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Literature summary for 6.1.1.5 extracted from

  • Zhai, 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 synthetase (2007), Biochemistry, 46, 3331-3337.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-isoleucine + tRNAIle Escherichia coli
-
AMP + diphosphate + L-isoleucyl-tRNAIle
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-isoleucine + tRNAIle
-
Escherichia coli AMP + diphosphate + L-isoleucyl-tRNAIle
-
?
ATP + L-isoleucine + tRNAIle 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,overview Escherichia coli AMP + diphosphate + L-isoleucyl-tRNAIle
-
?

Subunits

Subunits Comment Organism
More 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, overview Escherichia coli

Synonyms

Synonyms Comment Organism
IleRS
-
Escherichia coli
Isoleucyl-tRNA synthetase
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli