Information on EC 2.3.2.6 - leucyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY
2.3.2.6
-
RECOMMENDED NAME
GeneOntology No.
leucyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-leucyl-tRNALeu + protein = tRNALeu + L-leucyl-[protein]
show the reaction diagram
-
-
-
-
L-leucyl-tRNALeu + protein = tRNALeu + L-leucyl-[protein]
show the reaction diagram
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 ACCESSION NO.
COMMENTARY
LITERATURE
aminoacyl group transfer
-
-
-
-
aminoacyl group transfer
-
-
SYSTEMATIC NAME
IUBMB Comments
L-leucyl-tRNALeu:protein leucyltransferase
Also transfers phenylalanyl groups. Requires a univalent cation. Peptides and proteins containing an N-terminal arginine, lysine or histidine residue can act as acceptors.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L/F transferase
-
-
L/F transferase
P0A8P1
-
L/F-transferase
-
-
-
-
L/F-transferase
-
-
L/F-transferase
P0A8P1
-
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
P0A8P1
-
leucyl/phenylalanyl-tRNA protein transferase
P0A8P1
-
leucyl/phenylalanyl-tRNA-protein transferase
-
-
-
-
leucyl/phenylalanyl-tRNA-protein transferase
-
-
leucyl/phenylalanyl-tRNA-protein transferase
P0A8P1
-
leucyltransferase
-
-
LF-transferase
P0A8P1
-
CAS REGISTRY NUMBER
COMMENTARY
37257-22-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
B; K12 strain W4977 and revertant strain R18 of mutant strain MS845
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
regulated proteolysis, N-end rule pathway
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-naphthylalanyl-tRNA + L-Lys-SoCBM13
1-naphthylalanyl-L-Lys-SoCBM13 + tRNA
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
3-nitrotyrosyl-tRNA + L-Lys-glutathione S-transferase
3-nitrotyrosyl-L-Lys-glutathione S-transferase + tRNA
show the reaction diagram
-
-
-
-
?
3-nitrotyrosyl-tRNA + L-Lys-SoCBM13
3-nitrotyrosyl-L-Lys-SoCBM13 + tRNA
show the reaction diagram
-
a xylan binding domain with N-terminal Lys
-
-
?
L-leucyl-tRNA + REPGLCTWQSLR
tRNA + LREPGLCTWQSLR
show the reaction diagram
-
substrate peptide
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
-
-
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
acceptor protein: bovine serum albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
acceptor protein: alphaS1-casein
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
incorporation of Leu into the peptide linkage with the amino-terminal aspartic acid of albumin
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
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
show the reaction diagram
-
the association of the Leu-tRNA-enzyme complex is diffusion controlled
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
acceptors with arginine or lysine as initial NH2-terminal residue
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
basic NH2-terminal is absolute determinant of specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
basic NH2-terminal is absolute determinant of specificity, dipeptide specificity
-
?
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
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
show the reaction diagram
-
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 + putrescine aminotransferase
tRNALeu + L-leucyl-[putrescine aminotransferase]
show the reaction diagram
-
posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
show the reaction diagram
-
-
-
-
?
L-methionyl-tRNA + acceptor protein
tRNA + L-methionyl-protein
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
L-phenylalanyl + acceptor protein
tRNA + L-phenylalanyl-protein
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
show the reaction diagram
-
incorporation of Phe into the peptide linkage with the amino-terminal aspartic acid of albumin
-
-
?
L-phenylalanyl-tRNA + Lys-Ala-Ala
Phe-Lys-Ala-Ala + tRNA
show the reaction diagram
-
-
-
?
L-phenylalanyl-tRNA + protein
tRNA + L-phenylalanyl-protein
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA + putrescine aminotransferase
tRNA + L-phenylalanyl-putrescine aminotransferase
show the reaction diagram
-
posttranslationally modification of PATase to generate a primary N-degron
-
-
?
L-phenylalanyl-tRNA + REPGLCTWQSLR
tRNA + FREPGLCTWQSLR
show the reaction diagram
-
substrate peptide
-
-
?
L-phenylalanyl-tRNA + REPGLCTWQSLR
t-RNA + FREPGLCTWQSLR
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA(Leu) + L-arginyl-peptide
tRNA(Leu) + L-phenylalanyl-L-arginyl-protein
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA(Phe) + L-arginyl-peptide
tRNA(Phe) + L-phenylalanyl-L-arginyl-protein
show the reaction diagram
-
-
-
-
?
L-Trp + acceptor protein
tRNA + L-Trp
show the reaction diagram
-
-
-
-
?
L-Trp-tRNATrp + acceptor protein
tRNATrp + L-Trp-[acceptor protein]
show the reaction diagram
-
-
-
-
?
