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Literature summary extracted from

  • Nakama, T.; Nureki, O.; Yokoyama, S.
    Structural basis for the recognition of isoleucyl-adenylate and an antibiotic, mupirocin, by isoleucyl-tRNA synthetase (2001), J. Biol. Chem., 276, 47387-47393.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.5 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

EC Number Protein Variants Comment Organism
6.1.1.5 H581L/L583H site-directed mutagenesis, slightly reduced enzyme activity Staphylococcus aureus

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.1.1.5 5'-N-[N-(L-isoleucyl)sulfamoyl]adenosine non-hydrolyzable analogue of the reaction intermediate Ile-AMP Thermus thermophilus
6.1.1.5 muciproin
-
 Staphylococcus aureus
6.1.1.5 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.5 0.118
-
 L-isoleucine mutant enzyme Staphylococcus aureus
6.1.1.5 52.8
-
 L-isoleucine pH 8.0, 65°C, recombinant wild-type enzyme Thermus thermophilus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.5 ATP + L-isoleucine + tRNAIle Thermus thermophilus
-
 AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?
6.1.1.5 ATP + L-isoleucine + tRNAIle Staphylococcus aureus
-
 AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?
6.1.1.5 ATP + L-isoleucine + tRNAIle Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.5 Staphylococcus aureus P41368
-
-
6.1.1.5 Thermus thermophilus
-
 purified recombinant wild-type and mutant enzyme
-
6.1.1.5 Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 purified recombinant wild-type and mutant enzyme
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.5 ATP + L-isoleucine + tRNAIle = AMP + diphosphate + L-isoleucyl-tRNAIle substrate recognition mechanism, Glu551, Thr48, His581 and Lys594are involved Thermus thermophilus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.5 ATP + L-isoleucine + tRNAIle
-
 Thermus thermophilus AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?
6.1.1.5 ATP + L-isoleucine + tRNAIle
-
 Staphylococcus aureus AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?
6.1.1.5 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
-
 ?
6.1.1.5 ATP + L-isoleucine + tRNAIle
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 AMP + diphosphate + L-isoleucyl-tRNAIle
-
 ?
6.1.1.5 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

EC Number Synonyms Comment Organism
6.1.1.5 IleRS
-
 Thermus thermophilus
6.1.1.5 IleRS
-
 Staphylococcus aureus
6.1.1.5 IRS
-
 Thermus thermophilus
6.1.1.5 IRS
-
 Staphylococcus aureus
6.1.1.5 Isoleucine translase
-
 Thermus thermophilus
6.1.1.5 Isoleucine translase
-
 Staphylococcus aureus
6.1.1.5 Isoleucine--tRNA ligase
-
 Thermus thermophilus
6.1.1.5 Isoleucine--tRNA ligase
-
 Staphylococcus aureus
6.1.1.5 Isoleucine-transfer RNA ligase
-
 Thermus thermophilus
6.1.1.5 Isoleucine-transfer RNA ligase
-
 Staphylococcus aureus
6.1.1.5 Isoleucine-tRNA synthetase
-
 Thermus thermophilus
6.1.1.5 Isoleucine-tRNA synthetase
-
 Staphylococcus aureus
6.1.1.5 Isoleucyl-transfer ribonucleate synthetase
-
 Thermus thermophilus
6.1.1.5 Isoleucyl-transfer ribonucleate synthetase
-
 Staphylococcus aureus
6.1.1.5 Isoleucyl-transfer RNA synthetase
-
 Thermus thermophilus
6.1.1.5 Isoleucyl-transfer RNA synthetase
-
 Staphylococcus aureus
6.1.1.5 Isoleucyl-tRNA synthetase
-
 Thermus thermophilus
6.1.1.5 Isoleucyl-tRNA synthetase
-
 Staphylococcus aureus
6.1.1.5 Mupirocin resistance protein
-
 Thermus thermophilus
6.1.1.5 Mupirocin resistance protein
-
 Staphylococcus aureus
6.1.1.5 Synthetase, isoleucyl-transfer ribonucleate
-
 Thermus thermophilus
6.1.1.5 Synthetase, isoleucyl-transfer ribonucleate
-
 Staphylococcus aureus

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.5 ATP
-
 Thermus thermophilus
6.1.1.5 ATP
-
 Staphylococcus aureus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.1.1.5 additional information
-
 additional information
-
 Thermus thermophilus
6.1.1.5 0.00025
-
 muciproin pH 8.0, 65°C, recombinant wild-type enzyme, with respect to L-isoleucine Thermus thermophilus
6.1.1.5 0.0023
-
 muciproin mutant enzyme Staphylococcus aureus