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Literature summary for 6.1.1.3 extracted from

  • Minajigi, A.; Francklyn, C.S.
    Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase (2010), J. Biol. Chem., 285, 23810-23817.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.3

Protein Variants

Protein Variants Comment Organism
H73A site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, and a 2fold higher rate of ATP consumption relative to the rate of Ser-tRNAThr synthesis Escherichia coli
H73A/H309A site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, and a 2fold higher rate of ATP consumption relative to the rate of Ser-tRNAThr synthesis Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-threonine + tRNAThr Escherichia coli
-
 AMP + diphosphate + L-threonyl-tRNAThr
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-threonine + tRNAThr
-
 Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 ?
additional information in the pre-steady state, asymmetric activation of cognate threonine and noncognate serine is observed in the active sites of dimeric ThrRS, with similar rates of activation. In the absence of tRNA, seryl-adenylate is hydrolyzed 29old faster by the ThrRS catalytic domain than threonyl-adenylate. The rate of seryl transfer to cognate tRNA is only 2fold slower than threonine Escherichia coli ?
-
 ?

Subunits

Subunits Comment Organism
dimer
-
 Escherichia coli

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the class II aminoacyl-tRNA synthetases Escherichia coli
Threonyl-tRNA synthetase
-
 Escherichia coli
ThrRS
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information rate constants for adenylate synthesis by ThrRS in the absence of tRNA, overview Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function amino acid discrimination does not occur at the aminoacyl transfer step. pre-Transfer hydrolysis contributes to proofreading only when the rate of transfer is slowed significantly. Thus, the relative contributions of pre- and posttransfer editing in ThrRS are subject to modulation by the rate of aminoacyl transfer Escherichia coli