Information on EC 6.1.1.5 - Isoleucine-tRNA ligase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
6.1.1.5
-
RECOMMENDED NAME
GeneOntology No.
Isoleucine-tRNA ligase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
mechanism of aminoacylation in absence of diphosphatase is ordered ter-ter, in presence of diphosphatase random bi-uni uni-bi ping-pong
-
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
reaction kinetics and mechanism
-
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
substrate recognition mechanism, Glu551, Thr48, His581 and Lys594are involved
-
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
active site structure and mechanism
P41972
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aminacylation
-
-
-
-
aminacylation
-
-
aminacylation
-, Q8L1B1
-
aminacylation
-
-
aminacylation
Pseudomonas fluorescens NCIB10586, Staphylococcus aureus WCUH29
-
-
-
Aminoacylation
Q45477
-
Aminoacylation
-
-
Aminoacylation
-
-
Aminoacylation
Bacillus subtilis 168, Escherichia coli EM20031
-
-
-
deacylation
-
-
-
-
deacylation
-
-
deacylation
-, Q8L1B1
-
deacylation
Pseudomonas fluorescens NCIB10586, Staphylococcus aureus WCUH29
-
-
-
esterification
-
-
-
-
esterification
-
-
esterification
-
-
esterification
-, Q8L1B1
-
esterification
-
-
esterification
Pseudomonas fluorescens NCIB10586, Staphylococcus aureus WCUH29
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Aminoacyl-tRNA biosynthesis
-
tRNA charging
-
SYSTEMATIC NAME
IUBMB Comments
L-Isoleucine:tRNAIle ligase (AMP-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ile-tRNA synthetase
-
-
IleRS
-
-
-
-
IleRS
Q45477
-
IleRS
Bacillus subtilis 168
Q45477
-
-
IleRS
Escherichia coli EM20031
-
-
-
IleRS
-
-
IRS
-
-
-
-
Isoleucine translase
-
-
-
-
Isoleucine translase
-
-
Isoleucine translase
-
-
Isoleucine translase
-
-
Isoleucine translase
Q8L1B1
-
Isoleucine translase
-
-
Isoleucine translase
-
-
Isoleucine--tRNA ligase
-
-
-
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
Q8L1B1
-
Isoleucine--tRNA ligase
-
-
Isoleucine--tRNA ligase
-
-
Isoleucine-transfer RNA ligase
-
-
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
Q8L1B1
-
Isoleucine-transfer RNA ligase
Pseudomonas fluorescens NCIB10586
Q8L1B1
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-transfer RNA ligase
Staphylococcus aureus WCUH29
-
-
-
Isoleucine-transfer RNA ligase
-
-
Isoleucine-tRNA synthetase
-
-
-
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
Q8L1B1
-
Isoleucine-tRNA synthetase
-
-
Isoleucine-tRNA synthetase
-
-
isoleucyl tRNA synthetase
-
-
isoleucyl tRNA synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
Q8L1B1
-
Isoleucyl-transfer ribonucleate synthetase
Pseudomonas fluorescens NCIB10586
Q8L1B1
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer ribonucleate synthetase
Staphylococcus aureus WCUH29
-
-
-
Isoleucyl-transfer ribonucleate synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
-
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
Q8L1B1
-
Isoleucyl-transfer RNA synthetase
Pseudomonas fluorescens NCIB10586
Q8L1B1
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-transfer RNA synthetase
Staphylococcus aureus WCUH29
-
-
-
Isoleucyl-transfer RNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
-
-
Isoleucyl-tRNA synthetase
Q45477
-
Isoleucyl-tRNA synthetase
Bacillus subtilis 168
Q45477
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
Escherichia coli EM20031
-
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
Q8L1B1
-
Isoleucyl-tRNA synthetase
Pseudomonas fluorescens NCIB10586
Q8L1B1
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
-
-
Isoleucyl-tRNA synthetase
Staphylococcus aureus WCUH29
-
-
-
Mupirocin resistance protein
-
-
-
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
Q8L1B1
-
Mupirocin resistance protein
-
-
Mupirocin resistance protein
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
Q8L1B1
-
Synthetase, isoleucyl-transfer ribonucleate
Pseudomonas fluorescens NCIB10586
Q8L1B1
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Synthetase, isoleucyl-transfer ribonucleate
Staphylococcus aureus WCUH29
-
-
-
Synthetase, isoleucyl-transfer ribonucleate
-
-
Isoleucyl-tRNA synthetase
-
-
additional information
-
the enzyme is a class I aminoacyl-tRNA synthetase
CAS REGISTRY NUMBER
COMMENTARY
9030-96-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 168
UniProt
Manually annotated by BRENDA team
Bacillus subtilis 168
strain 168
UniProt
Manually annotated by BRENDA team
B; K12
-
-
Manually annotated by BRENDA team
strain EM20031
