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Literature summary for 6.1.1.18 extracted from

  • Conley, J.; Sherman, J.; Thomann, H.U.; Söll, D.
    Domains of E. coli glutaminyl-tRNA synthetase disordered in the crystal structure are essential for function or stability (1994), Nucleosides Nucleotides, 13, 1581-1595.
No PubMed abstract available
Search for more literature for 6.1.1.18

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information deletion mutants with C-terminal truncations and N-terminal truncations. A C-terminal deletion mutant exhibits sharp reduction in the specificity constant. Reduced stability of some of these mutants Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km value of mutant enzymes Escherichia coli
0.000019
-
 tRNAGln wild-type enzyme, strain UT172 Escherichia coli
0.04
-
 ATP wild-type enzyme, strain UT172 Escherichia coli
0.19
-
 Gln wild-type enzyme, strain UT172 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 strains UT172 and X3R2, and deletion mutants with C-terminal truncations and N-terminal truncations
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-glutamine + tRNAGln
-
 Escherichia coli AMP + diphosphate + L-glutaminyl-tRNAGln
-
 ?