Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-tRNA + REPGLCTWQSLR
tRNA + LREPGLCTWQSLR
-
substrate peptide
-
-
?
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-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-[protein]
L-leucyl-tRNALeu + putrescine aminotransferase
tRNALeu + L-leucyl-[putrescine aminotransferase]
-
posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
L-phenylalanyl + acceptor protein
tRNA + L-phenylalanyl-protein
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
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 + Lys-Ala-Ala
Phe-Lys-Ala-Ala + tRNA
L-phenylalanyl-tRNA + protein
tRNA + L-phenylalanyl-protein
-
-
-
-
?
L-phenylalanyl-tRNA + putrescine aminotransferase
tRNA + L-phenylalanyl-putrescine aminotransferase
-
posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-phenylalanyl-tRNA + REPGLCTWQSLR
t-RNA + FREPGLCTWQSLR
-
-
-
?
L-phenylalanyl-tRNA + REPGLCTWQSLR
tRNA + FREPGLCTWQSLR
-
substrate peptide
-
-
?
L-phenylalanyl-tRNA + RGPCRAFI
tRNA + L-phenylalanyl-RGPCRAFI
-
-
-
-
?
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]
-
-
-
?
L-phenylalanyl-tRNAPhe + protein
tRNAPhe + L-phenylalanyl-[protein]
-
-
-
-
?
L-Trp + acceptor protein
tRNA + L-Trp
-
-
-
-
?
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
-
-
-
-
?
O-(2-fluoromethyl)-L-tyrosinyl-tRNA + N-terminal L-leucyl-[protein]
tRNA + N-terminal O-(2-fluoromethyl)-L-tyrosinyl-L-leucyl-[protein]
-
-
-
?
additional information
?
-
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-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
-
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
-
incorporation of Leu into the peptide linkage with the amino-terminal aspartic acid of albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
-
acceptor protein: alphaS1-casein
-
?
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
-
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]
-
-
-
-
?
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-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
-
-
-
-
?
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
-
-
?
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
-
-
-
-
?
L-phenylalanyl-tRNA + Lys-Ala-Ala
Phe-Lys-Ala-Ala + tRNA
-
-
-
?
L-phenylalanyl-tRNA + Lys-Ala-Ala
Phe-Lys-Ala-Ala + tRNA
-
-
-
?
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
-
-
?
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
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
brenda
Deutch, C.E.
Aminoacyl-tRNA: protein transferases
Methods Enzymol.
106
198-205
1984
Escherichia coli
brenda
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
brenda
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
brenda
Abramochkin, G.; Shrader, T.E.
Aminoacyl-tRNA recognition by the leucyl/phenylalanyl-tRNA-protein transferase
J. Biol. Chem.
271
22901-22907
1996
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
Curr. Protein Pept. Sci.
16
163-180
2015
Escherichia coli (P0A8P1), Escherichia coli
brenda