Information on EC 6.1.1.5 - Isoleucine-tRNA ligase:
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EC NUMBERCOMMENTARY
6.1.1.5-

RECOMMENDED NAMEGeneOntology No.
Isoleucine-tRNA ligaseGO:0004822

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM 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-pongSaccharomyces cerevisiae-472
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		-Staphylococcus aureus-650527, 651904, 651905, 652205
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		-Rattus norvegicus-650527
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		-Escherichia coli-650559, 650560, 650564
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		reaction kinetics and mechanismStaphylococcus aureus-651903
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		-Cricetulus griseus, Oryctolagus cuniculus-652046
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		substrate recognition mechanism, Glu551, Thr48, His581 and Lys594are involvedThermus thermophilus-652205
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		-Pseudomonas fluorescensQ8L1B1652415
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 Thr230Thermus thermophilus-652566
ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		active site structure and mechanismStaphylococcus aureusP41972653886

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
aminacylation----
aminacylationStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
aminacylationRattus norvegicus--650527
aminacylationEscherichia coli--650559, 650560, 650564
aminacylationThermus thermophilus--652205, 652566
aminacylationPseudomonas fluorescensQ8L1B1-652415
AminoacylationCricetulus griseus, Oryctolagus cuniculus--652046
AminoacylationBacillus subtilisQ45477-704642
AminoacylationMethanopyrus kandleri--705210
AminoacylationEscherichia coli--706028
deacylation----
deacylationStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
deacylationRattus norvegicus--650527
deacylationEscherichia coli--650559, 650560, 650564
deacylationThermus thermophilus--652205, 652566
deacylationPseudomonas fluorescensQ8L1B1-652415
esterification----
esterificationStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
esterificationRattus norvegicus--650527
esterificationEscherichia coli--650559, 650560, 650564
esterificationCricetulus griseus, Oryctolagus cuniculus--652046
esterificationThermus thermophilus--652205, 652566
esterificationPseudomonas fluorescensQ8L1B1-652415

PATHWAYKEGG LinkMetaCyc Link
tRNA charging-TRNA-CHARGING-PWY

SYSTEMATIC NAMEIUBMB Comments
L-Isoleucine:tRNAIle ligase (AMP-forming)-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
Ile-tRNA synthetaseMethanopyrus kandleri--705210
IleRS----
IleRSStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886, 675256
IleRSRattus norvegicus--650527
IleRSEscherichia coli--650559, 650560, 650564, 664321, 672235, 706028, 715519
IleRSCricetulus griseus, Oryctolagus cuniculus--652046
IleRSThermus thermophilus--652205, 652566, 675388
IleRSPseudomonas fluorescensQ8L1B1-652415
IleRSHomo sapiens--691288
IleRSBacillus subtilisQ45477-704642
IleRSMethanopyrus kandleri--705210
IleRSSalmonella enterica--715118
IRS----
IRSStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
IRSRattus norvegicus--650527
IRSEscherichia coli--650559, 650560, 650564
IRSCricetulus griseus, Oryctolagus cuniculus--652046
IRSThermus thermophilus--652205, 652566
IRSPseudomonas fluorescensQ8L1B1-652415
Isoleucine translase----
Isoleucine translaseStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
Isoleucine translaseRattus norvegicus--650527
Isoleucine translaseEscherichia coli--650559, 650560, 650564
Isoleucine translaseCricetulus griseus, Oryctolagus cuniculus--652046
Isoleucine translaseThermus thermophilus--652205, 652566
Isoleucine translasePseudomonas fluorescensQ8L1B1-652415
Isoleucine--tRNA ligase----
Isoleucine--tRNA ligaseStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
Isoleucine--tRNA ligaseRattus norvegicus--650527
Isoleucine--tRNA ligaseEscherichia coli--650559, 650560, 650564
Isoleucine--tRNA ligaseCricetulus griseus, Oryctolagus cuniculus--652046
Isoleucine--tRNA ligaseThermus thermophilus--652205, 652566
Isoleucine--tRNA ligasePseudomonas fluorescensQ8L1B1-652415
Isoleucine-transfer RNA ligase----
Isoleucine-transfer RNA ligaseStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
Isoleucine-transfer RNA ligaseRattus norvegicus--650527
Isoleucine-transfer RNA ligaseEscherichia coli--650559, 650560, 650564
Isoleucine-transfer RNA ligaseCricetulus griseus, Oryctolagus cuniculus--652046
Isoleucine-transfer RNA ligaseThermus thermophilus--652205, 652566
Isoleucine-transfer RNA ligasePseudomonas fluorescensQ8L1B1-652415
Isoleucine-tRNA synthetase----
Isoleucine-tRNA synthetaseStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
Isoleucine-tRNA synthetaseRattus norvegicus--650527
Isoleucine-tRNA synthetaseEscherichia coli--650559, 650560, 650564
Isoleucine-tRNA synthetaseCricetulus griseus, Oryctolagus cuniculus--652046
Isoleucine-tRNA synthetaseThermus thermophilus--652205, 652566
Isoleucine-tRNA synthetasePseudomonas fluorescensQ8L1B1-652415
isoleucyl tRNA synthetaseHomo sapiens--691288
isoleucyl tRNA synthetaseStaphylococcus aureus--693190
Isoleucyl-transfer ribonucleate synthetase----
Isoleucyl-transfer ribonucleate synthetaseStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
Isoleucyl-transfer ribonucleate synthetaseRattus norvegicus--650527
Isoleucyl-transfer ribonucleate synthetaseEscherichia coli--650559, 650560, 650564
Isoleucyl-transfer ribonucleate synthetaseCricetulus griseus, Oryctolagus cuniculus--652046
Isoleucyl-transfer ribonucleate synthetaseThermus thermophilus--652205, 652566
Isoleucyl-transfer ribonucleate synthetasePseudomonas fluorescensQ8L1B1-652415
Isoleucyl-transfer RNA synthetase----
Isoleucyl-transfer RNA synthetaseStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
Isoleucyl-transfer RNA synthetaseRattus norvegicus--650527
Isoleucyl-transfer RNA synthetaseEscherichia coli--650559, 650560, 650564
Isoleucyl-transfer RNA synthetaseCricetulus griseus, Oryctolagus cuniculus--652046
Isoleucyl-transfer RNA synthetaseThermus thermophilus--652205, 652566
Isoleucyl-transfer RNA synthetasePseudomonas fluorescensQ8L1B1-652415
Isoleucyl-tRNA synthetase----
Isoleucyl-tRNA synthetaseStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886, 675256
Isoleucyl-tRNA synthetaseRattus norvegicus--650527
Isoleucyl-tRNA synthetaseEscherichia coli--650559, 650560, 650564, 672235, 706028, 715519
Isoleucyl-tRNA synthetaseCricetulus griseus, Oryctolagus cuniculus--652046
Isoleucyl-tRNA synthetaseThermus thermophilus--652205, 652566, 675388
Isoleucyl-tRNA synthetasePseudomonas fluorescensQ8L1B1-652415
Isoleucyl-tRNA synthetaseBacillus subtilisQ45477-704642
Isoleucyl-tRNA synthetaseMethanopyrus kandleri--705210
Isoleucyl-tRNA synthetaseSalmonella enterica--715118
Mupirocin resistance protein----
Mupirocin resistance proteinStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
Mupirocin resistance proteinRattus norvegicus--650527
Mupirocin resistance proteinEscherichia coli--650559, 650560, 650564
Mupirocin resistance proteinCricetulus griseus, Oryctolagus cuniculus--652046
Mupirocin resistance proteinThermus thermophilus--652205, 652566
Mupirocin resistance proteinPseudomonas fluorescensQ8L1B1-652415
Synthetase, isoleucyl-transfer ribonucleate----
Synthetase, isoleucyl-transfer ribonucleateStaphylococcus aureus--650527, 651903, 651904, 651905, 652205, 653886
Synthetase, isoleucyl-transfer ribonucleateRattus norvegicus--650527
Synthetase, isoleucyl-transfer ribonucleateEscherichia coli--650559, 650560, 650564
Synthetase, isoleucyl-transfer ribonucleateCricetulus griseus, Oryctolagus cuniculus--652046
Synthetase, isoleucyl-transfer ribonucleateThermus thermophilus--652205, 652566
Synthetase, isoleucyl-transfer ribonucleatePseudomonas fluorescensQ8L1B1-652415
Isoleucyl-tRNA synthetasePlasmodium falciparum--716781
additional informationEscherichia coli-the enzyme is a class I aminoacyl-tRNA synthetase715519