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes IleRS(C922S) and AIleRS, with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc (AIleRS), mutant enzymes have altered zinc binding and aminoacylation activity
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes with altered metal-binding sites
-
-
Manually annotated by BRENDA team
wild-type strain MC4100 and pseudomonic acid resistant mutant strain PS102
-
-
Manually annotated by BRENDA team
Escherichia coli EM20031
strain EM20031
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
Escherichia coli MRE600
MRE600
-
-
Manually annotated by BRENDA team
the Methanopyrus kandleri sequence is compared to the sequences of the Methanopyrus isolates GC34 and GC37 from the Pacific ocean and KOL6, TAG1, TAG11, and SNP6 from the Atlantic ocean
-
-
Manually annotated by BRENDA team
pseudomonic acid-resistant mutant; strain Marburg
-
-
Manually annotated by BRENDA team
strain Marburg; wild-type end pseudomonic-acid resistant mutant MBT10, with a Gly590 to aspartic acid transition
-
-
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicus Marburg
strain Marburg
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
two isozymes, an apicoplast isozyme encoded by gene PFL1210w, and a cytoplasmic isozyme encoded by gene PF13_0179
-
-
Manually annotated by BRENDA team
strain NCIB10586, gene ileS1, pseudomonic acid-sensitive isozyme IleRS-R1, recombinant enzyme expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
strain NCIB10586, pseudomonic acid-resistant isozyme IleRS-R2, gene ileS2
SwissProt
Manually annotated by BRENDA team
Pseudomonas fluorescens NCIB10586
strain NCIB10586, gene ileS1, pseudomonic acid-sensitive isozyme IleRS-R1, recombinant enzyme expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
Pseudomonas fluorescens NCIB10586
strain NCIB10586, pseudomonic acid-resistant isozyme IleRS-R2, gene ileS2
SwissProt
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
gene ileS
-
-
Manually annotated by BRENDA team
methicillin-resistant clinical isolates from humans, gene ileS
Uniprot
Manually annotated by BRENDA team
purified recombinant enzyme expressed in Escherichia coli strain DH1
-
-
Manually annotated by BRENDA team
strain WCUH29
-
-
Manually annotated by BRENDA team
Staphylococcus aureus WCUH29
strain WCUH29
-
-
Manually annotated by BRENDA team
strain HB8, purified recombinant wild-type and mutant enzyme
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
hydrolytic editing activities are present in aminoacyl-tRNA synthetases possessing reduced amino acid discrimination in the synthetic reactions. Post-transfer hydrolysis of misacylated tRNA in class I editing enzymes, e.g. IleRS, occurs in a spatially separate domain inserted into the catalytic Rossmann fold. tRNA-dependent hydrolysis of noncognate valyl-adenylate by IleRS is largely insensitive to mutations in the editing domain of the enzyme and that noncatalytic hydrolysis after release is too slow to account for the observed rate of clearing. Pre-transfer editing in IleRS is an enzyme-catalyzed activity residing in the synthetic active site. Balance between pretransfer and post-transfer editing pathways is controlled by kinetic partitioning of the noncognate aminoacyl-adenylate, overview. In IleRS both pre- and post-transfer editing are important
additional information
-
in mupirocin-resistant strains, e.g. evolved strain C12 that carried several copies of ileS, the antibiotic resistance leads also to reduced growth rates, these can be restored by the organism via increased expression of the original mutant ileS gene, also improving fitness while maintaining resistance, a process of adaptation initiated by common amplifications and followed by later acquisition of rare point mutations. A point mutation in one copy relaxes selection and allows loss of defective ileS copies, overview. Model for genetic adaptation of cells to the growth limitation caused by their MupR, overview
additional information
-
thiaisoleucine-resistant parasites possess a mutation in the cytoplasmic isoleucyl-tRNA synthetase, mutational analysis, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
P41368
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
P41972
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
P41972
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
r
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
-
-
-
-
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
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
P56690, -
-
-
r
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-, Q8L1B1
-
-
?
