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Literature summary extracted from

  • Covarrubias, A.S.; Högbom, M.; Bergfors, T.; Carroll, P.; Mannerstedt, K.; Oscarson, S.; Parish, T.; Jones, T.A.; Mowbray, S.L.
    Structural, biochemical, and in vivo investigations of the threonine synthase from Mycobacterium tuberculosis (2008), J. Mol. Biol., 381, 622-633.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.3.1 expressed as a His-tagged fusion protein Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.2.3.1 refined to 2.5 A. The structure of MtTS has a homodimeric organization in which the two subunits are related by a non-crystallographic 2fold axis. Each subunit is composed of three domains Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
4.2.3.1 additional information a deletion of the MtTS gene generated a strain of Mycobacterium tuberculosis that requires threonine for growth Mycobacterium tuberculosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.3.1 1.2
-
O-phospho-L-homoserine
-
Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
4.2.3.1 Mycobacterium tuberculosis P9WG59
-
-
4.2.3.1 Mycobacterium tuberculosis H37Rv P9WG59
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.3.1 using Ni-NTA chromatography Mycobacterium tuberculosis

Reaction

EC Number Reaction Comment Organism Reaction ID
4.2.3.1 O-phospho-L-homoserine + H2O = L-threonine + phosphate analyzed crystal structure gives new insights into the catalytic mechanism of threonine synthase in general, specifically by suggesting the direct involvement of the phosphate moiety of the cofactor, rather than the inorganic phosphate product, in transferring a proton from C4 to Cgamma in the formation of the alphabeta-unsaturated aldimine Mycobacterium tuberculosis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.3.1 1.05
-
-
Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.3.1 O-phospho-L-homoserine + H2O
-
Mycobacterium tuberculosis L-threonine + phosphate
-
?
4.2.3.1 O-phospho-L-homoserine + H2O
-
Mycobacterium tuberculosis H37Rv L-threonine + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
4.2.3.1 homodimer crystal structure Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
4.2.3.1 MtTS
-
Mycobacterium tuberculosis
4.2.3.1 threonine synthase
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.3.1 25
-
assay at Mycobacterium tuberculosis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.2.3.1 60
-
MtTS loses less than 10% of the initial activity during a 10 min incubation Mycobacterium tuberculosis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.3.1 7.3
-
O-phospho-L-homoserine
-
Mycobacterium tuberculosis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.3.1 8.4
-
assay at Mycobacterium tuberculosis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.2.3.1 7
-
MtTS is inactivated at pH 7 or below Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
4.2.3.1 pyridoxal 5'-phosphate MtTS is not influenced by S-adenosylmethionine Mycobacterium tuberculosis