CAS REGISTRY NUMBERCOMMENTARY
9030-96-0-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bacillus subtilisstrain 168704642Q45477UniProtManually annotated by BRENDA team
Bacillus subtilis 168strain 168704642Q45477UniProtManually annotated by BRENDA team
Cricetulus griseus-652046--Manually annotated by BRENDA team
Escherichia coli-448, 449, 451, 453, 455, 456, 461, 462, 467, 471, 650559, 650560, 650564, 664321, 672235, 715519--Manually annotated by BRENDA team
Escherichia coliB454, 463, 468--Manually annotated by BRENDA team
Escherichia coliB; K12465--Manually annotated by BRENDA team
Escherichia coliMRE600464, 476--Manually annotated by BRENDA team
Escherichia colistrain EM20031706028--Manually annotated by BRENDA team
Escherichia coliwild-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 activity450--Manually annotated by BRENDA team
Escherichia coliwild-type and mutant enzymes with altered metal-binding sites452--Manually annotated by BRENDA team
Escherichia coliwild-type strain MC4100 and pseudomonic acid resistant mutant strain PS102447--Manually annotated by BRENDA team
Escherichia coli EM20031strain EM20031706028--Manually annotated by BRENDA team
Geobacillus stearothermophilus-460, 461--Manually annotated by BRENDA team
Haloarcula marismortui-125--Manually annotated by BRENDA team
Homo sapiens-691288--Manually annotated by BRENDA team
Methanopyrus kandlerithe 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 ocean705210--Manually annotated by BRENDA team
Methanothermobacter thermautotrophicuspseudomonic acid-resistant mutant; strain Marburg475--Manually annotated by BRENDA team
Methanothermobacter thermautotrophicusstrain Marburg; wild-type end pseudomonic-acid resistant mutant MBT10, with a Gly590 to aspartic acid transition459--Manually annotated by BRENDA team
Mus musculus-126--Manually annotated by BRENDA team
Oryctolagus cuniculus-652046--Manually annotated by BRENDA team
Ovis aries-474--Manually annotated by BRENDA team
Plasmodium falciparumtwo isozymes, an apicoplast isozyme encoded by gene PFL1210w, and a cytoplasmic isozyme encoded by gene PF13_0179716781--Manually annotated by BRENDA team
Pseudomonas fluorescensstrain NCIB10586, gene ileS1, pseudomonic acid-sensitive isozyme IleRS-R1, recombinant enzyme expressed in Escherichia coli652415--Manually annotated by BRENDA team
Pseudomonas fluorescensstrain NCIB10586, pseudomonic acid-resistant isozyme IleRS-R2, gene ileS2652415Q8L1B1SwissProtManually annotated by BRENDA team
Pseudomonas fluorescens NCIB10586strain NCIB10586, gene ileS1, pseudomonic acid-sensitive isozyme IleRS-R1, recombinant enzyme expressed in Escherichia coli652415--Manually annotated by BRENDA team
Pseudomonas fluorescens NCIB10586strain NCIB10586, pseudomonic acid-resistant isozyme IleRS-R2, gene ileS2652415Q8L1B1SwissProtManually annotated by BRENDA team
Rattus norvegicus-470, 650527--Manually annotated by BRENDA team
Saccharomyces cerevisiae-458, 469, 472, 476--Manually annotated by BRENDA team
Saccharomyces cerevisiaeexpression in Escherichia coli457--Manually annotated by BRENDA team
Salmonella entericagene ileS715118--Manually annotated by BRENDA team
Staphylococcus aureus-651903, 651904, 693190--Manually annotated by BRENDA team
Staphylococcus aureus-652205P41368UniprotManually annotated by BRENDA team
Staphylococcus aureus-653886P41972UniprotManually annotated by BRENDA team
Staphylococcus aureusmethicillin-resistant clinical isolates from humans, gene ileS675256P41972UniprotManually annotated by BRENDA team
Staphylococcus aureuspurified recombinant enzyme expressed in Escherichia coli strain DH1651905--Manually annotated by BRENDA team
Staphylococcus aureusstrain WCUH29650527--Manually annotated by BRENDA team
Staphylococcus aureus WCUH29strain WCUH29650527--Manually annotated by BRENDA team
Thermus thermophilus-652566, 675388P56690UniprotManually annotated by BRENDA team
Thermus thermophilusHB8466, 67--Manually annotated by BRENDA team
Thermus thermophilusstrain HB8, purified recombinant wild-type and mutant enzyme652205--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionEscherichia coli-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 important715519
additional informationSalmonella enterica-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, overview715118
additional informationPlasmodium falciparum-thiaisoleucine-resistant parasites possess a mutation in the cytoplasmic isoleucyl-tRNA synthetase, mutational analysis, overview716781

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--664321--?
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilus--67-67-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilus--466-466-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilus--652205-652205?
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--447-447-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--448-448-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--449-449-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--450-450-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--452-452-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--453-453-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--454-454-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--455-455-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--456-456-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--461-461-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--462-462-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--463-463-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--464-464-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--465-465-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--467-467-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--468-468-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--471-471-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--476-476-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--650560-650560?
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--650564-650564?
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Rattus norvegicus--470-470-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Saccharomyces cerevisiae--458-458-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Saccharomyces cerevisiae--469-469-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Saccharomyces cerevisiae--472-472-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Saccharomyces cerevisiae--476-476-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Geobacillus stearothermophilus--461-461-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Methanothermobacter thermautotrophicus--459-459-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Methanothermobacter thermautotrophicus--475-475-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Ovis aries--474-474-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Geobacillus stearothermophilus-0.3% or less of the activity with isoleucine is measured with other amino acids460-460-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli-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 methionine451-451-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Saccharomyces cerevisiae-enzyme has specificity for E. coli tRNAIle457-457-
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilus-enzyme shows a common recognition mode of aminoacyl-adenylate for a class I aminoacyl-tRNA synthetase, formation of high-energy reaction intermediate Ile-AMP652205-652205?
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli-formation of an aminoacyl adenylate reaction intermediate650564-650564?
ATP + isoleucine + tRNAIle?
show the reaction diagram		Escherichia coli-physiological function is Thr formation of Ile-tRNA and editing of inadvertently misactivated homocysteine449---
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Cricetulus griseus--652046-652046?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus--650527-650527?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureusP41368-652205-652205?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureusP41972-653886-653886?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureusP41972-675256--?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus--651903-651903r
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus--651904-651904r
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus--651905-651905r
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilus--675388--?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilusP56690-652566-652566r
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--650559-650559?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--672235, 706028, 715519--?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Rattus norvegicus--650527-650527?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Oryctolagus cuniculus--652046-652046?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Pseudomonas fluorescensQ8L1B1-652415-652415?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Methanopyrus kandleri--705210--?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus-formation of a enzyme-bound aminoacyl adenylate intermediate651903-651903r
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus-reaction intermediate is the Ile-AMP-enzyme complex651905-651905r
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli-the binding region of the adenine moiety contains a wide hydrophobic pocket large enough to afford three linear aromatic rings650559-650559?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Pseudomonas fluorescensQ8L1B1tRNAIle from Pseudomonas fluorescens and Escherichia coli652415-652415?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Oryctolagus cuniculus-the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm652046-652046?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Cricetulus griseus-the reaction plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm652046-652046?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli-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,overview672235--?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilus-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 important675388--?
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Bacillus subtilisQ45477bacteria 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 IleRS704642--?
ATP + L-valine + tRNAIleAMP + diphosphate + L-valyl-tRNAIle
show the reaction diagram		Thermus thermophilusP56690-652566CP1 domain of the enzyme deacylates or edits the mischarged Val-tRNAIle652566r
Formycin 5'-triphosphate + isoleucine + tRNAIle?
show the reaction diagram		Saccharomyces cerevisiae--469---
Ile-tRNAIle + 3-mercaptopropionateS-Isoleucyl-3-mercaptopropionate + tRNAIle
show the reaction diagram		Escherichia coli--449-449-
Ile-tRNAIle + cysteaminetRNAIle + isoleucylcysteamine
show the reaction diagram		Escherichia coli--449-449-
Ile-tRNAIle + cysteinetRNAIle + isoleucylcysteine
show the reaction diagram		Escherichia coli-D- and L-isomer of Lys449D-isoleucylcysteine and L-isoleucylcysteine449-
Ile-tRNAIle + DTTThioester of Ile and DTT + tRNAIle
show the reaction diagram		Escherichia coli--449-449-
Ile-tRNAIle + L-cysteine methyl estertRNAIle + isoleucyl-L-cysteine methyl ester
show the reaction diagram		Escherichia coli--449-449-
Tubercidin 5'-triphosphate + isoleucine + tRNAIle?
show the reaction diagram		Saccharomyces cerevisiae--469---
Ile-tRNAIle + N-acetylcysteineS-Isoleucyl-N-acetylcysteine + tRNAIle
show the reaction diagram		Escherichia coli--449-449-
additional information?-Saccharomyces cerevisiae-position 2,6,7,8,9,2' and 3' of ATP are important for catalytic action of isleucyl-tRNA synthetase469---
additional information?-Escherichia coli, Saccharomyces cerevisiae-discrimination of 20 amino acids in aminoacylation of modified tRNAIle-C-C-A(3'NH2)476---
additional information?-Thermus thermophilus-Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphoshate exchange466---
additional information?-Escherichia coli-Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphoshate exchange450, 453, 454, 462---
additional information?-Saccharomyces cerevisiae-Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphoshate exchange472---
additional information?-Geobacillus stearothermophilus-Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphoshate exchange460---
additional information?-Staphylococcus aureus-enzyme also performs the reversible ATP-diphosphate exchange reaction651903-651903?
additional information?-Staphylococcus aureus-enzyme also performs the reversible ATP-diphosphate exchange reaction651904-651904?
additional information?-Staphylococcus aureus-enzyme also performs the reversible ATP-diphosphate exchange reaction651905-651905?
additional information?-Cricetulus griseus, Oryctolagus cuniculus-aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I652046-652046?
additional information?-Thermus thermophilus-Thr233 and His319 recognize the substrate valine side-chain, regardless of the valine side-chain rotation, and reject the isoleucine side-chain675388---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilus--652205-652205
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--650560-650560
ATP + isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--650564-650564
ATP + isoleucine + tRNAIle?
show the reaction diagram		Escherichia coli-physiological function is Thr formation of Ile-tRNA and editing of inadvertently misactivated homocysteine449--
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus--650527-650527
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureusP41368-652205-652205
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureusP41972-653886-653886
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureusP41972-675256--
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus--651903-651903
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus--651904-651904
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Staphylococcus aureus--651905-651905
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilus--675388--
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Thermus thermophilusP56690-652566-652566
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--650559-650559
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Escherichia coli--672235, 706028, 715519--
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Rattus norvegicus--650527-650527
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Pseudomonas fluorescensQ8L1B1-652415-652415
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Methanopyrus kandleri--705210--
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Oryctolagus cuniculus-the reaction catalyzed by the enzyme plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm652046-652046
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Cricetulus griseus-the reaction plays an important role in the transport of aminoacylated tRNAs from the nucleus to the cytoplasm652046-652046
ATP + L-isoleucine + tRNAIleAMP + diphosphate + L-isoleucyl-tRNAIle
show the reaction diagram		Bacillus subtilisQ45477bacteria 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 IleRS704642--
additional information?-Cricetulus griseus, Oryctolagus cuniculus-aminoacyl-tRNA is channeled in vivo by probably direct transfer to elongation factor I652046-652046

