Any feedback?
Information on EC 2.3.2.6 - lysine/arginine leucyltransferase and Organism(s) Escherichia coli and UniProt Accession P0A8P1
for references in articles please use BRENDA:EC2.3.2.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.2.6 lysine/arginine leucyltransferaseIUBMB Comments
Requires a univalent cation. The enzyme participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue. Once modified, the proteins are recognized by EC 3.4.21.92, the ClpAP/ClpS endopeptidase system. The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo . cf. EC 2.3.2.29, aspartate/glutamate leucyltransferase, and EC 2.3.2.8, arginyltransferase.
Specify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
+
N-terminal L-lysyl-[protein]
=
+
N-terminal L-leucyl-L-lysyl-[protein]
+
N-terminal L-arginyl-[protein]
=
+
N-terminal L-leucyl-L-arginyl-[protein]
Synonyms
l/f-transferase, l/f transferase, leucyl/phenylalanyl-trna-protein transferase, aminoacyl transferase, lf-transferase, leucyl/phenylalanyl-trna protein transferase, l/f-trna-protein transferase, leucyltransferase, leucyl/phenylalanyl trna protein transferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L/F-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/phenylalanyl-tRNA-protein transferase
L/F-transferase
-
-
-
-
leucyl/phenylalanyl-tRNA-protein transferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
aminoacyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-leucyl-tRNALeu:[protein] N-terminal L-lysine/L-arginine leucyltransferase
Requires a univalent cation. The enzyme participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue. Once modified, the proteins are recognized by EC 3.4.21.92, the ClpAP/ClpS endopeptidase system. The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo [5]. cf. EC 2.3.2.29, aspartate/glutamate leucyltransferase, and EC 2.3.2.8, arginyltransferase.
CAS REGISTRY NUMBER
COMMENTARY
37257-22-0
-
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
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein]
tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
-
-
-
?
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein]
tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
-
-
-
?
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]
-
-
-
?
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]
-
-
-
?
O-(2-fluoromethyl)-L-tyrosinyl-tRNA + N-terminal L-leucyl-[protein]
tRNA + N-terminal O-(2-fluoromethyl)-L-tyrosinyl-L-leucyl-[protein]
-
-
-
?
1-naphthylalanyl-tRNA + L-Lys-SoCBM13
1-naphthylalanyl-L-Lys-SoCBM13 + tRNA
-
a xylan binding domain with N-terminal Lys. Introduction of 1-naphthylalanine is more difficult than of 2-naphthylalanine
-
-
?
2-naphthylalanyl-tRNA + L-Lys-SoCBM13
2-naphthylalanyl-L-Lys-SoCBM13 + tRNA
-
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
-
-
-
-
?
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
-
a xylan binding domain with N-terminal Lys
-
-
?
L-leucyl-tRNALeu + putrescine aminotransferase
tRNALeu + L-leucyl-[putrescine aminotransferase]
-
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
-
posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-phenylalanyl-tRNA + REPGLCTWQSLR
tRNA + FREPGLCTWQSLR
-
substrate peptide
-
-
?
L-phenylalanyl-tRNAPhe + protein
tRNAPhe + L-phenylalanyl-[protein]
-
-
-
-
?
L-Trp-tRNATrp + acceptor protein
tRNATrp + L-Trp-[acceptor protein]
-
-
-
-
?
O-(2-fluoroethyl)- L-tyrosyl-tRNA + acceptor protein
tRNA + O-(2-fluoroethyl)-L-tyrosyl-protein
-
-
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptor protein: alphaS1-casein
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
incorporation of Leu into the peptide linkage with the amino-terminal aspartic acid of albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
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
-
the association of the Leu-tRNA-enzyme complex is diffusion controlled
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptors with arginine or lysine as initial NH2-terminal residue
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
dipeptide specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
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
-
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]
-
strongly preferred substrate
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
-
-
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
-
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-phenylalanyl + acceptor protein
tRNA + L-phenylalanyl-protein
-
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
-
-
?
additional information
?
-
in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
-
-
-
additional information
?
-
-
in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
substrate recognition. Vatiants of the enzyme, lacking either 33 or 78 N-terminal residues, retain measurable peptidyltransferase activity and wild type substrate specificity
-
-
?
additional information
?
-
-
no activity with Val-tRNAVal-1 (UAC anticodon), Val-tRNAMetm (UAC anticodon), and Arg-tRNAMetm
-
-
?
additional information
?
-
-
L-methionyl-tRNAMet is a very poor substrate
-
-
?
NATURAL SUBSTRATE
NATURAL 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
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein]
tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
-
-
-
?
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein]
tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
-
-
-
?
