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Literature summary for 6.1.1.5 extracted from
- Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase (2001), J. Biol. Chem., 276, 47387-47393.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| 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 | Thermus thermophilus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| H581L/L583H | site-directed mutagenesis, slightly reduced enzyme activity | Staphylococcus aureus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 5'-N-[N-(L-isoleucyl)sulfamoyl]adenosine | non-hydrolyzable analogue of the reaction intermediate Ile-AMP | Thermus thermophilus |  |
| muciproin | - |
Staphylococcus aureus | |
| 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 | Thermus thermophilus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.118 | - |
L-isoleucine | mutant enzyme | Staphylococcus aureus | |
| 52.8 | - |
L-isoleucine | pH 8.0, 65°C, recombinant wild-type enzyme | Thermus thermophilus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-isoleucine + tRNAIle | Thermus thermophilus | - |
AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | Staphylococcus aureus | - |
AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | P41368 | - |
- |
| Thermus thermophilus | - |
purified recombinant wild-type and mutant enzyme | - |
| Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | - |
purified recombinant wild-type and mutant enzyme | - |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle | substrate recognition mechanism, Glu551, Thr48, His581 and Lys594are involved | Thermus thermophilus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + L-isoleucine + tRNAIle | - |
Thermus thermophilus | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | - |
Staphylococcus aureus | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | enzyme shows a common recognition mode of aminoacyl-adenylate for a class I aminoacyl-tRNA synthetase, formation of high-energy reaction intermediate Ile-AMP | Thermus thermophilus | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | - |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
| ATP + L-isoleucine + tRNAIle | enzyme shows a common recognition mode of aminoacyl-adenylate for a class I aminoacyl-tRNA synthetase, formation of high-energy reaction intermediate Ile-AMP | Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | AMP + diphosphate + L-isoleucyl-tRNAIle | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| IleRS | - |
Thermus thermophilus |
| IleRS | - |
Staphylococcus aureus |
| IRS | - |
Thermus thermophilus |
| IRS | - |
Staphylococcus aureus |
| Isoleucine translase | - |
Thermus thermophilus |
| Isoleucine translase | - |
Staphylococcus aureus |
| Isoleucine--tRNA ligase | - |
Thermus thermophilus |
| Isoleucine--tRNA ligase | - |
Staphylococcus aureus |
| Isoleucine-transfer RNA ligase | - |
Thermus thermophilus |
| Isoleucine-transfer RNA ligase | - |
Staphylococcus aureus |
| Isoleucine-tRNA synthetase | - |
Thermus thermophilus |
| Isoleucine-tRNA synthetase | - |
Staphylococcus aureus |
| Isoleucyl-transfer ribonucleate synthetase | - |
Thermus thermophilus |
| Isoleucyl-transfer ribonucleate synthetase | - |
Staphylococcus aureus |
| Isoleucyl-transfer RNA synthetase | - |
Thermus thermophilus |
| Isoleucyl-transfer RNA synthetase | - |
Staphylococcus aureus |
| Isoleucyl-tRNA synthetase | - |
Thermus thermophilus |
| Isoleucyl-tRNA synthetase | - |
Staphylococcus aureus |
| Mupirocin resistance protein | - |
Thermus thermophilus |
| Mupirocin resistance protein | - |
Staphylococcus aureus |
| Synthetase, isoleucyl-transfer ribonucleate | - |
Thermus thermophilus |
| Synthetase, isoleucyl-transfer ribonucleate | - |
Staphylococcus aureus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Thermus thermophilus | |
| ATP | - |
Staphylococcus aureus | |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Thermus thermophilus | |
| 0.00025 | - |
muciproin | pH 8.0, 65°C, recombinant wild-type enzyme, with respect to L-isoleucine | Thermus thermophilus | |
| 0.0023 | - |
muciproin | mutant enzyme | Staphylococcus aureus | |
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