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
ATPStaphylococcus aureus--650527, 651904, 652205, 653886, 675256 2D-image
ATPRattus norvegicus--650527 2D-image
ATPEscherichia coli--650559, 650560, 650564, 672235, 706028, 715519 2D-image
ATPStaphylococcus aureus-binds more tightly to the enzyme-Ile complex than to the free enzyme651903 2D-image
ATPStaphylococcus aureus-dependent on, MgATP2-651905 2D-image
ATPCricetulus griseus, Oryctolagus cuniculus--652046 2D-image
ATPThermus thermophilus--652205, 652566, 675388 2D-image
ATPPseudomonas fluorescensQ8L1B1-652415 2D-image
ATPBacillus subtilisQ45477-704642 2D-image
ATPMethanopyrus kandleri--705210 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ce3+Escherichia coli-activates462
CobaltEscherichia coli-cobalt-substituted enzyme is active455
Dy3+Escherichia coli-activates462
Eu3+Escherichia coli-activates462
Gd3+Escherichia coli-activates462
La3+Escherichia coli-activates462
Mg2+Escherichia coli-at least 2 bound Mg2+ or spermidines required for the binding of tRNA to the enzyme454
Mg2+Geobacillus stearothermophilus-at a concentration of ATP and diphosphate of 3 mM, the optimal Mg2+ concentration is 6-10 mM; required460
Mg2+Escherichia coli-optimum at very low concentration (0.5-0.7 mM), slight inhibition at higher concentration461
Mg2+Geobacillus stearothermophilus-optimal concentration is 5-6 mM461
Mg2+Escherichia coli-activates isoleucyl-tRNA formation462
Mg2+Escherichia coli-activates isoleucyl-tRNA formation; enzyme-bound isoleucyl-AMP can be formed in the absence of Mg2+ and spermine; synergistic effect with spermine465
Mg2+Thermus thermophilus-optimal concentration is 10 mM; required466
Mg2+Rattus norvegicus-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 inhibits470
Mg2+Staphylococcus aureus-required, MgATP2-651905
Mg2+Escherichia coli--672235
Mg2+Staphylococcus aureusP41972-675256
Mg2+Thermus thermophilus--675388
Mg2+Escherichia coli-assay at715519
Nd3+Escherichia coli-activates462
Pr3+Escherichia coli-activates462
Sm3+Escherichia coli-activates462
Tb3+Escherichia coli-activates462
Yb3+Escherichia coli-activates462
ZincEscherichia coli-bound to a Cys4 cluster at the C-terminal end of the polypeptide; required448
ZincEscherichia coli-2 enzyme bound zinc atoms per polypeptide chain450
ZincEscherichia coli-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 A452
ZincEscherichia coli-2 tightly bound zinc atoms per active site; structural and catalytic role in aminoacylation453
ZincEscherichia coli-contains 1.5-2 mol of Zn bound per mol of polypeptide455
ZincEscherichia coli-zinc containing peptide at the C-terminus456
ZincOvis aries-contains 1 Zn2+ per polypeptide chain474
ZincThermus thermophilus-2 Zn2+ tightly bound67

