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Information on EC 6.1.1.5 - isoleucine-tRNA ligase and Organism(s) Thermus thermophilus and UniProt Accession P56690

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Thermus thermophilus
UNIPROT: P56690 not found.
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The taxonomic range for the selected organisms is: Thermus thermophilus
The enzyme appears in selected viruses and cellular organisms
Synonyms
isoleucyl-trna synthetase, ilers, iars2, isoleucyl trna synthetase, iles2, ile-trna synthetase, isoleucine-trna synthetase, mitochondrial isoleucyl-trna synthetase, iles1, isoleucyl-transfer rna synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Isoleucine translase
-
Isoleucine--tRNA ligase
-
Isoleucine-transfer RNA ligase
-
Isoleucine-tRNA synthetase
-
Isoleucyl-transfer ribonucleate synthetase
-
Isoleucyl-transfer RNA synthetase
-
Isoleucyl-tRNA synthetase
-
Mupirocin resistance protein
-
Synthetase, isoleucyl-transfer ribonucleate
-
IleRS
Isoleucine translase
Isoleucine--tRNA ligase
Isoleucine-transfer RNA ligase
Isoleucine-tRNA synthetase
Isoleucyl-transfer ribonucleate synthetase
Isoleucyl-transfer RNA synthetase
Isoleucyl-tRNA synthetase
Mupirocin resistance protein
Synthetase, isoleucyl-transfer ribonucleate
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
editing and substrate recognition and binding mechanism, important involved residues are Asp238, Thr228, Thr229, and Thr230
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
substrate recognition mechanism, Glu551, Thr48, His581 and Lys594are involved
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
esterification
aminacylation
deacylation
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-isoleucine:tRNAIle ligase (AMP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9030-96-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
ATP + L-valine + tRNAIle
AMP + diphosphate + L-valyl-tRNAIle
show the reaction diagram
-
CP1 domain of the enzyme deacylates or edits the mischarged Val-tRNAIle
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
-
2 Zn2+ tightly bound
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-N-[N-(L-isoleucyl)sulfamoyl]adenosine
-
non-hydrolyzable analogue of the reaction intermediate Ile-AMP
muciproin
-
inhibition by blockage of the binding site of high energy intermediate Ile-AMP, the inhibitor contains a moiety that morphologically resembles the hydrophobic side chain of L-isoleucine, recognition is mediated by Pro46, Trp518, and Trp558
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
52.8
L-isoleucine
-
pH 8.0, 65°C, recombinant wild-type enzyme
0.0001
tRNAIle
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00025
muciproin
-
pH 8.0, 65°C, recombinant wild-type enzyme, with respect to L-isoleucine
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.8
-
about 30% of maximal activity at pH 6.0 and 8.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62
-
isoleucine-tRNA formation with E. coli tRNA
75
-
isoleucine tRNA formation with Thermus thermophilus tRNA
80
-
isoleucine dependent ATP-diphosphate exchange
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
129000
-
1 * 129000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 129000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization of CP1 domain alone or in complex with L-valine, X-ray structure determination at 1.8 and 2.0 A resolution respectively, and analysis
IleRS editing domain complexed with the substrate analogues in the pre and post-transfer modes, X-ray diffraction structure determination and analysis at 1.7 A resolution
crystallization of the 5'-N-[N-(L-isoleucyl)sulfamoyl]adenosine-enzyme complex, and the muciproin-enzyme complex by preparation of enzyme crystals and soaking of the crystals in 0.1 mM 5'-N-[N-(L-isoleucyl)sulfamoyl]adenosine solution, and 1 mM muciproin solution, respectively, X-ray diffraction structure determination at 2.5 A resolution, and analysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H319A
site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview
T223A
site-directed mutagenesis, Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain, but the mutant shows detectable editing activities against the cognate isoleucine, mechanism, overview
W227A
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227F
site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme
W227H
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227L
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227V
site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme
W227Y
site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77
-
half-life is 15 min, inactivation is completely suppressed by addition of either E. coli or Thermus thermophilus tRNA
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50% glycerol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutants enzymes from Escherichia coli by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutants enzymes in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kohda, D.; Yokoyama, S; Miyazawa, T.
Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases from an extreme thermophile Thermus thermophilus HB8. Protein structure and Zn2+ binding
FEBS Lett.
174
20-23
1984
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Wakagi, T.; Ohta, T.; Imahori, K.
Studies on isoleucyl-tRNA synthetase of an extreme thermophile, Thermus thermophilus HB8
Agric. Biol. Chem.
39
1573-1580
1975
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
Manually annotated by BRENDA team
Nakama, T.; Nureki, O.; Yokoyama, S.
Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase
J. Biol. Chem.
276
47387-47393
2001
Staphylococcus aureus (P41368), Staphylococcus aureus, Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Manually annotated by BRENDA team
Fukunaga, R.; Fukai, S.; Ishitani, R.; Nureki, O.; Yokoyama, S.
Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine
J. Biol. Chem.
279
8396-8402
2004
Thermus thermophilus (P56690), Thermus thermophilus
Manually annotated by BRENDA team
Fukunaga, R.; Yokoyama, S.
Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase
J. Mol. Biol.
359
901-912
2006
Thermus thermophilus (P56690), Thermus thermophilus
Manually annotated by BRENDA team