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Literature summary extracted from

  • Laber, B.; Maurer, W.; Hanke, C.; Graefe, S.; Ehlert, S.; Messerschmidt, A.; Clausen, T.
    Characterization of recombinant Arabidopsis thaliana threonine synthase (1999), Eur. J. Biochem., 263, 212-221.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.2.3.1 S-adenosylmethionine same binding site as inhibitor AMP, 85fold increase of activity, maximum activity at 0.06-0.25 mM Arabidopsis thaliana

Application

EC Number Application Comment Organism
4.2.3.1 agriculture possible herbicide target Arabidopsis thaliana

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.1 expressed in Escherichia coli Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.3.1 x-ray diffraction studies Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.3.1 AMP same binding site as S-adenosylmethionine Arabidopsis thaliana

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.3.1 0.03
-
 O-phosphohomoserine in presence of S-adenosylmethionine Arabidopsis thaliana
4.2.3.1 0.12
-
 O-phosphohomoserine without S-adenosylmethionine Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
4.2.3.1 chloroplast
-
 Arabidopsis thaliana 9507
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.3.1 58000
-
 2 * 58000, comparison of nucleotide sequence and molecular mass of native enzyme Arabidopsis thaliana
4.2.3.1 110000
-
 gel filtration Arabidopsis thaliana

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.1 Arabidopsis thaliana
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.3.1
-
 Arabidopsis thaliana

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.1 O-phospho-L-homoserine + H2O
-
 Arabidopsis thaliana L-threonine + phosphate
-
 ir

Subunits

EC Number Subunits Comment Organism
4.2.3.1 dimer 2 * 58000, comparison of nucleotide sequence and molecular mass of native enzyme Arabidopsis thaliana
4.2.3.1 dimer N-terminal amino acids involved in dimerization Arabidopsis thaliana

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.3.1 20
-
 enzyme assay at Arabidopsis thaliana

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.3.1 0.0333
-
 O-phosphohomoserine without S-adenosylmethionine Arabidopsis thaliana
4.2.3.1 0.86
-
 O-phosphohomoserine in presence of S-adenosylmethionine Arabidopsis thaliana

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.3.1 8.5
-
 enzyme assay at Arabidopsis thaliana