INHIBITORSORGANISM 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 acidHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 15691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): 560.3. Cell death inducibility of osteoclasts (microgram/ml): not determined691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): 22.9. Cell death inducibility of osteoclasts (microgram/ml): 6.31691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): not determined691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): 497.4. Cell death inducibility of osteoclasts (microgram/ml): 9.6691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): 94.6. Cell death inducibility of osteoclasts (microgram/ml): 11.5691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): 57.9. Cell death inducibility of osteoclasts (microgram/ml): not determined691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): 14.4. Cell death inducibility of osteoclasts (microgram/ml): 1.01691288 2D-image
(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 acidHomo sapiens-IC50 (ng/ml): 292.8. Cell death inducibility of osteoclasts (microgram/ml): 2.5691288 2D-image
1,10-phenanthrolineOvis aries--474 2D-image
2',3'-dialdehyde of tRNAileEscherichia coli-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 activities706028-
2,2'-BipyridylOvis aries--474 2D-image
2,3-dideoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamateEscherichia coli-IC50: 0.0064 mM664321 2D-image
2,3-Dihydro-5-epireveromycin AHomo sapiens-IC50 (ng/ml): 58.3. Cell death inducibility of osteoclasts (microgram/ml): 0.82691288 2D-image
2,3-Dihydroreveromycin AHomo sapiens-IC50 (ng/ml): 11.6. Cell death inducibility of osteoclasts (microgram/ml): 0.22691288 2D-image
2-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamateEscherichia coli-IC50: 0.28 mM664321 2D-image
2-iodo-L-isoleucine-NHSO2-AMPEscherichia coli-highly potent inhibitor, hydrophobic interaction of the 2-substituent of the inhibitor with the adenine binding site of the enzyme650564 2D-image
3'-DeoxyadenosineSaccharomyces cerevisiae-i.e. cordycepin472 2D-image
3-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamateEscherichia coli-IC50: 0.035 mM664321 2D-image
5'-N-[N-(L-isoleucyl)sulfamoyl]adenosineThermus thermophilus-non-hydrolyzable analogue of the reaction intermediate Ile-AMP652205 2D-image
5-acetyl-Reveromycin AHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 0.46691288 2D-image
5-Epireveromycin AHomo sapiens-IC50 (ng/ml): 378.3. Cell death inducibility of osteoclasts (microgram/ml): 21.5691288 2D-image
5-methoxy-Reveromycin AHomo sapiens-IC50 (ng/ml): 374. Cell death inducibility of osteoclasts (microgram/ml): above 15691288 2D-image
5-O-succinyl-Spirofungin AHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 12.4691288 2D-image
5-tert-butyl-dimethylsilyl-Reveromycin AHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 5.9691288 2D-image
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-carboxamideRattus norvegicus-derivative of SB-203207, 10% inhibition at 0.1 mM650527 2D-image
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-carboxamideRattus norvegicus-derivative of SB-203207, 18% inhibition at 0.1 mM650527 2D-image
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-carboxamideStaphylococcus aureus-derivative of SB-203207, 26% inhibition at 0.1 mM650527 2D-image
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-carboxamideRattus norvegicus-derivative of SB-203207, 17% inhibition at 0.1 mM650527 2D-image
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-carboxamideRattus norvegicus, Staphylococcus aureus--650527 2D-image
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 esterRattus norvegicus-derivative of SB-203207, 49% inhibition at 0.1 mM650527 2D-image
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 esterStaphylococcus aureus-derivative of SB-203207, 31% inhibition at 0.1 mM650527 2D-image
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 esterRattus norvegicus-derivative of SB-203207, 46% inhibition at 0.1 mM650527 2D-image
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 esterStaphylococcus aureus-derivative of SB-203207, 34% inhibition at 0.1 mM650527 2D-image
7-[[(S)-2-amino-1-oxo-5-thiahexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamideRattus norvegicus-derivative of SB-203207, 31% inhibition at 0.1 mM650527 2D-image
7-[[(S)-2-amino-1-oxo-5-thiahexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamideStaphylococcus aureus-derivative of SB-203207, 38% inhibition at 0.1 mM650527 2D-image
7-[[(S)-2-amino-1-oxo-hexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamideRattus norvegicus-derivative of SB-203207, 17% inhibition at 0.1 mM650527 2D-image
7-[[(S)-2-amino-1-oxo-hexyl]amino]sulfonylacetyloxy-2,4a,5,6,7,7a-hexahydro-2-methyl-1H-cyclopenta[c]pyridine-4-carboxamideStaphylococcus aureus-derivative of SB-203207, 46% inhibition at 0.1 mM650527 2D-image
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 esterRattus norvegicus-derivative of SB-203207, 31% inhibition at 0.1 mM650527 2D-image
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 esterStaphylococcus aureus-derivative of SB-203207, 38% inhibition at 0.1 mM650527 2D-image
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 esterRattus norvegicus-derivative of SB-203207, 33% inhibition at 0.1 mM650527 2D-image
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 esterStaphylococcus aureus-derivative of SB-203207, 10% inhibition at 0.1 mM650527 2D-image
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 esterRattus norvegicus-derivative of SB-203207, 13% inhibition at 0.1 mM650527 2D-image
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 esterStaphylococcus aureus-derivative of SB-203207, 15% inhibition at 0.1 mM650527 2D-image
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 esterRattus norvegicus-derivative of SB-203207, 14% inhibition at 0.1 mM650527 2D-image
8-AminoadenosineSaccharomyces cerevisiae--472 2D-image
8-azidoadenosine 5'-triphosphateSaccharomyces cerevisiae--472 2D-image
adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamateEscherichia coli-IC50: 0.000265 mM664321 2D-image
bromometyl ketone derivative of L-isoleucineEscherichia coli-labeling reagent706028-
bromometyl ketone derivative of norleucineEscherichia coli-labeling reagent706028-
bromometyl ketone derivative of phenylalanineEscherichia coli-labeling reagent706028-
bromometyl ketone derivative of valineEscherichia coli-labeling reagent706028-
ChymotrypsinStaphylococcus aureus-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 37°C651905-
diethyl dicarbonateEscherichia coli--706028 2D-image
diphosphateEscherichia coli-partly inhibits the binding of tRNA454 2D-image
ester analogues of isoleucyl adenylateEscherichia coli-with or without cyclic substitutents at the adenine moiety650559 2D-image
ethyl monate-AStaphylococcus aureus--651904 2D-image
FuranomycinEscherichia coli--471 2D-image
hydroxamate analogues of isoleucyl adenylateEscherichia coli-with or without cyclic substitutents at the adenine moiety650559 2D-image
Ile-NHSO2-AMPStaphylococcus aureus-non-hydrolyzable reaction intermediate analogue, slow-tight binding, competitive and inhibition mechanism, reversible651904 2D-image
Ile-ol-AMPStaphylococcus aureus--651903 2D-image
isoleucinol adenylateStaphylococcus aureus-determination of binding structures, bound inhibitor protects against proteolytic inactivation by trypsin or chymotrypsin and specifically alters the proteolytic cleavage pattern651905 2D-image
isoleucinyl adenylateStaphylococcus aureus-i.e. Ile-ol-AMP, nonhydrolyzable reaction intermediate analogue, competitive with respect to both ATP and Ile651903 2D-image
isoleucinyl-adenylateStaphylococcus aureus-i.e. Ile-ol-AMP, non-hydrolyzable reaction intermediate analogue, slow-tight binding, competitive and inhibition mechanism, reversible651904 2D-image
isoleucyl isovanilloidsEscherichia coli-e.g. the isovanillic hydroxamate and amide analogue650560 2D-image
isoleucyl sulfamate analoguesEscherichia coli--650564 2D-image
isoleucyl vanilloidsEscherichia coli-e.g. the vanillic hydroxamate with a phenolic hydoxyl at the para-position650560 2D-image
isoleucyl-N'-adenosyl-N'-hydroxy sulfamideEscherichia coli--650564 2D-image
isoleucyl-N'-adenosyloxy sulfamideEscherichia coli--650564 2D-image
K+Thermus thermophilus--466 2D-image
muciproinStaphylococcus aureus--652205, 653886 2D-image
