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Literature summary extracted from

  • Saito, Y.; Ashida, H.; Kojima, C.; Tamura, H.; Matsumura, H.; Kai, Y.; Yokota, A.
    Enzymatic characterization of 5-methylthioribose 1-phosphate isomerase from Bacillus subtilis (2007), Biosci. Biotechnol. Biochem., 71, 2021-2028 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.1.23 gene mtnA, sequence comparisons and phylogenetic tree, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.1.23 additional information
-
 additional information Michaelis-Menten kinetics Bacillus subtilis
5.3.1.23 0.138
-
 S-methyl-5-thio-alpha-D-ribose 1-phosphate pH 8.1, 35°C Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.3.1.23 additional information the activity is not at all influenced by EDTA treatment, indicating that the Bacillus subtilis MTR-1-P isomerase does not require a metal ion for its catalysis Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.3.1.23 76000
-
 recombinant enzyme, gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.1.23 S-methyl-5-thio-alpha-D-ribose 1-phosphate Bacillus subtilis
-
 S-methyl-5-thio-D-ribulose 1-phosphate
-
 r
5.3.1.23 S-methyl-5-thio-alpha-D-ribose 1-phosphate Bacillus subtilis 168
-
 S-methyl-5-thio-D-ribulose 1-phosphate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.3.1.23 Bacillus subtilis O31662
-
-
5.3.1.23 Bacillus subtilis 168 O31662
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.1.23 recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, the tag is cleaved off by thrombin, followed by gel filtration Bacillus subtilis

Reaction

EC Number Reaction Comment Organism Reaction ID
5.3.1.23 S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate proposed reaction mechanism probably including residue Asp240, overview Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.1.23 additional information substrate MTR-1-P is synthesized from S-adenosyl-L-methionine through hydrolysis of the adenine base by HCl, and C1 of the ribose moiety is phosphorylated by ATP via MtnK, an MTR kinase. MTR-1-P isomerase is assayed in a coupling reaction with MtnB and MtnW, previously identified as MTRu-1-P dehydratase and 2,3-diketo-5-methylthiopentyl-1-phosphate enolase respectively. In this assay, the reaction product MTRu-1-P is converted to 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) by sequential reactions of MtnB and MtnW. NMR analysis of the MtnA reaction product, overview Bacillus subtilis ?
-
-
5.3.1.23 additional information substrate MTR-1-P is synthesized from S-adenosyl-L-methionine through hydrolysis of the adenine base by HCl, and C1 of the ribose moiety is phosphorylated by ATP via MtnK, an MTR kinase. MTR-1-P isomerase is assayed in a coupling reaction with MtnB and MtnW, previously identified as MTRu-1-P dehydratase and 2,3-diketo-5-methylthiopentyl-1-phosphate enolase respectively. In this assay, the reaction product MTRu-1-P is converted to 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P) by sequential reactions of MtnB and MtnW. NMR analysis of the MtnA reaction product, overview Bacillus subtilis 168 ?
-
-
5.3.1.23 S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
 Bacillus subtilis S-methyl-5-thio-D-ribulose 1-phosphate
-
 r
5.3.1.23 S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
 Bacillus subtilis 168 S-methyl-5-thio-D-ribulose 1-phosphate
-
 r

Subunits

EC Number Subunits Comment Organism
5.3.1.23 homodimer 2 * 38900, detagged recombinant enzyme, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
5.3.1.23 5-methylthioribose 1-phosphate isomerase
-
 Bacillus subtilis
5.3.1.23 mtnA
-
 Bacillus subtilis
5.3.1.23 MTR-1-P isomerase
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.1.23 35
-
-
 Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
5.3.1.23 13
-
 S-methyl-5-thio-alpha-D-ribose 1-phosphate pH 8.1, 35°C Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.1.23 8.1
-
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
5.3.1.23 metabolism the enzyme is part of the methionine salvage pathway (MSP) is a metabolic pathway for recovery of the reduced sulfur in 5-methylthioribose (MTR), which is formed in the synthesis of polyamines, as methionine Bacillus subtilis
5.3.1.23 physiological function enzyme MtnA of Bacillus subtilis catalyzes the isomerization of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P). The reaction is an isomerization of an aldose phosphate harboring a phosphate group on the hemiacetal group Bacillus subtilis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.3.1.23 94.2
-
 S-methyl-5-thio-alpha-D-ribose 1-phosphate pH 8.1, 35°C Bacillus subtilis