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
-
0.3% or less of the activity with isoleucine is measured with other amino acids
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
the anticodon for methionine and isoleucine tRNAs differ by a single nucleotide, changing this nucleotide in an isoleucine tRNA is sufficient to change aminoacylation specificity to methionine
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
enzyme has specificity for E. coli tRNAIle
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
enzyme shows a common recognition mode of aminoacyl-adenylate for a class I aminoacyl-tRNA synthetase, formation of high-energy reaction intermediate Ile-AMP
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
formation of a enzyme-bound aminoacyl adenylate intermediate
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
formation of an aminoacyl adenylate reaction intermediate
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
reaction intermediate is the Ile-AMP-enzyme complex
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
the binding region of the adenine moiety contains a wide hydrophobic pocket large enough to afford three linear aromatic rings
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-, Q8L1B1
tRNAIle from Pseudomonas fluorescens and Escherichia coli
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
physiological function is Thr formation of Ile-tRNA and editing of inadvertently misactivated homocysteine
-
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
the reaction plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
a two-step reaction, the first of which, the amino acid activation step, is reversible, while the second aminoacylation step is not, the amino acid editing site for LeuRS resides within the homologous CP1 domain containing a conserved threonine conferring amino acid substrate recognition, editing mechanism, some positions of the site are idiosyncratic to IleRS, residues Arg249, Asp251, Thr252, Met336, and Val338 are involved,overview
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
substrate recognition mechanisms of IleRS are characterized by the active-site rearrangement between the two editing modes, overview, the editing domain contributes to accurate aminoacylation by hydrolyzing the mis-synthesized intermediate, valyl-adenylate, in the pre-transfer editing mode and the incorrect final product, valyl-tRNAIle, in the post-transfer editing mode, Trp227 with its aromatic ring is important
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-, Q45477
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine, the lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by IleRS
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Bacillus subtilis 168
Q45477
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine, the lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by IleRS
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Methanothermobacter thermautotrophicus Marburg
-
-
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Methanothermobacter thermautotrophicus Marburg
-
-
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Escherichia coli EM20031
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Staphylococcus aureus WCUH29
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Pseudomonas fluorescens NCIB10586
-, Q8L1B1
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Pseudomonas fluorescens NCIB10586
-, Q8L1B1
tRNAIle from Pseudomonas fluorescens and Escherichia coli
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Escherichia coli K12
-
-
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Escherichia coli MRE600
-
-
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Escherichia coli MRE600
-
-
-
-
ATP + L-valine + tRNAIle
AMP + diphosphate + L-valyl-tRNAIle
show the reaction diagram
P56690, -
-
CP1 domain of the enzyme deacylates or edits the mischarged Val-tRNAIle
r
Formycin 5'-triphosphate + isoleucine + tRNAIle
?
show the reaction diagram
-
-
-
-
-
Ile-tRNAIle + 3-mercaptopropionate
S-Isoleucyl-3-mercaptopropionate + tRNAIle
show the reaction diagram
-
-
-
-
Ile-tRNAIle + cysteamine
tRNAIle + isoleucylcysteamine
show the reaction diagram
-
-
-
-
Ile-tRNAIle + cysteine
tRNAIle + isoleucylcysteine
show the reaction diagram
-
D- and L-isomer of Lys
D-isoleucylcysteine and L-isoleucylcysteine
-
Ile-tRNAIle + DTT
Thioester of Ile and DTT + tRNAIle
show the reaction diagram
-
-
-
-
Ile-tRNAIle + L-cysteine methyl ester
tRNAIle + isoleucyl-L-cysteine methyl ester
show the reaction diagram
-
-
-
-
Tubercidin 5'-triphosphate + isoleucine + tRNAIle
?
show the reaction diagram
-
-
-
-
-
Ile-tRNAIle + N-acetylcysteine
S-isoleucyl-N-acetylcysteine + tRNAIle
show the reaction diagram
-
-
-
-
additional information
?
-
-
position 2,6,7,8,9,2' and 3' of ATP are important for catalytic action of isleucyl-tRNA synthetase
-
-
-
additional information
?
-
-
discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)
-
-
-
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange
-
-
-
additional information
?
-
-
enzyme also performs the reversible ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
enzyme also performs the reversible ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
enzyme also performs the reversible ATP-diphosphate exchange reaction
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
additional information
?
-
-
Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain
-
-
-
additional information
?
-
Escherichia coli MRE600
-
discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)
-
-
-
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
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
P41368
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
P41972
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
P41972
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
r
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
-
-
r
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
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
P56690, -
-
-
r
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
-
-
-
?
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
-
-
-
-
?
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
-, Q8L1B1
-
-
?
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
-
physiological function is Thr formation of Ile-tRNA and editing of inadvertently misactivated homocysteine
-
-
-
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-
the reaction plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
-, Q45477
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine, the lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by IleRS
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Bacillus subtilis 168
Q45477
bacteria decode the isoleucine codon AUA using a tRNA species that is posttranscriptionally modified at the wobble position of the anticodon with a lysine-containing cytidine derivative called lysidine, the lysidine modification of tRNAIle2 is an essential identity determinant for proper aminoacylation by IleRS
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Escherichia coli EM20031
-
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Staphylococcus aureus WCUH29
-
-
-
?
ATP + L-isoleucine + tRNAIle
AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram
Pseudomonas fluorescens NCIB10586
-, Q8L1B1
-
-
?
additional information
?
