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

RECOMMENDED NAMEGeneOntology No.
S-methyl-5-thioribose-1-phosphate isomeraseGO:0046523

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
show the reaction diagram		----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
intramolecular oxidoreduction----
isomerization----
isomerizationHomo sapiens--705716

PATHWAYKEGG LinkMetaCyc Link
S-methyl-5-thio-alpha-D-ribose 1-phosphate degradation-PWY-6755

SYSTEMATIC NAMEIUBMB Comments
S-methyl-5-thio-alpha-D-ribose-1-phosphate aldose-ketose-isomerase-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
1-PMTR isomerase----
5'-methylthioribose-1-phosphate isomeraseSaccharomyces cerevisiae--692309
5-methylthio-5-deoxy-D-ribose-1-phosphate ketol-isomerase----
5-methylthioribose 1-phosphate isomeraseBacillus subtilisO31662-695004
5-methylthioribose-1-phosphate isomerase----
Isomerase, methylthioribose 1-phosphate----
M1PiBacillus subtilisO31662-695004
methylthioribose-1-phosphate isomeraseSaccharomyces cerevisiae--662258, 692309
methylthioribose-1-phosphate isomeraseHomo sapiens--705716
Meu1pSaccharomyces cerevisiae--692309
MRDIHomo sapiens-mediator of Rho-dependent invasion705716
MRI1Saccharomyces cerevisiae--692309
Mri1pSaccharomyces cerevisiae--692309
Ypr118wSaccharomyces cerevisiae--662258
Ypr118wpSaccharomyces cerevisiae--692309

CAS REGISTRY NUMBERCOMMENTARY
91608-95-6-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Bacillus subtilis-660630--Manually annotated by BRENDA team
Bacillus subtilis-695004O31662UniprotManually annotated by BRENDA team
Homo sapiens-2661, 705716--Manually annotated by BRENDA team
Klebsiella pneumoniae-2660--Manually annotated by BRENDA team
Rattus norvegicus-2659--Manually annotated by BRENDA team
Saccharomyces cerevisiae-662258, 692309--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionHomo sapiens-MRDI is induced in metastatic cells by constitutive RhoA activation and promotes cell invasion705716

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
5-Methylthio-5-deoxy-D-ribose 1-phosphate5-Methylthio-5-deoxy-D-ribulose 1-phosphate
show the reaction diagram		Bacillus subtilisO31662-695004--r
5-Methylthio-5-deoxy-D-ribose 1-phosphate5-Methylthio-5-deoxy-D-ribulose 1-phosphate
show the reaction diagram		Homo sapiens--2661-2661-
5-Methylthio-5-deoxy-D-ribose 1-phosphate5-Methylthio-5-deoxy-D-ribulose 1-phosphate
show the reaction diagram		Rattus norvegicus--2659-2659-
5-Methylthio-5-deoxy-D-ribose 1-phosphate5-Methylthio-5-deoxy-D-ribulose 1-phosphate
show the reaction diagram		Saccharomyces cerevisiae--692309--?
5-Methylthio-5-deoxy-D-ribose 1-phosphate5-Methylthio-5-deoxy-D-ribulose 1-phosphate
show the reaction diagram		Klebsiella pneumoniae--2660-2660-
5-Methylthio-5-deoxy-D-ribose 1-phosphate?
show the reaction diagram		Rattus norvegicus-enzyme in synthesis of methionine from 5'-S-methylthioadenosine2659---
5-Methylthio-5-deoxy-D-ribose 1-phosphate?
show the reaction diagram		Klebsiella pneumoniae-enzyme in synthesis of methionine from 5'-S-methylthioadenosine2660---
5-Methylthio-5-deoxy-D-ribose 1-phosphate?
show the reaction diagram		Homo sapiens-enzyme of the pathway of the conversion of methylthioribose-1-phosphate to methionine2661---
S-methyl-5-thio-alpha-D-ribose 1-phosphateS-methyl-5-thio-D-ribulose 1-phosphate
show the reaction diagram		Homo sapiens--705716--?

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
5-Methylthio-5-deoxy-D-ribose 1-phosphate?
show the reaction diagram		Rattus norvegicus-enzyme in synthesis of methionine from 5'-S-methylthioadenosine2659--
5-Methylthio-5-deoxy-D-ribose 1-phosphate?
show the reaction diagram		Klebsiella pneumoniae-enzyme in synthesis of methionine from 5'-S-methylthioadenosine2660--
5-Methylthio-5-deoxy-D-ribose 1-phosphate?
show the reaction diagram		Homo sapiens-enzyme of the pathway of the conversion of methylthioribose-1-phosphate to methionine2661--
S-methyl-5-thio-alpha-D-ribose 1-phosphateS-methyl-5-thio-D-ribulose 1-phosphate
show the reaction diagram		Homo sapiens--705716--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
additional informationBacillus subtilisO31662M1Pi does not require any metals to exhibit catalytic activity695004

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
RNAiHomo sapiens-stable knockdown of MRDI is carried out in A-375 cells705716-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
RhoAHomo sapiens-MRDI is induced by RhoA and mediates RhoA-dependent cell invasion705716 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.3-Klebsiella pneumoniae--2660

