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

BRENDA support

Literature summary for 6.1.1.11 extracted from

  • Godinic-Mikulcic, V.; Jaric, J.; Hausmann, C.D.; Ibba, M.; Weygand-Durasevic, I.
    An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions (2011), J. Biol. Chem., 286, 3396-3404.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
co-expression of MtSerRS with arginyl-tRNA synthetase, MtArgRS, EC 6.1.1.19, from in the Saccharomyces cerevisiae two-hybrid system using yeast strain MaV203 Methanothermobacter thermautotrophicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information addition of MtArgRS to MtSerRS leads to an almost 4fold increase in the catalytic efficiency of serine attachment to tRNA, also under conditions of elevated temperature and osmolarity, but has no effect on the activity of MtArgRS, steady-state kinetic analyses, overview Methanothermobacter thermautotrophicus
0.002
-
tRNASer pH 7.5, 50°C, recombinant MtSerRS in presence of recombinant MtArgRS Methanothermobacter thermautotrophicus
0.00561
-
tRNASer pH 7.5, 50°C, recombinant MtSerRS Methanothermobacter thermautotrophicus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-serine + tRNASer Methanothermobacter thermautotrophicus
-
AMP + diphosphate + L-seryl-tRNASer
-
?
additional information Methanothermobacter thermautotrophicus seryl-tRNA synthetase, MtSerRS, directly and stably interacts with arginyl-tRNA synthetase, MtArgRS, EC 6.1.1.19, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C ?
-
?

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
GST-MtArgRS shows the ability to co-purify with His-tagged MtSerRS by nickel affinity chromatography, co-elution of the two enzymes during gel filtration Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-serine + tRNASer
-
Methanothermobacter thermautotrophicus AMP + diphosphate + L-seryl-tRNASer
-
?
additional information seryl-tRNA synthetase, MtSerRS, directly and stably interacts with arginyl-tRNA synthetase, MtArgRS, EC 6.1.1.19, two-hybrid system and surface plasmon resonance analysis, overview. The MtSerRS-MtArgRS complex also contains tRNAArg, consistent with the existence of a stable ribonucleoprotein complex active in aminoacylation. Deletion of the HTH motif, which contributes to the stability of SerRS dimers, significantly weakens the interaction between the two synthetases. Stimulation by MtArgRS peaks at 65°C Methanothermobacter thermautotrophicus ?
-
?

Synonyms

Synonyms Comment Organism
mtSerRS
-
Methanothermobacter thermautotrophicus
SerRS
-
Methanothermobacter thermautotrophicus
Seryl-tRNA synthetase
-
Methanothermobacter thermautotrophicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
assay at Methanothermobacter thermautotrophicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0073
-
tRNASer pH 7.5, 50°C, recombinant MtSerRS Methanothermobacter thermautotrophicus
0.1
-
tRNASer pH 7.5, 50°C, recombinant MtSerRS in presence of recombinant MtArgRS Methanothermobacter thermautotrophicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Methanothermobacter thermautotrophicus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Methanothermobacter thermautotrophicus