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Literature summary for 6.1.1.3 extracted from

  • Caillet, J.; Graffe, M.; Eyermann, F.; Romby, P.; Springer, M.
    Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype (2007), J. Bacteriol., 189, 6839-6848.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.3

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of His-tagged mutant enzymes Escherichia coli K-12

Protein Variants

Protein Variants Comment Organism
H385A site-directed mutagenesis, the mutant shows altered substrate specificity, overview Escherichia coli K-12
H385N site-directed mutagenesis, the mutant shows altered substrate specificity, overview Escherichia coli K-12
H385Y site-directed mutagenesis, the mutant shows altered substrate specificity, overview Escherichia coli K-12
additional information mutations of any of the three amino acids forming the zinc-binding site inactivate the enzyme and have a dominant negative effect on growth if the corresponding genes are placed on a multicopy plasmid, not due to the formation of inactive heterodimers, the titration of tRNAThr by an inactive enzyme, or its misaminoacylation but is, rather, due to the regulatory function of threonyl-tRNA synthetase, overview, the mutations confer a dominant lethal phenotype, overproduction of the inactive enzyme represses the expression of the wild-type chromosomal copy of the gene to an extent incompatible with bacterial growth, phenotypes, overview Escherichia coli K-12
R583H site-directed mutagenesis, the mutant shows altered substrate specificity, overview Escherichia coli K-12

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Escherichia coli K-12
Zn2+ zinc binding in the catalytic site, the active site zinc atom is essential for the recognition of threonine, three amino acids forming the zinc-binding site, overview Escherichia coli K-12

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-threonine + tRNAThr Escherichia coli K-12 the enzyme acts as both an enzyme and a regulator of gene expression, it aminoacylates tRNAThr isoacceptors and binds to its own mRNA, inhibiting its translation, overview AMP + diphosphate + L-threonyl-tRNAThr
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli K-12
-
 several strains, overview, gene thrS
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged mutant H385A Escherichia coli K-12

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-threonine + tRNAThr the enzyme acts as both an enzyme and a regulator of gene expression, it aminoacylates tRNAThr isoacceptors and binds to its own mRNA, inhibiting its translation, overview Escherichia coli K-12 AMP + diphosphate + L-threonyl-tRNAThr
-
 ?
ATP + L-threonine + tRNAThr the zinc atom in the active site is essential for the recognition of threonine Escherichia coli K-12 AMP + diphosphate + L-threonyl-tRNAThr
-
 ?

Synonyms

Synonyms Comment Organism
Threonyl-tRNA synthetase
-
 Escherichia coli K-12

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Escherichia coli K-12

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli K-12