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 + protein
tRNAPhe + L-phenylalanyl-[protein]
-
-
-
-
?
additional information
?
-
in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
-
-
-
additional information
?
-
-
in vivo, the dominating modification is leucylation of the N-terminus of the substrate protein
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
NH4+
-
monovalent cation required, stimulation of Leu transfer is somewhat greater than that of Phe
K+
-
monovalent cation required, stimulation of Leu transfer is somewhat greater than that of Phe
K+
-
monovalent cation required, maximal activity is 0.15 M KCl for the transfer of Phe and 0.2 M for the transfer of Leu
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
puromycin
-
aminonucleoside derivative, which lacks the aminoacyl analogus structure, fails to inhibit the reaction
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetic analysis of L/F-transferase
-
2.2
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-azido phenylalanine, Km apparent
3.2
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, phenylalanine, Km apparent
4.3
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-bromo phenylalanine, Km apparent
18
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-acetyl-N-(tert-butoxycarbonyl)-L-phenylalanine, Km apparent
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00183
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-azido phenylalanine, Kcat apparent
0.00283
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-acetyl-N-(tert-butoxycarbonyl)-L-phenylalanine, Kcat apparent
0.00333
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, 4-bromo phenylalanine, Kcat apparent
0.00367
REPGLCTWQSLR
-
amino acid residue on the aminoacyl-tRNA(Phe) transferred to the peptide substrate, phenylalanine, Kcat apparent
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.5
Arginine methyl ester
-
inhibition of reaction with alphaS1-casein as acceptor
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
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
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
-
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
in complex with puromycin. The p-methoxybenzyl group of puromycin is accomodated in a highly hydrophobic pocket. Model of complex with tRNA and a substrate bearing an N-terminal Arg or Lys
enzyme adopts a monomeric structure consisting of two domains that form a bilobate molecule. The n-terminal domain forms a small lobe with an unusual fold. The large C-terminal domain has a highly conserved fold. Comparison with bacterial peptidoglycan synthase FemX
in complex with minimal substrate phenylalanyl adenosine inhibitor puromycin
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
M144A
the mutant exhibits about 9% activity compared to the wild type
Q188A
the mutant exhibits about 8% activity compared to the wild type
W49A
the mutant exhibits about 10% activity compared to the wild type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
leucyl/phenylalanyl(L/F)-tRNA-protein transferase mediates aminoacyl transfer of a nonnatural amino acid to the N-terminus of peptides and proteins and the bioorthogonal reactive group can be converted to a variety of functional groups
analysis
-
a novel method to quantify L/F transferase activity by matrix assisted laser desorption/ionization time-of-flight mass spectrometry, MALDI-TOF, is reported
synthesis
-
use of enzyme to link non-natural amino acids to the N termini of target proteins through the use of tRNAPhes aminoacylated with various types of non-natural amino acids
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leibowitz, M.J.; Soffer, R.L.
A soluble enzyme from Escherichia coli which catalyzes the transfer of leucine and phenylalanine from tRNA to acceptor proteins
Biochem. Biophys. Res. Commun.
36
47-53
1969
Escherichia coli, Escherichia coli B / ATCC 11303
Leibowitz, M.J.; Soffer, R.L.
Enzymatic modification of proteins. 3. Purification and properties of a leucyl, phenylalanyl transfer ribonucleic acid protein transferase from Escherichia coli
J. Biol. Chem.
245
2066-2073
1970
Escherichia coli, Escherichia coli B / ATCC 11303
Soffer, R.L.
Peptide acceptors in the leucine, phenylalanine transfer reaction
J. Biol. Chem.
248
8424-8428
1973
Escherichia coli, Escherichia coli B / ATCC 11303
Deutch, C.E.
Aminoacyl-tRNA: protein transferases
Methods Enzymol.
106
198-205
1984
Escherichia coli
Scarpulla, R.C.; Deutch, C.E.; Soffer, R.L.
Transfer of methionyl residues by leucyl, phenylalanyl-tRNA-protein transferase
Biochem. Biophys. Res. Commun.
71
584-589
1976
Escherichia coli, Escherichia coli B / ATCC 11303
Abrahamochkin, G.; Shrader, T.E.
The leucyl/phenylalanyl-tRNA-protein transferase. Overexpression and characterization of substrate recognition, domain structure, and secondary structure
J. Biol. Chem.
270
20621-20628
1995
Escherichia coli
Abramochkin, G.; Shrader, T.E.
Aminoacyl-tRNA recognition by the leucyl/phenylalanyl-tRNA-protein transferase
J. Biol. Chem.
271
22901-22907
1996
Escherichia coli
Ichetovkin, I.E.; Abramochkin, G.; Shrader, T.E.
