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Literature summary extracted from

  • Ling, J.; Peterson, K.M.; Simonovic, I.; Soell, D.; Simonovic, M.
    The mechanism of pre-transfer editing in yeast mitochondrial threonyl-tRNA synthetase (2012), J. Biol. Chem., 287, 28518-28525.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.3 expressed in Escherichia coli Rosetta pLysS cells Saccharomyces cerevisiae

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.1.1.3 complexed with an analog of Ser-AMP, sitting drop vapor diffusion method, using 0.1 M Na2HPO4/KH2PO4 (pH 6.2), 0.2 M NaCl, 10% (w/v) PEG 8000 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.1.1.3 0.3
-
L-threonine in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C Saccharomyces cerevisiae
6.1.1.3 120
-
L-serine in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.1.1.3 mitochondrion
-
Saccharomyces cerevisiae 5739
-

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-serine + tRNASer Saccharomyces cerevisiae yeast mitochondrial threonyl-tRNA synthetase MST1 lacks an editing domain and utilizes pre-transfer editing to discriminate against serine. MST1 misactivates serine and edits seryl adenylate (Ser-AMP) in the absence of the cognate tRNA. MST1 hydrolyzes 80% of misactivated Ser-AMP at a rate 4fold higher than that for the cognate threonyl adenylate (Thr-AMP) while releasing 20% of Ser-AMP into the solution. ?
-
?
6.1.1.3 ATP + L-threonine + tRNAThr Saccharomyces cerevisiae
-
AMP + diphosphate + L-threonyl-tRNAThr
-
?
6.1.1.3 additional information Saccharomyces cerevisiae no activity with L-Val, L-Ala, or L-Cys ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.3 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.1.1.3 Ni2+ affinity column chromatography Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.3 ATP + L-serine + tRNASer yeast mitochondrial threonyl-tRNA synthetase MST1 lacks an editing domain and utilizes pre-transfer editing to discriminate against serine. MST1 misactivates serine and edits seryl adenylate (Ser-AMP) in the absence of the cognate tRNA. MST1 hydrolyzes 80% of misactivated Ser-AMP at a rate 4fold higher than that for the cognate threonyl adenylate (Thr-AMP) while releasing 20% of Ser-AMP into the solution. Saccharomyces cerevisiae ?
-
?
6.1.1.3 ATP + L-threonine + tRNAThr
-
Saccharomyces cerevisiae AMP + diphosphate + L-threonyl-tRNAThr
-
?
6.1.1.3 additional information no activity with L-Val, L-Ala, or L-Cys Saccharomyces cerevisiae ?
-
?

Synonyms

EC Number Synonyms Comment Organism
6.1.1.3 Mst1
-
Saccharomyces cerevisiae
6.1.1.3 Threonyl-tRNA synthetase
-
Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.1.1.3 1.83
-
L-serine in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C Saccharomyces cerevisiae
6.1.1.3 3.32
-
L-threonine in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.3 ATP
-
Saccharomyces cerevisiae

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.1.1.3 0.016
-
L-serine in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C Saccharomyces cerevisiae
6.1.1.3 11.18
-
L-threonine in 100 mM Na-HEPES (pH 7.2), 30 mM KCl, 10 mM MgCl2, 2 mM potassium fluoride, at 37°C Saccharomyces cerevisiae