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

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

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EC NUMBER
COMMENTARY hide
5.3.1.23
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RECOMMENDED NAME
GeneOntology No.
S-methyl-5-thioribose-1-phosphate isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
S-methyl-5-thio-alpha-D-ribose 1-phosphate degradation
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S-methyl-5-thio-alpha-D-ribose 1-phosphate degradation II
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methionine metabolism
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Cysteine and methionine metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
S-methyl-5-thio-alpha-D-ribose-1-phosphate aldose-ketose-isomerase
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CAS REGISTRY NUMBER
COMMENTARY hide
91608-95-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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MRDI is induced in metastatic cells by constitutive RhoA activation and promotes cell invasion
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-Methylthio-5-deoxy-D-ribose 1-phosphate
5-Methylthio-5-deoxy-D-ribulose 1-phosphate
show the reaction diagram
5-Methylthio-5-deoxy-D-ribose 1-phosphate
?
show the reaction diagram
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5-Methylthio-5-deoxy-D-ribose 1-phosphate
?
show the reaction diagram
S-methyl-5-thio-alpha-D-ribose 1-phosphate
S-methyl-5-thio-D-ribulose 1-phosphate
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
RNAi
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stable knockdown of MRDI is carried out in A-375 cells
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
RhoA
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MRDI is induced by RhoA and mediates RhoA-dependent cell invasion
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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clone A has 5-methylthioribose-1-phosphate isomerase activity, clone D lacks this enzyme
Manually annotated by BRENDA team
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cocrystallized with the substrate 5-methylthio-5-deoxy-D-ribose 1-phosphate, sitting drop vapour diffusion method, using 0.2 M K formate and 15% (w/v) polyethylene glycol 3350, at 20�C
sitting-drop vapour-diffusion method. Crystals diffract to 2.5 A at 100 K using synchrotron radiation and belong to the tetragonal space group P4(1), with unit-cell parameters a = b = 69.2 A, c = 154.7 A
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hanging drop vapor diffusion method, using 0.7 M sodium citrate and 100 mM imidazole, pH 8.0
in silico analysis of conserved residues and molecular modeling of structure. Residues of the enzymic activity of methylthioribose-1-phosphate isomerase that interact with the substrate are absolutely conserved. Residues essential for the hydrophobic stabilization of the substrate/product in the active site are conserved as well
sitting-drop vapour-diffusion method
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by nickel-nitrilotriacetic acid affinity chromatography, the His-tag is removed by treatment with tobacco etch virus protease
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
into pCMV plasmid for expression in mammalian cells and into pMS356 plasmid for esxpression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
RhoA induces expression of MRDI
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C168S
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inactive mutant
D248A
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inactive mutant
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LINKS TO OTHER DATABASES (specific for EC-Number 5.3.1.23)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)