-
-
aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
binds more tightly to the enzyme-Ile complex than to the free enzyme
ATP
-
dependent on, MgATP2-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ce3+
-
activates
Cobalt
-
cobalt-substituted enzyme is active
Dy3+
-
activates
Eu3+
-
activates
Gd3+
-
activates
La3+
-
activates
Mg2+
-
at least 2 bound Mg2+ or spermidines required for the binding of tRNA to the enzyme
Mg2+
-
at a concentration of ATP and diphosphate of 3 mM, the optimal Mg2+ concentration is 6-10 mM; required
Mg2+
-
optimum at very low concentration (0.5-0.7 mM), slight inhibition at higher concentration
Mg2+
-
optimal concentration is 5-6 mM
Mg2+
-
activates isoleucyl-tRNA formation
Mg2+
-
activates isoleucyl-tRNA formation; enzyme-bound isoleucyl-AMP can be formed in the absence of Mg2+ and spermine; synergistic effect with spermine
Mg2+
-
optimal concentration is 10 mM; required
Mg2+
-
in presence of 50 mM K+ and in absence of polyamines, the optimal Mg2+ concentration for Ile-tRNA formation is 1 mM, an increase in Mg2+ concentration markedly inhibits
Mg2+
-
required, MgATP2-
Mg2+
-
assay at
Nd3+
-
activates
Pr3+
-
activates
Sm3+
-
activates
Tb3+
-
activates
Yb3+
-
activates
Zinc
-
bound to a Cys4 cluster at the C-terminal end of the polypeptide; required
Zinc
-
2 enzyme bound zinc atoms per polypeptide chain
Zinc
-
a single zinc atom which is coordinated to ligands is contained in the catalytic domain, a second, functionally essential zinc is bound to ligands at the C-terminal end of the 939 amino acid polypeptide, the average zinc environment contains predominantly sulfur ligands with a Zn-S distance of 2.33 A
Zinc
-
2 tightly bound zinc atoms per active site; structural and catalytic role in aminoacylation
Zinc
-
contains 1.5-2 mol of Zn bound per mol of polypeptide
Zinc
-
zinc containing peptide at the C-terminus
Zinc
-
contains 1 Zn2+ per polypeptide chain
Zinc
-
2 Zn2+ tightly bound
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-(2-hydroxyethyl)-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-[(2E)-4-hydroxy-3-methylbut-2-en-1-yl]-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-[(2E)-4-[(3-carboxypropanoyl)oxy]-3-methylbut-2-en-1-yl]-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 15
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-[(2E,4E)-6-hydroxy-3-methylhexa-2,4-dien-1-yl]-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): 560.3. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4E)-5-[(2S,3R,6S,8R,9S)-3-butyl-3-[(3-carboxypropanoyl)oxy]-8-[(2E,4E,6S,7S)-6,8-dihydroxy-3,7-dimethylocta-2,4-dien-1-yl]-9-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-3-methylpenta-2,4-dienoic acid
-
IC50 (ng/ml): 22.9. Cell death inducibility of osteoclasts (microgram/ml): 6.31
(2E,4E)-6-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-[(3-carboxypropanoyl)oxy]-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-4-methylhexa-2,4-dienoic acid
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-3-methyl-9-[(methylsulfanyl)methoxy]-1,7-dioxaspiro[5.5]undec-2-yl]-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 497.4. Cell death inducibility of osteoclasts (microgram/ml): 9.6
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-hydroxy-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 94.6. Cell death inducibility of osteoclasts (microgram/ml): 11.5
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-methoxy-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 57.9. Cell death inducibility of osteoclasts (microgram/ml): not determined
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-[(3-carboxypropanoyl)oxy]-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-4,5-dihydroxy-8-methyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 14.4. Cell death inducibility of osteoclasts (microgram/ml): 1.01
(2E,4S,5S,6E,8E)-10-[(2R,3S,6S,8S,9R)-9-butyl-8-[(1E,3E)-4-carboxy-3-methylbuta-1,3-dien-1-yl]-9-[(4-methoxy-4-oxobutanoyl)oxy]-3-methyl-1,7-dioxaspiro[5.5]undec-2-yl]-5-hydroxy-4,8-dimethyldeca-2,6,8-trienoic acid
-
IC50 (ng/ml): 292.8. Cell death inducibility of osteoclasts (microgram/ml): 2.5
(3S)-3-amino-1-bromo-4-methylhexan-2-one
-
labeling reagent
(3S)-3-amino-1-bromo-4-methylpentan-2-one
-
labeling reagent
(3S)-3-amino-1-bromo-4-phenylbutan-2-one
-
labeling reagent
(3S)-3-amino-1-bromoheptan-2-one
-
labeling reagent
1,10-phenanthroline
-
-
2',3'-dialdehyde of tRNAile
-
used to label the binding site for the 3'end of tRNA on the synthetase, incubation of the reagent with IleRS results in a rapid loss of tRNAIle aminoacylation and isoleucine-dependent isotopic ATP-PPi exchange activities
-
2,2'-Bipyridyl
-
-
2,3-dideoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.0064 mM
2,3-Dihydro-5-epireveromycin A
-
IC50 (ng/ml): 58.3. Cell death inducibility of osteoclasts (microgram/ml): 0.82
2,3-Dihydroreveromycin A
-
IC50 (ng/ml): 11.6. Cell death inducibility of osteoclasts (microgram/ml): 0.22
2-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.28 mM
2-iodo-L-isoleucine-NHSO2-AMP
-
highly potent inhibitor, hydrophobic interaction of the 2-substituent of the inhibitor with the adenine binding site of the enzyme
