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
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-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
-
-
-
-
?
S: more
?
show the reaction diagram
-
L-methionyl-tRNAMet is a very poor substrate
-
-
-
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
Escherichia coli
-
at pH 7.6 and 37°C
-
0.8
KPC-acrydonylalanine
Escherichia coli
-
at pH 7.6 and 37°C
-
0.5
KQC-acrydonylalanine
Escherichia coli
-
at pH 7.6 and 37°C
-
0.002
L-leucyl-tRNALeu
Escherichia coli
-
apparent value, at pH 9.0 and 37°C
0.00052
L-phenylalanyl-tRNAPhe
Escherichia coli
-
apparent value, at pH 9.0 and 37°C
0.00183 - 0.00367
REPGLCTWQSLR
1
RGPCRAFI
Escherichia coli
-
at pH 7.6 and 37°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
216.7
KAC-acrydonylalanine
Escherichia coli
-
at pH 7.6 and 37°C
210589
40
KPC-acrydonylalanine
Escherichia coli
-
at pH 7.6 and 37°C
210591
96.7
KQC-acrydonylalanine
Escherichia coli
-
at pH 7.6 and 37°C
210590
916.7
RGPCRAFI
Escherichia coli
-
at pH 7.6 and 37°C
210592
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
ORGANISM
UNIPROT
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
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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