muciproinThermus thermophilus-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 Trp558652205 2D-image
mupirocinStaphylococcus aureusP41972a 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 gene675256 2D-image
mupirocinStaphylococcus aureus--693190 2D-image
mupirocinSalmonella enterica-Mup, an isoleucyl-adenylate analogue that inhibits the essential enzyme, isoleucyl-tRNA synthetase715118 2D-image
mupirocinPlasmodium falciparum-irreversible inhibition, inhibits development of invasion-competent parasites in the second asexual cycle, delayed death phenotype716781 2D-image
Na+Thermus thermophilus--466 2D-image
Pseudomonic acidEscherichia coli-bifunctional inhibitor with characteristics of both isoleucine and ATP447 2D-image
Pseudomonic acidSaccharomyces cerevisiae-pseudomonic acid A: Saccharomyces cerevisiae enzyme is 10000 times less sensitive than Escherichia coli enzyme457 2D-image
Pseudomonic acidMethanothermobacter thermautotrophicus--459 2D-image
Pseudomonic acidEscherichia coli--471 2D-image
Pseudomonic acidMethanothermobacter thermautotrophicus-wild-type enzyme strongly inhibited, pseudomonic acid-resistant mutant only marginally475 2D-image
Pseudomonic acidStaphylococcus aureus-forms a non-hydrolyzable reaction intermediate analogue, competitive inhibition651904 2D-image
Pseudomonic acidStaphylococcus aureus-competitive, determination of binding structures, bound inhibitor protects against proteolytic inactivation by trypsin or chymotrypsin and specifically alters the proteolytic cleavage pattern651905 2D-image
Pseudomonic acidPseudomonas fluorescensQ8L1B1i.e. muciproin652415 2D-image
purineribosideSaccharomyces cerevisiae-i.e. nebularin472 2D-image
pyridoxal 5'-diphospho-5'-adenosineEscherichia coli-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 activities706028 2D-image
Reveromycin AHomo sapiens-IC50 (ng/ml): 2.95. Cell death inducibility of osteoclasts (microgram/ml): 0.06691288 2D-image
Reveromycin A 1-methyl esterHomo sapiens-IC50 (ng/ml): 211. Cell death inducibility of osteoclasts (microgram/ml): 2691288 2D-image
Reveromycin A 24-methyl esterHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): 3.1691288 2D-image
Reveromycin BHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 15691288 2D-image
SB-203207Rattus norvegicus, Staphylococcus aureus-anti-infective agent, isolated from Streptomyces NCIMB 40513, analogous to the reaction intermediate650527 2D-image
SB-205952Staphylococcus aureus-a semisynthetic analogue of monic acid, possesing a nitrofuryl chromophore651904 2D-image
SB-205952Staphylococcus aureus-a semisynthetic analogue of monic acid651905 2D-image
spermineEscherichia coli-catalyzes ATP-diphosphate exchange, no inhibition of specific aminoacylation of tRNAIle463 2D-image
Spirofungin AHomo sapiens-IC50 (ng/ml): 564.5. Cell death inducibility of osteoclasts (microgram/ml): above 30691288 2D-image
Spirofungin BHomo sapiens-IC50 (ng/ml): value above 1000. Cell death inducibility of osteoclasts (microgram/ml): above 30691288 2D-image
thiaisoleucinePlasmodium falciparum-directly competes with isoleucine for a target, irreversible inhibition, inhibits ring-stage parasites in development716781-
tRNAEscherichia coli-partly inhibits the binding of diphosphate454 2D-image
TrypsinStaphylococcus aureus-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 37°C651905-
Mg2+Rattus norvegicus-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 inhibits470 2D-image
additional informationRattus norvegicus, Staphylococcus aureus-diverse analogues of SB-203207 are not inhibitory, overview650527-
additional informationEscherichia coli-inhibition mechanism and structural determinants650559-
additional informationEscherichia coli-the ribose of ATP/AMP can be substituted by its biosteres acyclic amide, hydroxamate, dihydroisooxazole, and dihydrooxazole, binding structure, overview650560-
additional informationPseudomonas fluorescensQ8L1B1no inhibition of isozyme IleRS-R2 by pseudomonic acid, i.e. muciproin652415-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
spermidineEscherichia coli-at least 2 bound Mg2+ or spermidines required for binding of tRNA to the enzyme454 2D-image
spermidineEscherichia coli-activates462 2D-image
spermidineRattus norvegicus-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 mM470 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00028-ATPEscherichia coli--448 2D-image
0.00054-ATPEscherichia coli-wild-type enzyme452 2D-image
0.007-ATPPseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R1652415 2D-image
0.01-ATPPseudomonas fluorescensQ8L1B1pH 7.5, native isozyme IleRS-R2652415 2D-image
0.24-ATPStaphylococcus aureus-tRNAIle aminoacylation reaction, pH 7.9, 22°C651903 2D-image
0.285-ATPPseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R2652415 2D-image
0.33-ATPPseudomonas fluorescensQ8L1B1pH 7.5, native isozyme IleRS-R2652415 2D-image
0.6-ATPEscherichia coli-pH 7.5, 37°C, mutant T243R/D342A, in presence of tRNA715519 2D-image
0.7-ATPEscherichia coli-wild-type enzyme450 2D-image
0.7-ATPEscherichia coli-pH 7.5, 37°C, mutant T234R, in presence of tRNA715519 2D-image
2.4-ATPEscherichia coli-pH 7.5, 37°C, mutant D342A, in presence of tRNA715519 2D-image
4.4-ATPEscherichia coli-pH 7.5, 37°C, wild-type IleRS, in presence of tRNA715519 2D-image
0.0036-IleEscherichia coli--448 2D-image
0.0052-IleEscherichia coli-wild-type enzyme452 2D-image
1.3-IleEscherichia coli-wild-type enzyme450 2D-image
0.00125-L-isoleucinePseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R1652415 2D-image
0.005-L-isoleucineStaphylococcus aureus-tRNAIle aminoacylation reaction, pH 7.9, 22°C651903 2D-image
0.01-L-isoleucineStaphylococcus aureus-ATP-diphosphate exchange reaction, pH 7.9, 22°C651903 2D-image
0.012-L-isoleucinePseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R2652415 2D-image
0.118-L-isoleucineStaphylococcus aureusP41368mutant enzyme652205 2D-image
0.0001-tRNAIleThermus thermophilus--466 2D-image
0.0001-tRNAIleStaphylococcus aureus-below, tRNAIle aminoacylation reaction, pH 7.9, 22°C651903 2D-image
0.0001-tRNAIleStaphylococcus aureus-below, pH 7.9, 22°C651905 2D-image
0.0021-tRNAIleEscherichia coli-wild-type enzyme450 2D-image
52.8-L-isoleucineThermus thermophilus-pH 8.0, 65°C, recombinant wild-type enzyme652205 2D-image
additional information-additional informationEscherichia coli-Km value of mutant enzynes with altered metal-binding sites452-
additional information-additional informationSaccharomyces cerevisiae-Km value of structural analogs of adenosine 5'-triphosphate in the aminoacylation reaction469-
additional information-additional informationStaphylococcus aureus-reaction kinetics651903-
additional information-additional informationEscherichia coli-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, overview715519-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.29-ATPEscherichia coli-pH 7.5, 37°C, mutant T243R/D342A, in presence of tRNA715519 2D-image
0.48-ATPEscherichia coli-pH 7.5, 37°C, mutant D342A, in presence of tRNA715519 2D-image
1.04-ATPEscherichia coli-pH 7.5, 37°C, mutant T234R, in presence of tRNA715519 2D-image
1.56-ATPEscherichia coli-pH 7.5, 37°C, wild-type IleRS, in presence of tRNA715519 2D-image
80.4-ATPEscherichia coli-wild-type enzyme448 2D-image
27.7-IsoleucineEscherichia coli-wild-type enzyme452 2D-image
104-IsoleucineEscherichia coli-wild-type enzyme450 2D-image
0.18-L-isoleucinePseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R1652415 2D-image
0.35-L-isoleucineStaphylococcus aureus-tRNAIle aminoacylation reaction, pH 7.9, 22°C651903 2D-image
2.64-L-isoleucinePseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R2652415 2D-image
36L-isoleucinePseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R2652415 2D-image
3.3-L-isoleucinePseudomonas fluorescensQ8L1B1pH 7.5, native isozyme IleRS-R2652415 2D-image
4.63-L-isoleucinePseudomonas fluorescensQ8L1B1pH 7.5, native isozyme IleRS-R2652415 2D-image
18-L-isoleucineStaphylococcus aureus-ATP-diphosphate exchange reaction, pH 7.9, 22°C651903 2D-image
3.1-tRNAIleEscherichia coli-wild-type enzyme450 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.2-ATPEscherichia coli-pH 7.5, 37°C, mutant D342A, in presence of tRNA71551922040
0.35-ATPEscherichia coli-pH 7.5, 37°C, wild-type IleRS, in presence of tRNA71551922040
0.48-ATPEscherichia coli-pH 7.5, 37°C, mutant T243R/D342A, in presence of tRNA71551922040
1.49-ATPEscherichia coli-pH 7.5, 37°C, mutant T234R, in presence of tRNA71551922040