3'-deoxyadenosine
-
i.e. cordycepin
3-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.035 mM
5'-N-[N-(L-isoleucyl)sulfamoyl]adenosine
-
non-hydrolyzable analogue of the reaction intermediate Ile-AMP
5-acetyl-Reveromycin A
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 0.46
5-Epireveromycin A
-
IC50 (ng/ml): 378.3. Cell death inducibility of osteoclasts (microgram/ml): 21.5
5-methoxy-Reveromycin A
-
IC50 (ng/ml): 374. Cell death inducibility of osteoclasts (microgram/ml): above 15
5-O-succinyl-Spirofungin A
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 12.4
5-tert-butyl-dimethylsilyl-Reveromycin A
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 5.9
7-[3-[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]propanoyl-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 10% inhibition at 0.1 mM
7-[4-[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]butanoyl-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 18% inhibition at 0.1 mM
7-[4-[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]butanoyl-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 26% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]acetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 17% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
-
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 49% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 31% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 46% inhibition at 0.1 mM
7-[[(2S,3S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 34% inhibition at 0.1 mM
7-[[(S)-2-amino-1-oxo-5-thiahexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 31% inhibition at 0.1 mM
7-[[(S)-2-amino-1-oxo-5-thiahexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 38% inhibition at 0.1 mM
7-[[(S)-2-amino-1-oxo-hexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 17% inhibition at 0.1 mM
7-[[(S)-2-amino-1-oxo-hexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamide
-
derivative of SB-203207, 46% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 31% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 38% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 33% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxobutyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 10% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 13% inhibition at 0.1 mM
7-[[(S)-2-amino-3-methyl-1-oxopentyl]amino]sulfonylacetyloxy-4,4a,5,6,7,7a-hexahydro-1-methyl-1H-cyclopenta[b]pyridine-3-carboxylic acid methyl ester
-
derivative of SB-203207, 15% inhibition at 0.1 mM
7-[[(S)-2-amino-4-methyl-1-oxopentyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxylic acid methyl ester
-
derivative of SB-203207, 14% inhibition at 0.1 mM
8-Aminoadenosine
-
-
8-azidoadenosine 5'-triphosphate
-
-
adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.000265 mM
Chymotrypsin
-
proteolytic inactivation patterns, bound Ile-AMP or inhibitors isoleucinol adenylate and pseudomonic acid protect, 50fold higher concentration is needed for digestion of Ile-AMP-enzyme complex than for the free enzyme at 37C
-
diethyl dicarbonate
-
-
diphosphate
-
partly inhibits the binding of tRNA
ester analogues of isoleucyl adenylate
-
with or without cyclic substitutents at the adenine moiety
Furanomycin
-
-
hydroxamate analogues of isoleucyl adenylate
-
with or without cyclic substitutents at the adenine moiety
Ile-NHSO2-AMP
-
non-hydrolyzable reaction intermediate analogue, slow-tight binding, competitive and inhibition mechanism, reversible
isoleucinol adenylate
-
determination of binding structures, bound inhibitor protects against proteolytic inactivation by trypsin or chymotrypsin and specifically alters the proteolytic cleavage pattern
isoleucinyl adenylate
-
i.e. Ile-ol-AMP, nonhydrolyzable reaction intermediate analogue, competitive with respect to both ATP and Ile
isoleucinyl-adenylate
-
i.e. Ile-ol-AMP, non-hydrolyzable reaction intermediate analogue, slow-tight binding, competitive and inhibition mechanism, reversible
isoleucyl isovanilloids
-
e.g. the isovanillic hydroxamate and amide analogue
isoleucyl sulfamate analogues
-
-
isoleucyl vanilloids
-
e.g. the vanillic hydroxamate with a phenolic hydoxyl at the para-position
isoleucyl-N'-adenosyl-N'-hydroxy sulfamide
-
-
isoleucyl-N'-adenosyloxy sulfamide
-
-
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
mupirocin
P41972
a specific inhibitor of IleRS, which binds in the vicinity of an ATP-binding subsite, and is a bifunctional inhibitor with characteristics of both isoleucine and ATP, i.e. an analogue of isoleucyladenylate, binding structure, overview, mupirocin resistance is phenotypically divided into two groups: low-level and high-level. Highlevel resistance is mediated by a plasmid containing the ileS-2 gene that encodes a distinct isoleucyl-tRNA synthetase enzyme, whereas low-level resistance usually results from alteration of the native IleS as a consequence of spontaneous mutations in the ileS gene
mupirocin
-
Mup, an isoleucyl-adenylate analogue that inhibits the essential enzyme, isoleucyl-tRNA synthetase
mupirocin
-