Substrate recognition by the leucyl/phenylalanyl-tRNA-protein transferase. Conservation within the enzyme family and localization to the trypsin-resistant domain
J. Biol. Chem.
272
33009-33014
1997
Escherichia coli
Kaji, A.; Kaji, H.; Novelli, G.D.
Soluble amino acid-incorporating system. I. Preparation of the system and nature of the reaction
J. Biol. Chem.
240
1185-1191
1965
Escherichia coli
Kaji, A.; Kaji, H.; Novelli, G.D.
Soluble amino acid-incorporating system. II. Soluble nature of the system and the characterization of the radioactive product
J. Biol. Chem.
240
1192-1197
1965
Escherichia coli
Momose, K.; Kaji, A.
Soluble amino acid-incorporating system: III. Further studies on the product and its relation to the ribosomal system for incorporation
J. Biol. Chem.
241
3294-3207
1966
Escherichia coli
Taki, M.; Kuno, A.; Matoba, S.; Kobayashi, Y.; Futami, J.; Murakami, H.; Suga, H.; Taira, K.; Hasegawa, T.; Sisido, M.
Leucyl/phenylalanyl-tRNA-protein transferase-mediated chemoenzymic coupling of N-terminal Arg/Lys units in post-translationally processed proteins with non-natural amino acids
ChemBiochem
7
1676-1679
2006
Escherichia coli
Suto, K.; Shimizu, Y.; Watanabe, K.; Ueda, T.; Fukai, S.; Nureki, O.; Tomita, K.
Crystal structures of leucyl/phenylalanyl-tRNA-protein transferase and its complex with an aminoacyl-tRNA analog
EMBO J.
25
5942-5950
2006
Escherichia coli (P0A8P1), Escherichia coli
Dong, X.; Kato-Murayama, M.; Muramatsu, T.; Mori, H.; Shirouzu, M.; Bessho, Y.; Yokoyama, S.
The crystal structure of leucyl/phenylalanyl-tRNA-protein transferase from Escherichia coli
Protein Sci.
16
528-534
2007
Escherichia coli, Escherichia coli (P0A8P1)
Taki, M.; Sisido, M.
Leucyl/phenylalanyl(L/F)-tRNA-protein transferase-mediated aminoacyl transfer of a nonnatural amino acid to the N-terminus of peptides and proteins and subsequent functionalization by bioorthogonal reactions
Biopolymers
88
263-271
2007
Escherichia coli (P0A8P1)
Watanabe, K.; Toh, Y.; Suto, K.; Shimizu, Y.; Oka, N.; Wada, T.; Tomita, K.
Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase
Nature
449
867-871
2007
Escherichia coli (P0A8P1)
Ebhardt, H.; Xu, Z.; Fung, A.; Fahlman, R.
Quantification of the post-translational addition of amino acids to proteins by MALDI-TOF mass spectrometry
Anal. Chem.
81
1937-1943
2009
Escherichia coli
Ninnis, R.L.; Spall, S.K.; Talbo, G.H.; Truscott, K.N.; Dougan, D.A.
Modification of PATase by L/F-transferase generates a ClpS-dependent N-end rule substrate in Escherichia coli
EMBO J.
28
1732-1744
2009
Escherichia coli
Fung, A.W.; Ebhardt, H.A.; Abeysundara, H.; Moore, J.; Xu, Z.; Fahlman, R.P.
An alternative mechanism for the catalysis of peptide bond formation by L/F transferase: substrate binding and orientation
J. Mol. Biol.
409
617-629
2011
Escherichia coli (P0A8P1), Escherichia coli
Kawaguchi, J.; Maejima, K.; Kuroiwa, H.; Taki, M.
Kinetic analysis of the leucyl/phenylalanyl-tRNA-protein transferase with acceptor peptides possessing different N-terminal penultimate residues
FEBS open bio
3
252-255
2013
Escherichia coli
Fung, A.W.; Ebhardt, H.A.; Krishnakumar, K.S.; Moore, J.; Xu, Z.; Strazewski, P.; Fahlman, R.P.
Probing the leucyl/phenylalanyl tRNA protein transferase active site with tRNA substrate analogues
Protein Pept. Lett.
21
603-614
2014
Escherichia coli
Fung, A.W.; Leung, C.C.; Fahlman, R.P.
The determination of tRNALeu recognition nucleotides for Escherichia coli L/F transferase
RNA
20
1210-1222
2014
Escherichia coli
Taki, M.; Kuroiwa, H.
Unexpectedly fast transfer of positron-emittable artificial substrate into N-terminus of peptide/protein mediated by wild-type L/F-tRNA-protein transferase
Amino Acids
47
1279-1282
2015
Escherichia coli (P0A8P1)
EXTERNAL LINKS (specific for EC-Number 2.3.2.6)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
