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Literature summary extracted from

  • Ashida, H.; Saito, Y.; Kojima, C.; Yokota, A.
    Enzymatic characterization of 5-methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway in Bacillus subtilis (2008), Biosci. Biotechnol. Biochem., 72, 959-967.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.2.1.109 expressed as (His)6-tagged soluble protein in Escherichia BL21 (DE3), vector pET15b Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.109 0.0089
-
S-methyl-5-thio-D-ribulose 1-phosphate 25°C Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.109 additional information MtnB requires metal ions for catalysis, but it is unclear what kind of metal ions are bound to the MtnB purified from Escherichia coli cells. Considering that FucA/RibE/RhuA-related enzymes require the zinc ion for optimal catalysis under physiological conditions and that recombinant class II aldolase enzymes expressed in Escherichia coli cells are almost all of the Zn2+ form, purified MtnB might also be of the Zn2+ form Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.109 23800
-
4 * 23800 Bacillus subtilis
4.2.1.109 90000
-
without His-tag, 4 * 23800, SDS-PAGE Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.109 S-methyl-5-thio-D-ribulose 1-phosphate Bacillus subtilis
-
5-(methylthio)-2,3-dioxopentyl phosphate + H2O
-
?
4.2.1.109 S-methyl-5-thio-D-ribulose 1-phosphate Bacillus subtilis 168
-
5-(methylthio)-2,3-dioxopentyl phosphate + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.109 Bacillus subtilis O31668 trp C2
-
4.2.1.109 Bacillus subtilis 168 O31668 trp C2
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.109 homogeneity, using the His-tag, the His-tag is cleaved with thrombin Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.109 S-methyl-5-thio-D-ribulose 1-phosphate
-
Bacillus subtilis 5-(methylthio)-2,3-dioxopentyl phosphate + H2O
-
?
4.2.1.109 S-methyl-5-thio-D-ribulose 1-phosphate
-
Bacillus subtilis 5-(methylthio)-2,3-dioxopentyl phosphate + H2O the reaction product 5-(methylthio)-2,3-dioxopentyl phosphate is so labile that its chemical structure could not be isolated and analyzed ?
4.2.1.109 S-methyl-5-thio-D-ribulose 1-phosphate
-
Bacillus subtilis 168 5-(methylthio)-2,3-dioxopentyl phosphate + H2O
-
?
4.2.1.109 S-methyl-5-thio-D-ribulose 1-phosphate
-
Bacillus subtilis 168 5-(methylthio)-2,3-dioxopentyl phosphate + H2O the reaction product 5-(methylthio)-2,3-dioxopentyl phosphate is so labile that its chemical structure could not be isolated and analyzed ?

Subunits

EC Number Subunits Comment Organism
4.2.1.109 homotetramer 4 * 23800 Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
4.2.1.109 5-Methylthioribulose-1-phosphate
-
Bacillus subtilis
4.2.1.109 MtnB
-
Bacillus subtilis
4.2.1.109 MTRu-1-P dehydratase
-
Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.2.1.109 40
-
at 55°C the enzyme loses most of its activity Bacillus subtilis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4.2.1.109 15 55 at 55°C the enzyme loses most of its activity Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.2.1.109 16.5
-
S-methyl-5-thio-D-ribulose 1-phosphate
-
Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.109 7.5 8
-
Bacillus subtilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.2.1.109 6.5 10.5
-
Bacillus subtilis