irreversible inhibition, inhibits development of invasion-competent parasites in the second asexual cycle, delayed death phenotype
Pseudomonic acid
-
bifunctional inhibitor with characteristics of both isoleucine and ATP
Pseudomonic acid
-
pseudomonic acid A: Saccharomyces cerevisiae enzyme is 10000 times less sensitive than Escherichia coli enzyme
Pseudomonic acid
-
-
Pseudomonic acid
-
wild-type enzyme strongly inhibited, pseudomonic acid-resistant mutant only marginally
Pseudomonic acid
-
forms a non-hydrolyzable reaction intermediate analogue, competitive inhibition
Pseudomonic acid
-
competitive, determination of binding structures, bound inhibitor protects against proteolytic inactivation by trypsin or chymotrypsin and specifically alters the proteolytic cleavage pattern
Pseudomonic acid
-, Q8L1B1
i.e. muciproin
purineriboside
-
i.e. nebularin
pyridoxal 5'-diphospho-5'-adenosine
-
affinity labeling reagent for the ATP-binding site, incubation of the reagent with IleRS results in a rapid loss of tRNAIle aminoacylation and isoleucine-dependent isotopic ATP-PPi exchange activities
Reveromycin A
-
IC50 (ng/ml): 2.95. Cell death inducibility of osteoclasts (microgram/ml): 0.06
Reveromycin A 1-methyl ester
-
IC50 (ng/ml): 211. Cell death inducibility of osteoclasts (microgram/ml): 2
Reveromycin A 24-methyl ester
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 3.1
Reveromycin B
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 15
SB-203207
-
anti-infective agent, isolated from Streptomyces NCIMB 40513, analogous to the reaction intermediate
SB-205952
-
a semisynthetic analogue of monic acid, possesing a nitrofuryl chromophore
SB-205952
-
a semisynthetic analogue of monic acid
spermine
-
catalyzes ATP-diphosphate exchange, no inhibition of specific aminoacylation of tRNAIle
Spirofungin A
-
IC50 (ng/ml): 564.5. Cell death inducibility of osteoclasts (microgram/ml): above 30
Spirofungin B
-
IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 30
thiaisoleucine
-
directly competes with isoleucine for a target, irreversible inhibition, inhibits ring-stage parasites in development
-
tRNA
-
partly inhibits the binding of diphosphate
Trypsin
-
proteolytic inactivation patterns, bound Ile-AMP or inhibitors isoleucinol adenylate and pseudomonic acid protect, 50fold higher concentration is needed for digestion of Ile-AMP-enzyme complex than for the free enzyme at 37C
-
Mg2+
-
in presence of 50 mM K+ and in absence of polyamines, the optimal Mg2+ concentration for Ile-tRNA formation is 1 mM, an increase in Mg2+ concentration markedly inhibits
additional information
-
diverse analogues of SB-203207 are not inhibitory, overview
-
additional information
-
inhibition mechanism and structural determinants
-
additional information
-
the ribose of ATP/AMP can be substituted by its biosteres acyclic amide, hydroxamate, dihydroisooxazole, and dihydrooxazole, binding structure, overview
-
additional information
-, Q8L1B1
no inhibition of isozyme IleRS-R2 by pseudomonic acid, i.e. muciproin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
spermidine
-
at least 2 bound Mg2+ or spermidines required for binding of tRNA to the enzyme
spermidine
-
activates
spermidine
-
in presence of 50 mM K+, addition of spermine prevents inhibitory effect of 1.5 mM Mg2+ or above. In presence of 200 mM K+, the addition of spermine stimulates isoleucyl-tRNA formation in presence of Mg2+, 0-5 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00028
-
ATP
-
-
0.00054
-
ATP
-
wild-type enzyme
0.007
-
ATP
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R1
0.01
-
ATP
-, Q8L1B1
pH 7.5, native isozyme IleRS-R2
0.24
-
ATP
-
tRNAIle aminoacylation reaction, pH 7.9, 22C
0.285
-
ATP
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R2
0.33
-
ATP
-, Q8L1B1
pH 7.5, native isozyme IleRS-R2
0.6
-
ATP
-
pH 7.5, 37C, mutant T243R/D342A, in presence of tRNA
0.7
-
ATP
-
wild-type enzyme
0.7
-
ATP
-
pH 7.5, 37C, mutant T234R, in presence of tRNA
2.4
-
ATP
-
pH 7.5, 37C, mutant D342A, in presence of tRNA
4.4
-
ATP
-
pH 7.5, 37C, wild-type IleRS, in presence of tRNA
0.0036
-
Ile
-
-
0.0052
-
Ile
-
wild-type enzyme
1.3
-
Ile
-
wild-type enzyme
0.00125
-
L-isoleucine
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R1
0.005
-
L-isoleucine
-
tRNAIle aminoacylation reaction, pH 7.9, 22C
0.01
-
L-isoleucine
-
ATP-diphosphate exchange reaction, pH 7.9, 22C
0.012
-
L-isoleucine
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R2
0.118
-
L-isoleucine
P41368
mutant enzyme
0.0001
-
tRNAIle
-
-
0.0001
-
tRNAIle
-
below, tRNAIle aminoacylation reaction, pH 7.9, 22C
0.0001
-
tRNAIle
-
below, pH 7.9, 22C
0.0021
-
tRNAIle
-
wild-type enzyme
52.8
-
L-isoleucine
-
pH 8.0, 65C, recombinant wild-type enzyme
additional information
-
additional information
-
Km value of mutant enzynes with altered metal-binding sites
-
additional information
-
additional information
-
Km value of structural analogs of adenosine 5'-triphosphate in the aminoacylation reaction
-
additional information
-
additional information
-
reaction kinetics
-
additional information
-
additional information
-