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
A-375 cellHomo sapiens--705716Manually annotated by BRENDA team
colonic carcinoma cellHomo sapiens-clone A has 5-methylthioribose-1-phosphate isomerase activity, clone D lacks this enzyme2661Manually annotated by BRENDA team
FOM71 cellHomo sapiens--705716Manually annotated by BRENDA team
FOM78 cellHomo sapiens--705716Manually annotated by BRENDA team
liverRattus norvegicus--2659Manually annotated by BRENDA team
melanocyte cell lineHomo sapiens--705716Manually annotated by BRENDA team
melanoma cell lineHomo sapiens--705716Manually annotated by BRENDA team
NHEM2493 cellHomo sapiens--705716Manually annotated by BRENDA team
NHEM693 cellHomo sapiens--705716Manually annotated by BRENDA team
WM-35 cellHomo sapiens--705716Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
cytoplasmHomo sapiens--5737705716Manually annotated by BRENDA team
cytosolSaccharomyces cerevisiae--5829692309Manually annotated by BRENDA team
nucleusHomo sapiens--5634705716Manually annotated by BRENDA team
plasma membraneHomo sapiens--5886705716Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
2yrf, downloadSCOP (2yrf)CATH (2yrf)Bacillus subtilis (strain 168)
2yvk, downloadSCOP (2yvk)CATH (2yvk)Bacillus subtilis (strain 168)
1w2w, downloadSCOP (1w2w)CATH (1w2w)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
1t9k, downloadSCOP (1t9k)CATH (1t9k)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerSaccharomyces cerevisiae--662258
dimerBacillus subtilisO31662x-ray crystallography695004

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. 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°CBacillus subtilisO31662695004
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 ABacillus subtilis-660630
sitting-drop vapour-diffusion methodSaccharomyces cerevisiae-662258

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bacillus subtilisO31662695004
by nickel-nitrilotriacetic acid affinity chromatography, the His-tag is removed by treatment with tobacco etch virus proteaseHomo sapiens-705716
-Klebsiella pneumoniae-2660
-Saccharomyces cerevisiae-662258

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expressed in Escherichia coliBacillus subtilisO31662695004
into pCMV plasmid for expression in mammalian cells and into pMS356 plasmid for esxpression in Escherichia coliHomo sapiens-705716

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
RhoA induces expression of MRDIHomo sapiens-705716

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
C168SHomo sapiens-inactive mutant705716
D248AHomo sapiens-inactive mutant705716

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Breast NeoplasmsProteomic analysis of infiltrating ductal carcinoma tissues by coupled 2-D DIGE/MS/MS analysis. PubMed
NeoplasmsCrystal structure of yeast Ypr118w, a methylthioribose-1-phosphate isomerase related to regulatory eIF2B subunits. PubMed
NeoplasmsProteomic analysis of infiltrating ductal carcinoma tissues by coupled 2-D DIGE/MS/MS analysis. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
2659Trackman, P.C.; Abeles, R.H.Methionine synthesis from 5'-S-methylthioaenosine. Resolution of enzyme activities and identification of 1-phospho-5-S-methylthioribuloseJ. Biol. Chem.2586717-67201983Rattus norvegicus PubMed
2660Furfine, E.S.; Abeles, R.H.Intermediates in the conversion of 5'-S-methylthioadenosine to methionine in Klebsiella pneumoniaeJ. Biol. Chem.2639598-96061988Klebsiella pneumoniae PubMed
2661Ghoda, L.Y.; Savarese, T.M.; Dexter, D.L.; Parks, R.E.; Trackman, P.C.; Abeles, R.H.Characterization of a defect in the pathway for converting 5'-deoxy-5'-methylthioadenosine to methionine in a subline of a cultured heterogeneous human colon carcinomaJ. Biol. Chem.2596715-67191984Homo sapiens PubMed
660630Tamura, H.; Matsumura, H.; Inoue, T.; Ashida, H.; Saito, Y.; Yokota, A.; Kai, Y.Crystallization and preliminary X-ray analysis of methylthioribose-1-phosphate isomerase from Bacillus subtilisActa Crystallogr. Sect. FF61595-5982005Bacillus subtilis PubMed
662258Bumann, M.; Djafarzadeh, S.; Oberholzer, A.E.; Bigler, P.; Altmann, M.; Trachsel, H.; Baumann, U.Crystal structure of yeast Ypr118w, a methylthioribose-1-phosphate isomerase related to regulatory eIF2B subunitsJ. Biol. Chem.27937087-370942004Saccharomyces cerevisiae PubMed
692309Pirkov, I.; Norbeck, J.; Gustafsson, L.; Albers, E.A complete inventory of all enzymes in the eukaryotic methionine salvage pathwayFEBS J.2754111-41202008Saccharomyces cerevisiae PubMed
695004Tamura, H.; Saito, Y.; Ashida, H.; Inoue, T.; Kai, Y.; Yokota, A.; Matsumura, H.Crystal structure of 5-methylthioribose 1-phosphate isomerase product complex from Bacillus subtilis: implications for catalytic mechanismProtein Sci.17126-1352008Bacillus subtilis PubMed
705716Kabuyama, Y.; Litman, E.S.; Templeton, P.D.; Metzner, S.I.; Witze, E.S.; Argast, G.M.; Langer, S.J.; Polvinen, K.; Shellman, Y.; Chan, D.; Shabb, J.B.; Fitzpatrick, J.E.; Resing, K.A.; Sousa, M.C.; Ahn, N.G.A mediator of Rho-dependent invasion moonlights as a methionine salvage enzymeMol. Cell. Proteomics82308-23202009Homo sapiens PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 5.3.1.23)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)