Literature summary for 5.3.1.23 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 .

Search for more literature for 5.3.1.23

Cloned(Commentary)

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

KM Value [mM]

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O31662	-	-
Bacillus subtilis 168	O31662	-	-

Purification (Commentary)

Purification (Comment)	Organism
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

Reaction	Comment	Organism	Reaction ID
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	-
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	?	-	-
S-methyl-5-thio-alpha-D-ribose 1-phosphate	-	Bacillus subtilis	S-methyl-5-thio-D-ribulose 1-phosphate	-	r
S-methyl-5-thio-alpha-D-ribose 1-phosphate	-	Bacillus subtilis 168	S-methyl-5-thio-D-ribulose 1-phosphate	-	r

Subunits

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

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.1	-	-	Bacillus subtilis

General Information

General Information	Comment	Organism
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
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]

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

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Release 2023.1 (January 2023)