steady-state parameters for tRNA-independent pre-transfer editing by IleRS and its mutants determined by varying concentrations of noncognate valine, overview. Kinetic method to distinguish among three models for pre-transfer editing by IleRS, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.29
-
ATP
-
pH 7.5, 37C, mutant T243R/D342A, in presence of tRNA
0.48
-
ATP
-
pH 7.5, 37C, mutant D342A, in presence of tRNA
1.04
-
ATP
-
pH 7.5, 37C, mutant T234R, in presence of tRNA
1.56
-
ATP
-
pH 7.5, 37C, wild-type IleRS, in presence of tRNA
80.4
-
ATP
-
wild-type enzyme
27.7
-
Isoleucine
-
wild-type enzyme
104
-
Isoleucine
-
wild-type enzyme
0.18
-
L-isoleucine
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R1
0.35
-
L-isoleucine
-
tRNAIle aminoacylation reaction, pH 7.9, 22C
2.64
-
L-isoleucine
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R2
3
6
L-isoleucine
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R2
3.3
-
L-isoleucine
-, Q8L1B1
pH 7.5, native isozyme IleRS-R2
4.63
-
L-isoleucine
-, Q8L1B1
pH 7.5, native isozyme IleRS-R2
18
-
L-isoleucine
-
ATP-diphosphate exchange reaction, pH 7.9, 22C
3.1
-
tRNAIle
-
wild-type enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.2
-
ATP
-
pH 7.5, 37C, mutant D342A, in presence of tRNA
22040
0.35
-
ATP
-
pH 7.5, 37C, wild-type IleRS, in presence of tRNA
22040
0.48
-
ATP
-
pH 7.5, 37C, mutant T243R/D342A, in presence of tRNA
22040
1.49
-
ATP
-
pH 7.5, 37C, mutant T234R, in presence of tRNA
22040
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4e-05
-
ethyl monate-A
-
pH 7.9, 22C
3e-06
-
Ile-NHSO2-AMP
-
pH 7.9, 22C
3e-05
-
Ile-ol-AMP
-
pH 7.9, 22C
3e-05
-
isoleucinol adenylate
-
pH 7.9, 22C, in complex with the enzyme and Ile, in analogy to the reaction intermediate
0.00025
-
muciproin
-
pH 8.0, 65C, recombinant wild-type enzyme, with respect to L-isoleucine
0.0023
-
muciproin
P41368
mutant enzyme
1e-06
-
Pseudomonic acid
-
pH 7.9, 22C, in complex with the enzyme and Ile, in analogy to the reaction intermediate
1.05e-05
-
Pseudomonic acid
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R1, versus L-isoleucine
1.5e-05
-
Pseudomonic acid
-, Q8L1B1
pH 7.5, recombinant isozyme IleRS-R1, versus ATP
2e-05
-
Pseudomonic acid
-
pH 7.9, 22C
4.5e-05
-
SB-205952
-
pH 7.9, 22C
9e-05
-
isoleucinyl-adenylate
-
pH 7.9, 22C
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
inhibition kinetics
-
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0064
-
2,3-dideoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.0064 mM
0.28
-
2-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.28 mM
0.035
-
3-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.035 mM
0.000265
-
adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamate
-
IC50: 0.000265 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00084
-
-
-
0.05
-
-
-
0.06
-
-
-
0.97
-
-
-
additional information
-
-
-
additional information
-
-
rate constants for hydrolysis and transfer of a noncognate intermediate are roughly equal in IleRS
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.3
-
Q45477
activity assay
7.5
-
-, Q8L1B1
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-
assay at, aminoacylation and deacylation reactions
8.5
-
-
-
additional information
-
-
pH-dependence of enzyme-substrate complex formation
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8.8
-
about 30% of maximal activity at pH 6.0 and 8.8
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
Q45477
activity assay at room temperature
37
-
-
assay at
37
-
-
assay at, aminoacylation and deacylation reactions
45
-
-
formation of isoleucyl-tRNA
62
-
-
isoleucine-tRNA formation with E. coli tRNA
65
-
-
isoleucine-dependent ATP-diphosphate exchange reaction
75
-
-
isoleucine tRNA formation with Thermus thermophilus tRNA
80
-
-
isoleucine dependent ATP-diphosphate exchange
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
cell line LCC-RK1
Manually annotated by BRENDA team
-
cell line CRL-1781
Manually annotated by BRENDA team
additional information
-
the cytoplasmic isozyme gene is expressed during the erythrocytic stages and is localized in the proper compartment for the bulk of protein synthesis, while the apicoplast isozyme is expressed at low rates in the erythrocytic stage and gets more abundant in later developmental stages, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
major part, enzyme participates in a multienzyme complex, not as large and stable as the one from nucleus
Manually annotated by BRENDA team
-
1.3% of total activity in the cell, enzyme participates in a large and stable multienzyme complex
Manually annotated by BRENDA team
-
0.32% of total activity in the cell, enzyme participates in a large and stable multienzyme complex
Manually annotated by BRENDA team
additional information
-
two IRS isozymes localize to distinct compartments in the parasite
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
102000
-
-
sedimentation equilibrium measurement
115000
-
-
disc gel electrophoresis
115000
-
-
gel filtration
115000
-
-
HPLC gel filtration
200000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 139000, SDS-PAGE
?
-, Q8L1B1
x * 117000-117738, native isozyme IleRS-R2, SDS-PAGE and amino acid sequence determination
?