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4e-05-ethyl monate-AStaphylococcus aureus-pH 7.9, 22°C651904 2D-image
3e-06-Ile-NHSO2-AMPStaphylococcus aureus-pH 7.9, 22°C651904 2D-image
3e-05-Ile-ol-AMPStaphylococcus aureus-pH 7.9, 22°C651903 2D-image
3e-05-isoleucinol adenylateStaphylococcus aureus-pH 7.9, 22°C, in complex with the enzyme and Ile, in analogy to the reaction intermediate651905 2D-image
0.00025-muciproinThermus thermophilus-pH 8.0, 65°C, recombinant wild-type enzyme, with respect to L-isoleucine652205 2D-image
0.0023-muciproinStaphylococcus aureusP41368mutant enzyme652205 2D-image
1e-06-Pseudomonic acidStaphylococcus aureus-pH 7.9, 22°C, in complex with the enzyme and Ile, in analogy to the reaction intermediate651905 2D-image
1.05e-05-Pseudomonic acidPseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R1, versus L-isoleucine652415 2D-image
1.5e-05-Pseudomonic acidPseudomonas fluorescensQ8L1B1pH 7.5, recombinant isozyme IleRS-R1, versus ATP652415 2D-image
2e-05-Pseudomonic acidStaphylococcus aureus-pH 7.9, 22°C651904 2D-image
4.5e-05-SB-205952Staphylococcus aureus-pH 7.9, 22°C651904 2D-image
9e-05-isoleucinyl-adenylateStaphylococcus aureus-pH 7.9, 22°C651904 2D-image
additional information-additional informationRattus norvegicus, Staphylococcus aureus--650527-
additional information-additional informationEscherichia coli--650559, 650560, 650564-
additional information-additional informationStaphylococcus aureus-inhibition kinetics651904-
additional information-additional informationThermus thermophilus--652205-

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0064-2,3-dideoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamateEscherichia coli-IC50: 0.0064 mM664321 2D-image
0.28-2-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamateEscherichia coli-IC50: 0.28 mM664321 2D-image
0.035-3-deoxy-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamateEscherichia coli-IC50: 0.035 mM664321 2D-image
0.000265-adenosine-5-[(2S,3S)-2-amino-3-methylpentanoyl]-sulfamateEscherichia coli-IC50: 0.000265 mM664321 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.00084-Rattus norvegicus--470
0.05-Escherichia coli--468
0.06-Ovis aries--474
0.97-Escherichia coli--464
73.8-Thermus thermophilus--466
254.5-Geobacillus stearothermophilus--460
additional information-Cricetulus griseus, Oryctolagus cuniculus--652046
additional information-Escherichia coli-rate constants for hydrolysis and transfer of a noncognate intermediate are roughly equal in IleRS715519

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.3-Bacillus subtilisQ45477activity assay704642
7.5-Cricetulus griseus, Oryctolagus cuniculus-assay at652046
7.5-Pseudomonas fluorescensQ8L1B1assay at652415
7.5-Escherichia coli-assay at672235
7.5-Thermus thermophilus-assay at675388
7.5-Escherichia coli-assay at, aminoacylation and deacylation reactions715519
7.7-Thermus thermophilus--466
7.9-Staphylococcus aureus-assay at651903, 651904, 651905
8.5-Escherichia coli--467
additional information-Escherichia coli-pH-dependence of enzyme-substrate complex formation467

