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Literature summary for 6.1.1.5 extracted from

  • Zhou, L.; Rosevear, P.R.
    Mutation of the carboxy terminal zinc finger of E. coli isoleucyl-tRNA synthetase alters zinc binding and aminoacylation activity (1995), Biochem. Biophys. Res. Commun., 216, 648-654.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
AIleRS mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity Escherichia coli
IleRS(C922S) mutant enzymes IleRS(C922S) and AIleRS with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc. Mutant enzymes have altered zinc binding and aminoacylation activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0021
-
tRNAIle wild-type enzyme Escherichia coli
0.7
-
ATP wild-type enzyme Escherichia coli
1.3
-
Ile wild-type enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zinc 2 enzyme bound zinc atoms per polypeptide chain Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
wild-type and mutant enzymes IleRS(C922S) and AIleRS, with replacement of Cys922 through Ala939 with a 33 amino acid peptide unable to bind zinc (AIleRS), mutant enzymes have altered zinc binding and aminoacylation activity
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-isoleucine + tRNAIle
-
Escherichia coli AMP + diphosphate + L-isoleucyl-tRNAIle
-
?
additional information Ile + ATP + enzyme/Ile-AMP-enzyme + diphosphate, isoleucine-dependent ATP-diphosphate exchange Escherichia coli ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1
-
tRNAIle wild-type enzyme Escherichia coli
104
-
isoleucine wild-type enzyme Escherichia coli