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

BRENDA support

Literature summary for 4.2.1.109 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
Search for more literature for 4.2.1.109

Cloned(Commentary)

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O31668 trp C2
-
Bacillus subtilis 168 O31668 trp C2
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits Comment Organism
homotetramer 4 * 23800 Bacillus subtilis

Synonyms

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 8
-
 Bacillus subtilis

pH Range

pH Minimum pH Maximum Comment Organism
6.5 10.5
-
 Bacillus subtilis