5.3.1.23: S-methyl-5-thioribose-1-phosphate isomerase

This is an abbreviated version!
For detailed information about S-methyl-5-thioribose-1-phosphate isomerase, go to the full flat file.

Reaction

Synonyms

1-PMTR isomerase, 5'-methylthioribose-1-phosphate isomerase, 5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase, 5-methylthioribose 1-phosphate isomerase, 5-methylthioribose-1-phosphate isomerase, Bs-M1Pi, Isomerase, methylthioribose 1-phosphate, M1Pi, methylthioribose-1-phosphate isomerase, Meu1p, MRDI, MRI1, Mri1p, mtnA, MTR-1-P, MTR-1-P isomerase, PH0702, PhM1Pi, Ypr118w, Ypr118wp

ECTree

     5 Isomerases

         5.3 Intramolecular oxidoreductases

             5.3.1 Interconverting aldoses and ketoses, and related compounds

                5.3.1.23 S-methyl-5-thioribose-1-phosphate isomerase

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7	Crystallization (Commentary)
7	Disease/ Diagnostics
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13	General Information
1	Inhibitors
1	kcat/KM [mM/s]
2	KM Value [mM]
4	Localization
3	Metals/Ions
2	Molecular Weight [Da]
12	Natural Substrates/ Products (Substrates)
23	Organism
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28	PDB ID
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19	Substrates and Products (Substrate)
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46	Synonyms
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1	Turnover Number [1/s]

General Information

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General Information on EC 5.3.1.23 - S-methyl-5-thioribose-1-phosphate isomerase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

Pyrococcus horikoshii

O58433

the enzyme is a member of the family PF01008. The open and closed states of the proteins belonging to the family PF01008 are usually demarcated by the degree of angle formed owing to the bend in the longest helix alpha5

761764

metabolism

4 entries

physiological function

5 entries

additional information

4 entries

metabolism

Bacillus subtilis

O31662

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

760727

metabolism

Bacillus subtilis

O31662

the methionine salvage pathway (MSP) plays a crucial role in recycling a sulfhydryl derivative of the nucleoside. In MSP of Bacillus subtilis, the 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes a conversion of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P)

762331

metabolism

Bacillus subtilis 168

-

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

-

metabolism

Bacillus subtilis 168

-

the methionine salvage pathway (MSP) plays a crucial role in recycling a sulfhydryl derivative of the nucleoside. In MSP of Bacillus subtilis, the 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes a conversion of 5-methylthioribose 1-phosphate (MTR-1-P) to 5-methylthioribulose 1-phosphate (MTRu-1-P)

-

physiological function

Homo sapiens

-

MRDI is induced in metastatic cells by constitutive RhoA activation and promotes cell invasion

705716

physiological function

Bacillus subtilis

O31662

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

760727

physiological function

Bacillus subtilis

O31662

in the methionine salvage pathway (MSP) of Bacillus subtilis, 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes an interconversion of 5-methylthioribose 1-phosphate (MTR-1-P) and 5-methylthioribulose 1-phosphate (MTRu-1-P), classified as an aldose-ketose isomerase reaction

762331

physiological function

Bacillus subtilis 168

-

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

-

physiological function

Bacillus subtilis 168

-

in the methionine salvage pathway (MSP) of Bacillus subtilis, 5-methylthioribose 1-phosphate isomerase (M1Pi) catalyzes an interconversion of 5-methylthioribose 1-phosphate (MTR-1-P) and 5-methylthioribulose 1-phosphate (MTRu-1-P), classified as an aldose-ketose isomerase reaction

-

additional information

Bacillus subtilis

O31662

enzyme structure and active site structure comparisons. The highly conserved residues at the active site, Cys160 and Asp240, are most likely to be involved in catalysis, structure-function analysis and catalytic mechanism, overview. Two variants of isomerization mechanism are possible, the enediol and the hydride transfer mechanism. M1Pi does not require any metals to exhibit its catalytic activity, which is analogous to the enzymes that proceed via a cis-enediol intermediate. On the other hand, NMR and mass spectrometry suggest the isomerase reaction of M1Pi in D2O proceeds without incorporation of deuterium from solvent into the product, resembling those measurements of xylose isomerase (XI), which adopts the hydride transfer mechanism, but which also requires two divalent cations such as Mg2+ or Mn2+. The hydrophobic interaction of the methylthio group includes the side chains of Pro54, Ala162, Ala166, and Thr167. The side chain of Asp240 is surrounded by the hydrophobic pocket formed by residues Thr96, Ala97, and Phe317, which are absolutely conserved in all M1Pis. This hydrophobic pocket appears to restrict the rotation of the Asp240 side chain, which may permit a favorable interaction with the substrate (or product). The pKa of Asp240 is likely to be increased, which might enable Asp240 to play a dual role as a proton donor/acceptor

762331

additional information

Bacillus subtilis

-

enzyme structure and active site structure comparisons. The highly conserved residues at the active site, Cys160 and Asp240, are most likely to be involved in catalysis, structure-function analysis and catalytic mechanism, overview. Two variants of isomerization mechanism are possible, the enediol and the hydride transfer mechanism. M1Pi does not require any metals to exhibit its catalytic activity, which is analogous to the enzymes that proceed via a cis-enediol intermediate. On the other hand, NMR and mass spectrometry suggest the isomerase reaction of M1Pi in D2O proceeds without incorporation of deuterium from solvent into the product, resembling those measurements of xylose isomerase (XI), which adopts the hydride transfer mechanism, but which also requires two divalent cations such as Mg2+ or Mn2+. The hydrophobic interaction of the methylthio group includes the side chains of Pro54, Ala162, Ala166, and Thr167. The side chain of Asp240 is surrounded by the hydrophobic pocket formed by residues Thr96, Ala97, and Phe317, which are absolutely conserved in all M1Pis. This hydrophobic pocket appears to restrict the rotation of the Asp240 side chain, which may permit a favorable interaction with the substrate (or product). The pKa of Asp240 is likely to be increased, which might enable Asp240 to play a dual role as a proton donor/acceptor

762331

additional information

Pyrococcus horikoshii

O58433

transition from an open to closed state creates a hydrophobic active site environment. The active-site pocket of M1Pi is optimized to follow a reaction mechanism via the formation of a cis-phosphoenolate intermediate, structural transition, overview

761764

additional information

Bacillus subtilis 168

-

enzyme structure and active site structure comparisons. The highly conserved residues at the active site, Cys160 and Asp240, are most likely to be involved in catalysis, structure-function analysis and catalytic mechanism, overview. Two variants of isomerization mechanism are possible, the enediol and the hydride transfer mechanism. M1Pi does not require any metals to exhibit its catalytic activity, which is analogous to the enzymes that proceed via a cis-enediol intermediate. On the other hand, NMR and mass spectrometry suggest the isomerase reaction of M1Pi in D2O proceeds without incorporation of deuterium from solvent into the product, resembling those measurements of xylose isomerase (XI), which adopts the hydride transfer mechanism, but which also requires two divalent cations such as Mg2+ or Mn2+. The hydrophobic interaction of the methylthio group includes the side chains of Pro54, Ala162, Ala166, and Thr167. The side chain of Asp240 is surrounded by the hydrophobic pocket formed by residues Thr96, Ala97, and Phe317, which are absolutely conserved in all M1Pis. This hydrophobic pocket appears to restrict the rotation of the Asp240 side chain, which may permit a favorable interaction with the substrate (or product). The pKa of Asp240 is likely to be increased, which might enable Asp240 to play a dual role as a proton donor/acceptor

-