Pseudomonas fluorescens NCIB10586
-
x * 117000-117738, native isozyme IleRS-R2, SDS-PAGE and amino acid sequence determination
-
monomer
-
1 * 103000, SDS-PAGE
monomer
-
1 * 129000, SDS-PAGE
monomer
Escherichia coli MRE600
-
1 * 103000, SDS-PAGE
-
additional information
-
aggregation of aminoacyl-tRNA synthetases into a multienzyme complex
additional information
-
high molecular mass aminoacyl-tRNA synthetase complex with a coherent structure that can be visualized by electron microscopy
additional information
-
the amino acid editing site for IleRS resides within the homologous CP1 domain: threonine-rich peptide and a second conserved GTG region that are separated by about 100 amino acids comprise parts of the hydrolytic editing site, comparison to LeuRS, some positions of the site are idiosyncratic to IleRS, tertiary and primary structure analysis of the amino acid editing site, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
analysis of the crystal structure with bound muciproin, PDB ID: 1FFY
P41972
purified recombinant enzyme cocrystallized with Escherichia coli tRNAIle and inhibitor muciproin, formation of the socalled editing complex, X-ray diffraction structure determination at 2.2 A resolution, and structure analysis
P41972
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
-
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
-
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
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
-
-
stable below
77
-
-
half-life is 15 min, inactivation is completely suppressed by addition of either E. coli or Thermus thermophilus tRNA
additional information
-
-
isoleucine, isoleucine + ATP and tRNA + Mg2+ protect against heat inactivation, some protection by high concentrations of valine
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-15C, 50% glycerol
-
-20C, 50% glycerol
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using M2-FLAG resin
Q45477
recombinant His-tagged IleRS from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
native enzyme, and recombinant enzyme from Escherichia coli, amino acid sequence determination
-, Q8L1B1
recombinant His-tagged wild-type and mutants enzymes from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
into the vector pET3D-FLAG for expression in Escherichia coli BL21DE3 cells
Q45477
overexpression of His-tagged IleRS in Escherichia coli strain BL21 (DE3)
-
with the pCR2.1-TOPO TA cloning kit for sequencing
-
genotyping of thiaisoleucine-resistant enzymes, expression of GFP-tagged cytoplasmic isozyme in erythrocytic stage parasite
-
gene ileS2, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strains DH5alpha and Ts331 mediates resistance against pseudomonic acid, complementation of the ileS-deficient strain Ts331
-, Q8L1B1
expression in Escherichia coli
-
gene ileS, quantitative real-time PCR expression analysis
-
expression of His-tagged wild-type and mutants enzymes in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AIleRS
-
mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity
D342A
-
site-directed mutagenesis, the IleRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
T243R
-
site-directed mutagenesis, the mutant retains tRNA-independent editing at a level identical to the WT enzyme and shows increased ATP hydrolysis compared to the wild-type enzyme
T243R/D342A
-
site-directed mutagenesis, the IleRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations
L810F
-
naturally occuring mutation in the cytoplasmic IleRS responsible for thiaisoleucine-resistance in the parasite, phenotype, overview
P184T
-
naturally occuring mutation that restores fitness in mupirocin resistant strains
Q420H
-
naturally occuring mutation that restores fitness in mupirocin resistant strains
F227L
P41972
the naturally occuring mutation affects the muciprocin binding
H581L/L583H
P41368
site-directed mutagenesis, slightly reduced enzyme activity
K226T
P41972
the naturally occuring mutation affects the muciprocin binding
P187F
P41972
the naturally occuring mutation affects the muciprocin binding
Q612H
P41972
the naturally occuring mutation is involved in stabilizing the conformation of the catalytic loop containing the KMSKS motif
V588F
P41972
the naturally occuring mutation affects the Rossman fold and leads to low-level mupirocin resistance
V767D
P41972
the naturally occuring mutation affects the muciprocin binding
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
IleRS(C922S)
-
mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity
additional information
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pseudomonic acid resistant mutant strain PS102
additional information
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mutant enzymes with altered metal-binding sites
G590D
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pseudomonic-acid resistant mutant MBT10, with a Gly590 to aspartic acid transition
additional information
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pseudomonic acid-resistant mutant
G590D
Methanothermobacter thermautotrophicus Marburg
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pseudomonic-acid resistant mutant MBT10, with a Gly590 to aspartic acid transition
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additional information
Methanothermobacter thermautotrophicus Marburg
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pseudomonic acid-resistant mutant
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
molecular biology
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enzyme is a target for receptor-guided inhibitor design
drug development
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isoleucine utilization is an essential pathway that can be targeted for antimalarial drug development
medicine
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four hundred nine methicillin-resistant Staphylococcus aureus (MRSA) clinical isolates collected in 2006 and 2007 at Madigan Army Medical Center are screened for mupirocin resistance by E test and polymerase chain reaction. No trend of increased mupirocin resistance is found when compared with subsequent years. These results show that mupirocin remains a valid infection control measure due to its unique mechanism of action and the high susceptibility rate of MRSA isolates