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
68.8Thermus thermophilus-about 30% of maximal activity at pH 6.0 and 8.8466

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
22-Staphylococcus aureus-assay at651903, 651904, 651905
22-Bacillus subtilisQ45477activity assay at room temperature704642
37-Cricetulus griseus, Oryctolagus cuniculus-assay at652046
37-Thermus thermophilus-assay at675388
37-Escherichia coli-assay at, aminoacylation and deacylation reactions715519
45-Geobacillus stearothermophilus-formation of isoleucyl-tRNA460
62-Thermus thermophilus-isoleucine-tRNA formation with E. coli tRNA466
65-Geobacillus stearothermophilus-isoleucine-dependent ATP-diphosphate exchange reaction460
75-Thermus thermophilus-isoleucine tRNA formation with Thermus thermophilus tRNA466
80-Thermus thermophilus-isoleucine dependent ATP-diphosphate exchange466

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
erythroleukemia cellMus musculus--126Manually annotated by BRENDA team
HL-60 cellHomo sapiens--691288Manually annotated by BRENDA team
kidneyOryctolagus cuniculus-cell line LCC-RK1652046Manually annotated by BRENDA team
liverRattus norvegicus--470, 650527Manually annotated by BRENDA team
ovaryCricetulus griseus-cell line CRL-1781652046Manually annotated by BRENDA team
PC-3 cellHomo sapiens--691288Manually annotated by BRENDA team
liverOvis aries--474Manually annotated by BRENDA team
additional informationPlasmodium falciparum-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, overview716781Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
apicoplastPlasmodium falciparum--20011716781Manually annotated by BRENDA team
cytoplasmCricetulus griseus, Oryctolagus cuniculus-major part, enzyme participates in a multienzyme complex, not as large and stable as the one from nucleus5737652046Manually annotated by BRENDA team
nucleusCricetulus griseus-1.3% of total activity in the cell, enzyme participates in a large and stable multienzyme complex5634652046Manually annotated by BRENDA team
nucleusOryctolagus cuniculus-0.32% of total activity in the cell, enzyme participates in a large and stable multienzyme complex5634652046Manually annotated by BRENDA team
cytoplasmPlasmodium falciparum--5737716781Manually annotated by BRENDA team
additional informationPlasmodium falciparum-two IRS isozymes localize to distinct compartments in the parasite-716781Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
1ffy, downloadSCOP (1ffy)CATH (1ffy)Staphylococcus aureus
1qu2, downloadSCOP (1qu2)CATH (1qu2)Staphylococcus aureus
1qu3, downloadSCOP (1qu3)CATH (1qu3)Staphylococcus aureus
1jzq, downloadSCOP (1jzq)CATH (1jzq)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
1jzs, downloadSCOP (1jzs)CATH (1jzs)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
1udz, downloadSCOP (1udz)CATH (1udz)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
1ue0, downloadSCOP (1ue0)CATH (1ue0)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
1wk8, downloadSCOP (1wk8)CATH (1wk8)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
1wny, downloadSCOP (1wny)CATH (1wny)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
1wnz, downloadSCOP (1wnz)CATH (1wnz)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
102000-Escherichia coli-sedimentation equilibrium measurement464
115000-Geobacillus stearothermophilus-disc gel electrophoresis460
115000-Thermus thermophilus-gel filtration466
115000-Thermus thermophilus-HPLC gel filtration67
200000-Ovis aries-gel filtration474

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Ovis aries-x * 139000, SDS-PAGE474
?Pseudomonas fluorescensQ8L1B1x * 117000-117738, native isozyme IleRS-R2, SDS-PAGE and amino acid sequence determination652415
monomerEscherichia coli-1 * 103000, SDS-PAGE464
monomerThermus thermophilus-1 * 129000, SDS-PAGE67
additional informationHaloarcula marismortui-aggregation of aminoacyl-tRNA synthetases into a multienzyme complex125
additional informationMus musculus-high molecular mass aminoacyl-tRNA synthetase complex with a coherent structure that can be visualized by electron microscopy126
additional informationEscherichia coli-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, overview672235

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
analysis of the crystal structure with bound muciproin, PDB ID: 1FFYStaphylococcus aureusP41972675256
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 analysisStaphylococcus aureusP41972653886
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 analysisThermus thermophilus-652566
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 analysisThermus thermophilus-652205
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 resolutionThermus thermophilus-675388

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
60-Geobacillus stearothermophilus-stable below460
77-Thermus thermophilus-half-life is 15 min, inactivation is completely suppressed by addition of either E. coli or Thermus thermophilus tRNA466
additional information-Geobacillus stearothermophilus-isoleucine, isoleucine + ATP and tRNA + Mg2+ protect against heat inactivation, some protection by high concentrations of valine460

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-15°C, 50% glycerolEscherichia coli-464
-20°CGeobacillus stearothermophilus-460
-20°C, 50% glycerolThermus thermophilus-466

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
using M2-FLAG resinBacillus subtilisQ45477704642
-Escherichia coli-464, 468, 706028
recombinant His-tagged IleRS from Escherichia coli strain BL21 (DE3) by nickel affinity chromatographyEscherichia coli-715519
-Geobacillus stearothermophilus-460
-Ovis aries-474
native enzyme, and recombinant enzyme from Escherichia coli, amino acid sequence determinationPseudomonas fluorescensQ8L1B1652415
-Rattus norvegicus-470
-Saccharomyces cerevisiae-457
-Thermus thermophilus-67
partialThermus thermophilus-466
recombinant His-tagged wild-type and mutants enzymes from Escherichia coli by nickel affinity chromatographyThermus thermophilus-675388

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
into the vector pET3D-FLAG for expression in Escherichia coli BL21DE3 cellsBacillus subtilisQ45477704642
overexpression of His-tagged IleRS in Escherichia coli strain BL21 (DE3)Escherichia coli-715519
with the pCR2.1-TOPO TA cloning kit for sequencingMethanopyrus kandleri-705210
-Methanothermobacter thermautotrophicus-459
genotyping of thiaisoleucine-resistant enzymes, expression of GFP-tagged cytoplasmic isozyme in erythrocytic stage parasitePlasmodium falciparum-716781
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 Ts331Pseudomonas fluorescensQ8L1B1652415
-Saccharomyces cerevisiae-458
expression in Escherichia coliSaccharomyces cerevisiae-457
gene ileS, quantitative real-time PCR expression analysisSalmonella enterica-715118
expression of His-tagged wild-type and mutants enzymes in Escherichia coliThermus thermophilus-675388

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
AIleRSEscherichia coli-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 activity450
D342AEscherichia coli-site-directed mutagenesis, the IleRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations715519
T243REscherichia coli-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 enzyme715519
T243R/D342AEscherichia coli-site-directed mutagenesis, the IleRS CP1 domain mutant is unable to deacylate misacylated tRNA even at high enzyme concentrations715519
L810FPlasmodium falciparum-naturally occuring mutation in the cytoplasmic IleRS responsible for thiaisoleucine-resistance in the parasite, phenotype, overview716781
P184TSalmonella enterica-naturally occuring mutation that restores fitness in mupirocin resistant strains715118
Q420HSalmonella enterica-naturally occuring mutation that restores fitness in mupirocin resistant strains715118
F227LStaphylococcus aureusP41972the naturally occuring mutation affects the muciprocin binding675256
H581L/L583HStaphylococcus aureusP41368site-directed mutagenesis, slightly reduced enzyme activity652205
K226TStaphylococcus aureusP41972the naturally occuring mutation affects the muciprocin binding675256
P187FStaphylococcus aureusP41972the naturally occuring mutation affects the muciprocin binding675256
Q612HStaphylococcus aureusP41972the naturally occuring mutation is involved in stabilizing the conformation of the catalytic loop containing the KMSKS motif675256
V588FStaphylococcus aureusP41972the naturally occuring mutation affects the Rossman fold and leads to low-level mupirocin resistance675256
V767DStaphylococcus aureusP41972the naturally occuring mutation affects the muciprocin binding675256
H319AThermus thermophilus-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, overview675388
T223AThermus thermophilus-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, overview675388
W227AThermus thermophilus-site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme675388
W227FThermus thermophilus-site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme675388
W227HThermus thermophilus-site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme675388
W227LThermus thermophilus-site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme675388
W227VThermus thermophilus-site-directed mutagenesis, both editing activities of the mutant are reduced compared to the wild-type enzyme675388
W227YThermus thermophilus-site-directed mutagenesis, the mutant shows editing activities which are unaltered compared to the wild-type enzyme675388
IleRS(C922S)Escherichia coli-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 activity450
additional informationEscherichia coli-pseudomonic acid resistant mutant strain PS102447
additional informationEscherichia coli-mutant enzymes with altered metal-binding sites452
G590DMethanothermobacter thermautotrophicus-pseudomonic-acid resistant mutant MBT10, with a Gly590 to aspartic acid transition459
additional informationMethanothermobacter thermautotrophicus-pseudomonic acid-resistant mutant475

