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Literature summary for 6.1.1.5 extracted from

  • Pope, A.J.; McVey, M.; Fantom, K.; Moore, K.J.
    Effects of substrate and inhibitor binding on proteolysis of isoleucyl-tRNA synthetase from Staphylococcus aureus (1998), J. Biol. Chem., 273, 31702-31706.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
chymotrypsin proteolytic inactivation patterns, bound Ile-AMP or inhibitors isoleucinol adenylate and pseudomonic acid protect, 50fold higher concentration is needed for digestion of Ile-AMP-enzyme complex than for the free enzyme at 37°C Staphylococcus aureus
isoleucinol adenylate determination of binding structures, bound inhibitor protects against proteolytic inactivation by trypsin or chymotrypsin and specifically alters the proteolytic cleavage pattern Staphylococcus aureus
pseudomonic acid competitive, determination of binding structures, bound inhibitor protects against proteolytic inactivation by trypsin or chymotrypsin and specifically alters the proteolytic cleavage pattern Staphylococcus aureus
SB-205952 a semisynthetic analogue of monic acid Staphylococcus aureus
Trypsin proteolytic inactivation patterns, bound Ile-AMP or inhibitors isoleucinol adenylate and pseudomonic acid protect, 50fold higher concentration is needed for digestion of Ile-AMP-enzyme complex than for the free enzyme at 37°C Staphylococcus aureus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0001
-
tRNAIle below, pH 7.9, 22°C Staphylococcus aureus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, MgATP2- Staphylococcus aureus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-isoleucine + tRNAIle Staphylococcus aureus
-
AMP + diphosphate + L-isoleucyl-tRNAIle
-
r

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
purified recombinant enzyme expressed in Escherichia coli strain DH1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-isoleucine + tRNAIle
-
Staphylococcus aureus AMP + diphosphate + L-isoleucyl-tRNAIle
-
r
ATP + L-isoleucine + tRNAIle reaction intermediate is the Ile-AMP-enzyme complex Staphylococcus aureus AMP + diphosphate + L-isoleucyl-tRNAIle
-
r
additional information enzyme also performs the reversible ATP-diphosphate exchange reaction Staphylococcus aureus ?
-
?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.9
-
assay at Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
ATP dependent on, MgATP2- Staphylococcus aureus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000001
-
pseudomonic acid pH 7.9, 22°C, in complex with the enzyme and Ile, in analogy to the reaction intermediate Staphylococcus aureus
0.00003
-
isoleucinol adenylate pH 7.9, 22°C, in complex with the enzyme and Ile, in analogy to the reaction intermediate Staphylococcus aureus