Information on EC 2.3.2.6 - lysine/arginine leucyltransferase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
2.3.2.6
-
RECOMMENDED NAME
GeneOntology No.
lysine/arginine leucyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-leucyl-tRNALeu + N-terminal L-arginyl-[protein] = tRNALeu + N-terminal L-leucyl-L-arginyl-[protein]
show the reaction diagram
(2)
-
-
-
L-leucyl-tRNALeu + N-terminal L-lysyl-[protein] = tRNALeu + N-terminal L-leucyl-L-lysyl-[protein]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
N-end rule pathway I (prokaryotic)
-
-
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 hide
37257-22-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Escherichia coli B / ATCC 11303
B
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
regulated proteolysis, N-end rule pathway
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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 + 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-phenylalanyl + acceptor protein
tRNA + L-phenylalanyl-protein
show the reaction diagram
L-phenylalanyl-tRNA + acceptor protein
tRNA + L-phenylalanyl-protein
show the reaction diagram
L-phenylalanyl-tRNA + KAC-acrydonylalanine
tRNA + L-phenylalanyl-KAC-acrydonylalanine
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA + KPC-acrydonylalanine
tRNA + L-phenylalanyl-KPC-acrydonylalanine
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA + KQC-acrydonylalanine
tRNA + L-phenylalanyl-KQC-acrydonylalanine
show the reaction diagram
-
-
-
-
?
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
t-RNA + FREPGLCTWQSLR
show the reaction diagram
-
-
-
-
?
L-phenylalanyl-tRNA + REPGLCTWQSLR
tRNA + FREPGLCTWQSLR
show the reaction diagram
-
substrate peptide
-
-
?
L-phenylalanyl-tRNA + RGPCRAFI
tRNA + L-phenylalanyl-RGPCRAFI
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-phenylalanyl-tRNAPhe + protein
tRNAPhe + L-phenylalanyl-[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
-
-
-
-
?
O-(2-fluoroethyl)- L-tyrosyl-tRNA + acceptor protein
tRNA + O-(2-fluoroethyl)-L-tyrosyl-protein
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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-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
-
-
-
-
?
L-phenylalanyl-tRNAPhe + protein
tRNAPhe + L-phenylalanyl-[protein]
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Na+
-
requirement
NH4+
-
monovalent cation required, stimulation of Leu transfer is somewhat greater than that of Phe
additional information
-
no Mg2+-requirement
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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-Gly
-
-
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
ribonuclease
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012
KAC-acrydonylalanine
-
at pH 7.6 and 37°C
0.021
KPC-acrydonylalanine
-
at pH 7.6 and 37°C
0.0051
KQC-acrydonylalanine
-
at pH 7.6 and 37°C
0.002
L-leucyl-tRNALeu
-
apparent value, at pH 9.0 and 37°C
0.0033
L-phenylalanyl-tRNAPhe
-
apparent value, at pH 9.0 and 37°C
2.2 - 18
REPGLCTWQSLR
0.011
RGPCRAFI
-
at pH 7.6 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25
KAC-acrydonylalanine
-
at pH 7.6 and 37°C
0.8
KPC-acrydonylalanine
-
at pH 7.6 and 37°C
0.5
KQC-acrydonylalanine
-
at pH 7.6 and 37°C
0.002
L-leucyl-tRNALeu
-
apparent value, at pH 9.0 and 37°C
0.00052
L-phenylalanyl-tRNAPhe
-
apparent value, at pH 9.0 and 37°C
0.00183 - 0.00367
REPGLCTWQSLR
1
RGPCRAFI
-
at pH 7.6 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
216.7
KAC-acrydonylalanine
-
at pH 7.6 and 37°C
40
KPC-acrydonylalanine
-
at pH 7.6 and 37°C
96.7
KQC-acrydonylalanine
-
at pH 7.6 and 37°C
916.7
RGPCRAFI
-
at pH 7.6 and 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
peptide bond formation assay
7.6 - 8.2
-
transfer of Leu
8.2 - 8.6
-
transfer of Phe
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
about 80% of maximal activity at pH 7.0 and 9.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
peptide bond formation assay
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
Crystallization/COMMENTARY
ORGANISM
UNIPROT
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 minimal substrate phenylalanyl adenosine inhibitor puromycin
-
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
t1/2: 1.5 min, complete inactivation after 8.5 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Stable to repeated freeze-thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 1 month
-
-20°C, stable for at least 2 months
-
-20°C, stable for at least 6 months
-
-20°C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
into the vector pCA24N
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
COMMENTARY hide
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
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