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
molecular biologyEscherichia coli-enzyme is a target for receptor-guided inhibitor design650559
drug developmentPlasmodium falciparum-isoleucine utilization is an essential pathway that can be targeted for antimalarial drug development716781
medicineStaphylococcus aureus-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 isolates693190

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Bone ResorptionReveromycin A, an agent for osteoporosis, inhibits bone resorption by inducing apoptosis specifically in osteoclasts. PubMed
CandidiasisEfficacy of PLD-118, a novel inhibitor of candida isoleucyl-tRNA synthetase, against experimental oropharyngeal and esophageal candidiasis caused by fluconazole-resistant C. albicans. PubMed
CandidiasisEfficacy, plasma pharmacokinetics, and safety of icofungipen, an inhibitor of Candida isoleucyl-tRNA synthetase, in treatment of experimental disseminated candidiasis in persistently neutropenic rabbits. PubMed
Cardiomyopathy, HypertrophicIsoleucyl-tRNA synthetase levels modulate the penetrance of a homoplasmic m.4277T>C mitochondrial tRNA(Ile) mutation causing hypertrophic cardiomyopathy. PubMed
InfectionMupirocin: biosynthesis, special features and applications of an antibiotic from a Gram-negative bacterium. PubMed
Influenza, HumanEffects of a minor isoleucyl tRNA on heterologous protein translation in Escherichia coli. PubMed
NeoplasmsAlterations of repeated sequences in 5' upstream and coding regions in colorectal tumors from patients with hereditary nonpolyposis colorectal cancer and Turcot syndrome. PubMed
TuberculosisA eubacterial Mycobacterium tuberculosis tRNA synthetase is eukaryote-like and resistant to a eubacterial-specific antisynthetase drug. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
67Kohda, 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+ bindingFEBS Lett.17420-231984Thermus thermophilus PubMed
125Goldgur, Y.; Safro, M.Aminoacyl-tRNA synthetases from Haloarcula marismortui: an evidence for a multienzyme complex in a procaryotic systemBiochem. Mol. Biol. Int.321075-10831994Haloarcula marismortui PubMed
126Norcum, M.T.Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cellsJ. Biol. Chem.26415043-150511989Mus musculus PubMed
447Yanagisawa, T.; Lee, J.T.; Wu, H.C.; Kawakami, M.Relationship of protein structure of isoleucyl-tRNA synthetase with pseudomonic acid resistance of Escherichia coliJ. Biol. Chem.26924304-243091994Escherichia coli PubMed
448Glasfeld, E.; Landro, J.A.; Schimmel, P.C-terminal zinc-containing peptide required for RNA recognition by a class I tRNA synthetaseBiochemistry354139-41451996Escherichia coli PubMed
449Jakubowski, H.Proofreading in trans by an aminoacyl-tRNA synthetase. A model for single site editing by isoleucyl-tRNA synthetaseNucleic Acids Res.242505-25101996Escherichia coli PubMed
450Zhou, L.; Rosevear, P.R.Mutation of the carboxy terminal zinc finger of E. coli isoleucyl-tRNA synthetase alters zinc binding and aminoacylation activityBiochem. Biophys. Res. Commun.216648-6541995Escherichia coli PubMed
451Auld, D.S.; Schimmel., P.Switching recognition of two tRNA synthetases with an amino acid swap in a designed peptideScience2671994-19961995Escherichia coli PubMed
452Landro, J.A.; Schmidt, E.; Schimmel, P.Thiol ligation of two zinc atoms to a class I tRNA synthetase. Evidence for unshared thiols and role in amino acid binding and utilizationBiochemistry3314213-142201994Escherichia coli PubMed
453Xu, B.; Trawick, B.; Krudy, G.A.; Phillips, R.M.; Zhou.L.; Rosevear, P.R.Probing the metal binding sites of E. coli isoleucyl-tRNA synthetaseBiochemistry33398-4021994Escherichia coli PubMed
454Airas, R.K.Analysis of the isoleucyl-tRNA synthetase reaction by total rate equation. Magnesium and spermidine in the tRNA kineticsEur. J. Biochem.210451-4541992Escherichia coli PubMed
455Schimmel, P.; Landro, J.A.; Schidt, E.Evidence for distinct locations for metal binding sites in two closely related class I tRNA synthetasesJ. Biomol. Struct. Dyn.11571-5811993Escherichia coli PubMed
456Glasfeld, E.; Schimmel, P.Zinc-dependent tRNA binding by a peptide element within a tRNA synthetaseBiochemistry366739-67441997Escherichia coli PubMed
457Racher, K.I.; Kalmar, G.B.; Borgford, T.J.Expression and characterization of a recombinant yeast isoleucyl-tRNA synthetaseJ. Biol. Chem.26617158-171641991Saccharomyces cerevisiae PubMed
458Englisch, U.; Englisch, S.; Markmeyer, P.; Schischkoff, J.; Sterbach, H.; Kratzin, H.; Cramer, F.Structure of the yeast isoleucyl-tRNA synthetase gene (ILS1). DNA-sequence, amino-acid sequence of the proteolytic peptides of the enzyme and comparison of the structure to those of other known aminoacyl-tRNA synthetasesBiol. Chem. Hoppe-Seyler368971-9791987Saccharomyces cerevisiae PubMed
459Jenal.U.; Rechsteiner, T.; Tan, P.Y.; Buhlmann, E.; Meile, L.; Leisinger, T.Isoleucyl-tRNA synthetase of Methanobacterium thermoautotrophicum Marburg. Cloning of the gene, nucleotide sequence, and localization of a base change conferring resistance to pseudomonic acidJ. Biol. Chem.26610570-105771991Methanothermobacter thermautotrophicus PubMed
460Charlier, J.; Grosjean, H.Isoleucyl-transfer ribonucleic acid synthetase from Bacillus stearothermophilus. Properties of the enzymeEur. J. Biochem.25163-1741972Geobacillus stearothermophilus PubMed
461Grosjean, H.; Charlier, J.Comparative studies on the isoleucyl-tRNA synthetases from Bacillus stearothermophilus and Escherichia coli. II. The effect of magnesium ions in the transacylation reactionFEBS Lett.18342-3461971Escherichia coli, Geobacillus stearothermophilus PubMed
462Steinmetz Kayne , M.; Cohn, M.Cation requirements of isoleucyl-tRNA synthetase from Escherichia coliBiochem. Biophys. Res. Commun.461285-12911972Escherichia coli PubMed
463Holler, E.Isoleucyl transfer ribonucleic acid synthetase of Escherichia coli B. Effects of magnesium and spermine on the amino acid activation reactionBiochemistry121142-11491973Escherichia coli PubMed
464Durekovic, A.; Flossdorf, J.; Kula, M.R.Isolation and properties of isoleucyl-tRNA synthetase from Escherichia coli MRE 600Eur. J. Biochem.36528-5331973Escherichia coli PubMed
465Carr, A.C.; Igloi, G.L.; Penzer, G.R.; Plumbridge, J.A.The effect of spermine anf Mg2+ on the catalytic mechanism of isoleucine:tRNA ligaseEur. J. Biochem.54169-1731975Escherichia coli PubMed
466Wakagi, T.; Ohta, T.; Imahori, K.Studies on isoleucyl-tRNA synthetase of an extreme thermophile, Thermus thermophilus HB8Agric. Biol. Chem.391573-15801975Thermus thermophilus-
467Hammer-Raber, B.; Rainey, P.M.; Holler, E.L-Isoleucyl-tRNA synthetase aus E. coli. pH-Abhängigkeit der Enzym-Substrat KomplexbildungHoppe-Seyler's Z. Physiol. Chem.3572951976Escherichia coli-
468Moe, J.G.; Piszkiewicz, D.Purification of isoleucyl transfer ribonucleic acid synthetase by affinity chromatography on blue dextran-SeparoseFEBS Lett.72147-1501976Escherichia coli PubMed
469Freist, W.; von der Haar, F.; Faulhammer, H.; Cramer, F.Valyl-tRNA, isoleucyl-tRNA and tyrosyl-tRNA synthetase from baker's yeast. Substrate specificity with regard to ATP analogs and mechanism of the aminoacylation reactionEur. J. Biochem.66493-4971976Saccharomyces cerevisiae PubMed
470Igarashi, K.; Eguchi, K.; Tanaka, M.; Hirose, S.Effect of polyamines on isoleucyl-tRNA formation by rat liver isoleucyl-tRNA synthetaseEur. J. Biochem.82301-3071978Rattus norvegicus PubMed
471Hughes, J.; Mellows, G.Inhibition of isoleucyl-transfer ribonucleic acid synthetase in Escherichia coli by pseudomonic acidBiochem. J.176305-3181978Escherichia coli PubMed
472Freist, W.; von der Haar, F.; Cramer, F.Isoleucyl-tRNA synthetase from baker's yeastEur. J. Biochem.119151-1641981Saccharomyces cerevisiae PubMed
474Lazard, M.; Mirande, M.; Waller, J.P.Purification and characterization of the isoleucyl-tRNA synthetase component from the high molecular weight complex of sheep liver. A hydrophobic metalloproteinBiochemistry245099-51061985Ovis aries PubMed
475Kiener, A.; Rechsteiner, T.; Leisinger, T.Mutation to pseudomonic acid resistance of Methanobacterium thermoautotrophicum leads to an altered isoleucyl-tRNA synthetaseFEMS Microbiol. Lett.3315-181986Methanothermobacter thermautotrophicus-
476Freist, W.; Sternbach, H.; Cramer, F.Isoleucyl-tRNA synthetase from baker's yeast and from Escherichia coli MRE 600. Discrimination of 20 amino acids in aminoacylation of tRNAIle-C-C-A(3'NH2)Eur. J. Biochem.16933-391987Escherichia coli, Saccharomyces cerevisiae PubMed
650527Crasto, C.F.; Forrest, A.K.; Karoli, T.; March, D.R.; Mensah, L.; O'Hanlon, P.J.; Nairn, M.R.; Oldham, M.D.; Yue, W.; Banwell, M.G.; Easton, C.J.Synthesis and activity of analogues of the isoleucyl tRNA synthetase inhibitor SB-203207Bioorg. Med. Chem.112687-26942003Rattus norvegicus, Staphylococcus aureus PubMed
650559Lee, J.; Kang, S.U.; Kim, S.Y.; Kim, S.E.; Kang, M.K.; Jo, Y.J.; Kim, S.Ester and hydroxamate analogues of methionyl and isoleucyl adenylates as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetasesBioorg. Med. Chem. Lett.11961-9642001Escherichia coli PubMed
650560Lee, J.; Kang, S.U.; Kim, S.Y.; Kim, S.E.; Job, Y.J.; Kim, S.Vanilloid and isovanilloid analogues as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetasesBioorg. Med. Chem. Lett.11965-9682001Escherichia coli PubMed
650564Lee, J.; Kim, S.E.; Lee, J.Y.; Kim, S.Y.; Kang, S.U.; Seo, S.H.; Chun, M.W.; Kang, T.; Choi, S.Y.; Kim, H.O.N-Alkoxysulfamide, N-hydroxysulfamide, and sulfamate analogues of methionyl and isoleucyl adenylates as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetasesBioorg. Med. Chem. Lett.131087-10922003Escherichia coli PubMed
651903Pope, A.J.; Lapointe, J.; Mensah, L.; Benson, N.; Brown, M.J.; Moore, K.J.Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus. I: Kinetic mechanism of the substrate activation reaction studied by transient and steady-state techniquesJ. Biol. Chem.27331680-316901998Staphylococcus aureus PubMed
651904Pope, A.J.; Moore, K.J.; McVey, M.; Mensah, L.; Benson, N.; Osbourne, N.; Broom, N.; Brown, M.J.; O'Hanlon, P.Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus. II. Mechanism of inhibition by reaction intermediate and pseudomonic acid analogues studied using transient and steady-state kineticsJ. Biol. Chem.27331691-317011998Staphylococcus aureus PubMed
651905Pope, A.J.; McVey, M.; Fantom, K.; Moore, K.J.Effects of substrate and inhibitor binding on proteolysis of isoleucyl-tRNA synthetase from Staphylococcus aureusJ. Biol. Chem.27331702-317061998Staphylococcus aureus PubMed
652046Nathanson, L.; Deutscher, M.P.Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complexJ. Biol. Chem.27531559-315622000Cricetulus griseus, Oryctolagus cuniculus PubMed
652205Nakama, T.; Nureki, O.; Yokoyama, S.Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetaseJ. Biol. Chem.27647387-473932001Staphylococcus aureus, Thermus thermophilus PubMed
652415Yanagisawa, T.; Kawakami, M.How does Pseudomonas fluorescens avoid suicide from its antibiotic pseudomonic acid?: Evidence for two evolutionarily distinct isoleucyl-tRNA synthetases conferring self-defenseJ. Biol. Chem.27825887-258942003Pseudomonas fluorescens PubMed
652566Fukunaga, 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-valineJ. Biol. Chem.2798396-84022004Thermus thermophilus PubMed
653886Silvian, L.F.; Wang, J.; Steitz, T.A.Insights into editing from an Ile-tRNA synthetase structure with tRNAIle and mupirocinScience2851074-10771999Staphylococcus aureus PubMed
664321Kim, S.E.; Kim, S.Y.; KI, S.; Kang, T.; Lee, J.Deoxyribosyl analogues of methionyl and isoleucyl sulfamate adenylates as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetaseBioorg. Med. Chem. Lett.153389-33932005Escherichia coli PubMed
672235Zhai, Y.; Nawaz, M.H.; Lee, K.W.; Kirkbride, E.; Briggs, J.M.; Martinis, S.A.Modulation of substrate specificity within the amino acid editing site of leucyl-tRNA synthetaseBiochemistry463331-33372007Escherichia coli PubMed
675256Yang, J.A.; Park, D.W.; Sohn, J.W.; Yang, I.S.; Kim, K.H.; Kim, M.J.Molecular analysis of isoleucyl-tRNA synthetase mutations in clinical isolates of methicillin-resistant Staphylococcus aureus with low-level mupirocin resistanceJ. Korean Med. Sci.21827-8322006Staphylococcus aureus PubMed
675388Fukunaga, R.; Yokoyama, S.Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetaseJ. Mol. Biol.359901-9122006Thermus thermophilus PubMed
691288Shimizu, T.; Usui, T.; Fujikura, M.; Kawatani, M.; Satoh, T.; Machida, K.; Kanoh, N.; Woo, J.T.; Osada, H.; Sodeoka, M.Synthesis and biological activities of reveromycin A and spirofungin A derivativesBioorg. Med. Chem. Lett.183756-37602008Homo sapiens PubMed
693190De Pascale, G.; Lloyd, A.J.; Schouten, J.A.; Gilbey, A.M.; Roper, D.I.; Dowson, C.G.; Bugg, T.D.Kinetic characterisation of lipid II-Ala:alanyl tRNA ligase (MurN) from Streptococcus pneumoniae using semi-synthetic aminoacyl-lipid II substratesJ. Biol. Chem.28334571-345792008Staphylococcus aureus PubMed
704642Salowe, S.P.; Wiltsie, J.; Hawkins, J.C.; Sonatore, L.M.The catalytic flexibility of tRNAIle-lysidine synthetase can generate alternative tRNA substrates for isoleucyl-tRNA synthetaseJ. Biol. Chem.2849656-96622009Bacillus subtilis PubMed
705210Yu, Z.; Takai, K.; Slesarev, A.; Xue, H.; Wong, J.T.Search for primitive Methanopyrus based on genetic distance between Val- and Ile-tRNA synthetasesJ. Mol. Evol.69386-3942009Methanopyrus kandleri PubMed
706028Baouz, S.; Schmitter, J.M.; Chenoune, L.; Beauvallet, C.; Blanquet, S.; Woisard, A.; Hountondji, C.Primary structure revision and active site mapping of E. coli isoleucyl-tRNA synthetase by means of maldi mass spectrometryOpen Biochem. J.326-382009Escherichia coli PubMed
715118Paulander, W.; Andersson, D.I.; Maisnier-Patin, S.Amplification of the gene for isoleucyl-tRNA synthetase facilitates adaptation to the fitness cost of mupirocin resistance in Salmonella entericaGenetics185305-3122010Salmonella enterica PubMed
715519Dulic, M.; Cvetesic, N.; Perona, J.J.; Gruic-Sovulj, I.Partitioning of tRNA-dependent editing between pre- and post-transfer pathways in class I aminoacyl-tRNA synthetasesJ. Biol. Chem.28523799-238092010Escherichia coli PubMed
716781Istvan, E.S.; Dharia, N.V.; Bopp, S.E.; Gluzman, I.; Winzeler, E.A.; Goldberg, D.E.Validation of isoleucine utilization targets in Plasmodium falciparumProc. Natl. Acad. Sci. USA1081627-16322011Plasmodium falciparum PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 6.1.1.5)
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NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
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Protein Mutant Database
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