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-leucyl-tRNALeu + protein
tRNALeu + L-leucyl-protein
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA + protein
tRNA + L-phenylalanyl-protein
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA(Leu) + L-arginyl-peptide
tRNA(Leu) + L-phenylalanyl-L-arginyl-protein
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA(Phe) + L-arginyl-peptide
tRNA(Phe) + L-phenylalanyl-L-arginyl-protein
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K+
-
monovalent cation required, stimulation of Leu transfer is somewhat greater than that of Phe
Na+
-
requirement
NH4+
-
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
additional information
-
no Mg2+-requirement
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Arg
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Ala
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Arg
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Asp
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Glu
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Gly
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Gly-Gly
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Leu
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Lys
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Phe
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Tyr
-
inhibition of alpha-S1-casein-dependent reaction
Arg-Val
-
inhibition of alpha-S1-casein-dependent reaction
Arginine methyl ester
-
inhibition of alpha-S1-casein-dependent reaction
CaCl2
-
20 mM, 35% inhibition
L-lysyl-L-serine
-
inhibition of alpha-S1-casein-dependent reaction
Lys
-
inhibition of alpha-S1-casein-dependent reaction
Lys-Ala
-
inhibition of alpha-S1-casein-dependent reaction
Lys-Ala-Ala
-
inhibition of alpha-S1-casein-dependent reaction
Lys-Glu
-
inhibition of alpha-S1-casein-dependent reaction
Lys-Leu
-
inhibition of alpha-S1-casein-dependent reaction
Lys-Phe
-
inhibition of alpha-S1-casein-dependent reaction
Lys-Tyr-Thr
-
inhibition of alpha-S1-casein-dependent reaction
Lys-Val
-
inhibition of alpha-S1-casein-dependent reaction
Mg2+
-
50 mM, 80% inhibition
MnCl2
-
91% inhibition
puromycin
-
aminonucleoside derivative, which lacks the aminoacyl analogus structure, fails to inhibit the reaction
ribonuclease
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no increase of activity by addition of GTP
-
additional information
-
not dependent on added GTP or mRNA
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.5
-
Arg-Ala
-
inhibition of reaction with alphaS1-casein as acceptor
0.4
-
Arg-Arg
-
inhibition of reaction with alphaS1-casein as acceptor
6
-
Arg-Asp
-
inhibition of reaction with alphaS1-casein as acceptor
7.5
-
Arg-Glu
-
inhibition of reaction with alphaS1-casein as acceptor
1.3
-
Arg-Gly
-
inhibition of reaction with alphaS1-casein as acceptor
0.4
-
Arg-Gly-Gly
-
inhibition of reaction with alphaS1-casein as acceptor
3.5
-
Arg-Leu
-
inhibition of reaction with alphaS1-casein as acceptor
0.2
-
Arg-Lys
-
inhibition of reaction with alphaS1-casein as acceptor
1.4
-
Arg-Phe
-
inhibition of reaction with alphaS1-casein as acceptor
1.6
-
Arg-Tyr
-
inhibition of reaction with alphaS1-casein as acceptor
1
-
Arg-Val
-
inhibition of reaction with alphaS1-casein as acceptor
10
-
arginine
-
inhibition of reaction with alphaS1-casein as acceptor
1.5
-
Arginine methyl ester
-
inhibition of reaction with alphaS1-casein as acceptor
3.6
-
Lys-Ala
-
inhibition of reaction with alphaS1-casein as acceptor
3
-
Lys-Ala-Ala
-
inhibition of reaction with alphaS1-casein as acceptor
15
-
Lys-Glu
-
inhibition of reaction with alphaS1-casein as acceptor
6
-
Lys-Gly
-
inhibition of reaction with alphaS1-casein as acceptor
7.8
-
Lys-Leu
-
inhibition of reaction with alphaS1-casein as acceptor
4
-
Lys-Phe
-
inhibition of reaction with alphaS1-casein as acceptor
10
-
Lys-Ser
-
inhibition of reaction with alphaS1-casein as acceptor
6.3
-
Lys-Tyr-Thr
-
inhibition of reaction with alphaS1-casein as acceptor
4
-
Lys-Val
-
inhibition of reaction with alphaS1-casein as acceptor
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
peptide bond formation assay
7.6
8.2
-
transfer of Leu
8.2
8.6
-
transfer of Phe
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
9
-
about 80% of maximal activity at pH 7.0 and 9.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
peptide bond formation assay
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the amino-acid-incorporating system is independent of ribosomes
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1.6 A resolution crystal structure; 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
-
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
t1/2: 1.5 min, complete inactivation after 8.5 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Stable to repeated freeze-thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for at least 1 month
-
-20C, stable for at least 2 months
-
-20C, stable for at least 6 months
-
-20C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
HisTrap column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into the vector pCA24N
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D186A
-
inactive
D186E
-
the mutation slightly reduces the reaction rate
D186N
-
inactive
M144A
-
the mutant exhibits about 9% activity compared to the wild type
Q188A
-
the mutant exhibits about 8% activity compared to the wild type
W111A
-
inactive
W49A
-
the mutant exhibits about 10% activity compared to the wild type
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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