serum albumin
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?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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acceptor protein: alphaS1-casein
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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incorporation of Leu into the peptide linkage with the amino-terminal aspartic acid of albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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all peptides containing a NH2-terminal L-Arg or Lys residue function as acceptor, however D-Arg-D-Val is inactive
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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the association of the Leu-tRNA-enzyme complex is diffusion controlled
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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acceptors with arginine or lysine as initial NH2-terminal residue
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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basic NH2-terminal is absolute determinant of specificity
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?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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dipeptide specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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the major portion of L-Leu incorporation is an addition of amino acid to the NH2 group of a preformed acceptor or to a Lys NH2 group in the internal linkage, The NH2 group addition involving ribosomes is dependent on aminoacyl S-RNA, soluble enzymes, and the acceptor substance on ribosomes
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
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the major portion of L-Leu incorporation is an addition of amino acid to the NH2 group of a preformed acceptor or to a Lys NH2 group in the internal linkage. The NH2 group addition involving ribosomes is dependent on aminoacyl S-RNA, soluble enzymes, and the acceptor substance on ribosomes
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
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acceptor protein: bovine serum albumin
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?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
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acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
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incorporation of Leu into the peptide linkage with the amino-terminal aspartic acid of albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
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acceptor protein: alphaS1-casein
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
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all peptides containing a NH2-terminal L-Arg or Lys residue function as acceptor, however D-Arg-D-Val is inactive
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
Escherichia coli B / ATCC 11303
-
dipeptide specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-[protein]
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strongly preferred substrate
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
-
-
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
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wild-type Met-tRNAMetm (CAU anticodon) and mischarged Met-tRNAVal-1 (CAU anticodon) are substrates for LF-transferase during the NH2-terminal aminoacylation of alpha-casein
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
-
methionyl-tRNAmMet preferred to methionyl-tRNAfMet. Peptides containing a basic amino acid at the NH2-terminus function as acceptors
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
Escherichia coli B / ATCC 11303
-
methionyl-tRNAmMet preferred to methionyl-tRNAfMet. Peptides containing a basic amino acid at the NH2-terminus function as acceptors
-
-
?
L-phenylalanyl + acceptor protein
tRNA + L-phenylalanyl-protein
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the major portion of L-Phe incorporation is an addition of amino acid to the NH2 group of a preformed acceptor or to a Lys NH2 group in the internal linkage. The NH2 group addition involving ribosomes is dependent on aminoacyl S-RNA, soluble enzymes, and the acceptor substance on ribosomes
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
-
-
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
-
incorporation of Phe into the peptide linkage with the amino-terminal aspartic acid of albumin
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
Escherichia coli B / ATCC 11303
-
-
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
Escherichia coli B / ATCC 11303
-
incorporation of Phe into the peptide linkage with the amino-terminal aspartic acid of albumin
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
Escherichia coli B / ATCC 11303
-
-
-
-
?
additional information
?
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substrate recognition. Vatiants of the enzyme, lacking either 33 or 78 N-terminal residues, retain measurable peptidyltransferase activity and wild type substrate specificity
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-
?
additional information
?
-
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no activity with Val-tRNAVal-1 (UAC anticodon), Val-tRNAMetm (UAC anticodon), and Arg-tRNAMetm
-
-
?
additional information
?
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L-methionyl-tRNAMet is a very poor substrate
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-
?
additional information
?
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in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
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-
-
additional information
?
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in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
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-
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additional information
?
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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
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-
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additional information
?
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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
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-
-
additional information
?
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various non-natural amino acids as artificial substrates can be enzymatically introduced only at the basic N-terminus of any kind of acceptor peptides/proteins by using Escherichia coli leucyl/phenylalanyl-tRNA-protein transferase (L/F-transferase) without any engineering of its catalytic pocket. Extension of this L/F-transferase-mediated functionalization of peptides/proteins in combination with aminoacyl-tRNA synthetase (ARS) mutant. Fast enzymatic introduction of a positron emission tomography (PET) probe into acceptor peptides/proteins, it is site-specifically introduced at the basic N-terminus of the acceptors by using L/F-transferase in combination with aminoacyl-tRNA synthetase, namely the NEXT-A/PET reaction. Estimated from kinetic analysis, the transfer efficiency of O-(2-fluoromethyl)-L-tyrosine as an artificial amino acid PET probe mediated by the wild-type transferase is almost as good as that of the natural substrate, phenylalanine. About 90 % of Lys-Ala-7-amino-4-methylcoumarin peptide or of Lys-bradykinin peptide are labeled by O-(2-fluoromethyl)-L-tyrosine (FMT), the model protein Lys-SoCBM13 is also labeled by FMT
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