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Literature summary extracted from

  • Caillet, J.; Nogueira, T.; Masquida, B.; Winter, F.; Graffe, M.; Dock-Bregeon, A.C.; Torres-Larios, A.; Sankaranarayanan, R.; Westhof, E.; Ehresmann, B.; Ehresmann, C.; Romby, P.; Springer, M.
    The modular structure of Escherichia coli threonyl-tRNA synthetase as both an enzyme and a regulator of gene expression (2003), Mol. Microbiol., 47, 961-974.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.3 overexpression of wild-type and mutants in the null mutant strain Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.3 D549A modified interation of anticodon loop/C-ter domain, activity similar to the wild-type Escherichia coli
6.1.1.3 E258K modified interation with the superrepressor, no activity Escherichia coli
6.1.1.3 E259K modified interation with the superrepressor, unaltered activity Escherichia coli
6.1.1.3 E600A modified interation of anticodon loop/C-ter domain, 710fold increased activity Escherichia coli
6.1.1.3 K246A modified interation of acceptor stem and catalytic domain, 2.9fold increased activity Escherichia coli
6.1.1.3 K249A modified interation of acceptor stem and catalytic domain, 3.5fold increased activity Escherichia coli
6.1.1.3 K577A modified interation of anticodon loop/C-ter domain, 118fold increased activity Escherichia coli
6.1.1.3 additional information construction of chromosomal disruption null mutant strain with no activity, construction of a truncated mutant lacking the N1 and N2 domains, 93.5fold increased activity Escherichia coli
6.1.1.3 N324A modified interation of cross-subunit contacts, 3.5fold increased activity Escherichia coli
6.1.1.3 N502A modified interation of cross-subunit contacts, 2.1fold increased activity Escherichia coli
6.1.1.3 N575A modified interation of anticodon loop/C-ter domain, 9.4fold increased activity Escherichia coli
6.1.1.3 R349A modified interation of cross-subunit contacts, 42fold increased activity Escherichia coli
6.1.1.3 R583H modified interation of anticodon loop/C-ter domain, no activity Escherichia coli
6.1.1.3 R609A modified interation of anticodon loop/C-ter domain, 35fold activity Escherichia coli
6.1.1.3 S347A modified interation of cross-subunit contacts, similar to the wild-type Escherichia coli
6.1.1.3 S367A modified interation of acceptor stem and catalytic domain, 11fold increased activity Escherichia coli
6.1.1.3 Y205F modified interation of acceptor stem and N-terminal domain, 7.7fold increased activity Escherichia coli
6.1.1.3 Y219F modified interation of acceptor stem and N-terminal domain, similar to the wild-type Escherichia coli
6.1.1.3 Y348F modified interation of cross-subunit contacts, 6.5fold increased activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.3 additional information
-
 additional information mutant enzymes complementing the null mutant Escherichia coli
6.1.1.3 0.00003
-
 L-threonine wild-type enzyme complementing the null mutant Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.3 ATP + L-threonine + tRNAThr Escherichia coli
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 ?
6.1.1.3 additional information Escherichia coli regulation mechanism, 2 essential steps of regulation are operator recognition and inhibition of ribosome binding performed by different domains of the enzyme ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.3 Escherichia coli
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
6.1.1.3 ATP + L-threonine + tRNAThr = AMP + diphosphate + L-threonyl-tRNAThr the catalytic domain is located at the C-terminus of the enzyme Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 ?
6.1.1.3 ATP + L-threonine + tRNAThr tRNA aminoacylation Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 ?
6.1.1.3 additional information enzyme also has a regulatory function by binding the so-called operator site located in the leader of its own mRNA and thereby inhibits translational initiation by competing with ribosome binding Escherichia coli ?
-
 ?
6.1.1.3 additional information regulation mechanism, 2 essential steps of regulation are operator recognition and inhibition of ribosome binding performed by different domains of the enzyme Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.3 Synthetase, threonyl-transfer ribonucleate
-
 Escherichia coli
6.1.1.3 Threonine translase
-
 Escherichia coli
6.1.1.3 Threonine--tRNA ligase
-
 Escherichia coli
6.1.1.3 Threonine-transfer ribonucleate synthetase
-
 Escherichia coli
6.1.1.3 Threonyl-ribonucleic synthetase
-
 Escherichia coli
6.1.1.3 Threonyl-transfer ribonucleate synthetase
-
 Escherichia coli
6.1.1.3 Threonyl-transfer ribonucleic acid synthetase
-
 Escherichia coli
6.1.1.3 Threonyl-transfer RNA synthetase
-
 Escherichia coli
6.1.1.3 Threonyl-tRNA synthetase
-
 Escherichia coli
6.1.1.3 ThrRS
-
 Escherichia coli
6.1.1.3 TRS
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.3 additional information
-
 additional information mutant enzymes complementing the null mutant Escherichia coli
6.1.1.3 0.64
-
 L-threonine wild-type enzyme complementing the null mutant Escherichia coli
6.1.1.3 6.08
-
 L-threonine wild-type enzyme complementing the null mutant Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 ATP
-
 Escherichia coli