Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Minajigi, A.; Deng, B.; Francklyn, C.S.
    Fidelity escape by the unnatural amino acid beta-hydroxynorvaline: an efficient substrate for Escherichia coli threonyl-tRNA synthetase with toxic effects on growth (2011), Biochemistry, 50, 1101-1109.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.1.1.3 additional information 3-hydroxynorvaline enhances the ATPase function of the synthetic site, at a rate not increased by nonaminoacylatable tRNA Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.3 expression of His-tagged ThrRS 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 pre-steady-state kinetics, kinetics of ATPase activity in presence of 3-hydroxynorvaline, overview Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.3 Mg2+ required Escherichia coli

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
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.3 recombinant His-tagged ThrRS by nickel affinity chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.3 ATP + 3-hydroxynorvaline + tRNAThr the specificity constant kcat/KM for beta-hydroxynorvaline is only 20-30fold less than that of cognate threonine, amino acid activation is the potential rate-limiting step of b3-hydroxynorvaline aminoacylation Escherichia coli AMP + diphosphate + 3-hydroxynorvalyl-tRNAThr
-
 ?
6.1.1.3 ATP + L-threonine + tRNAThr
-
 Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 ?
6.1.1.3 ATP + L-threonine + tRNAThr for cognate threonine, amino acid activation is likely to be the rate-limiting step. The inability of wild-type ThrRS to prevent utilization of beta-hydroxynorvaline as a substrate illustrates that the naturally occurring enzyme lacks the capability to effectively discriminate against nonproteogenic amino acids that are not encountered under normal physiological conditions Escherichia coli AMP + diphosphate + L-threonyl-tRNAThr
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.1.1.3 37
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.1.1.3 8
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 ATP
-
 Escherichia coli