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Literature summary extracted from

  • Landro, J.A.; Schmidt, E.; Schimmel, P.
    Thiol ligation of two zinc atoms to a class I tRNA synthetase. Evidence for unshared thiols and role in amino acid binding and utilization (1994), Biochemistry, 33, 14213-14220.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.5 additional information mutant enzymes with altered metal-binding sites Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.5 additional information
-
 additional information Km value of mutant enzynes with altered metal-binding sites Escherichia coli
6.1.1.5 0.00054
-
 ATP wild-type enzyme Escherichia coli
6.1.1.5 0.0052
-
 Ile wild-type enzyme Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.5 Zinc a single zinc atom which is coordinated to ligands is contained in the catalytic domain, a second, functionally essential zinc is bound to ligands at the C-terminal end of the 939 amino acid polypeptide, the average zinc environment contains predominantly sulfur ligands with a Zn-S distance of 2.33 A Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.5 Escherichia coli
-
 wild-type and mutant enzymes with altered metal-binding sites
-

Substrates and Products (Substrate)

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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.5 27.7
-
 isoleucine wild-type enzyme Escherichia coli