Information on EC 5.3.1.6 - Ribose-5-phosphate isomerase:

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


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EC NUMBERCOMMENTARY
5.3.1.6-

RECOMMENDED NAMEGeneOntology No.
Ribose-5-phosphate isomeraseGO:0004751

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
D-Ribose 5-phosphate = D-ribulose 5-phosphate
show the reaction diagram
----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
intramolecular oxidoreduction----
isomerization----

PATHWAYKEGG LinkMetaCyc Link
Bifidobacterium shunt-P124-PWY
Biosynthesis of secondary metabolites01110 -
Calvin-Benson-Bassham cycle-CALVIN-PWY
Carbon fixation in photosynthetic organisms00710 -
formaldehyde assimilation II (RuMP Cycle)-PWY-1861
formaldehyde assimilation III (dihydroxyacetone cycle)-P185-PWY
Fructose and mannose metabolism00051 -
Metabolic pathways01100 -
Microbial metabolism in diverse environments01120 -
Pentose phosphate pathway00030 -
pentose phosphate pathway (non-oxidative branch)-NONOXIPENT-PWY
Rubisco shunt-PWY-5723

SYSTEMATIC NAMEIUBMB Comments
D-ribose-5-phosphate aldose-ketose-isomeraseAlso acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5-phosphate ketol-isomeraseSaccharomyces cerevisiae--660967
5-Phosphoribose isomerase----
CTRPIClostridium thermocellumD1NPG0-701498
CTRpiBClostridium thermocellumA3DIL8-713894
CTRpiBClostridium thermocellum ATCC 27405A3DIL8--
D-Ribose 5-phosphate isomerase----
D-Ribose 5-phosphate isomeraseEscherichia coli, Mycobacterium tuberculosis--703070
D-ribose-5-phosphate isomeraseClostridium thermocellum--693296
D-ribose-5-phosphate isomeraseClostridium thermocellumD1NPG0-693296, 701498
D-ribose-5-phosphate isomerase AEscherichia coli--693661
D-ribose-5-phosphate isomerase BMycobacterium tuberculosisQ79FD7-693661
D-ribose-5-phosphate ketol-isomerase----
D-xylose ketol-isomerase----
EcRpiBEscherichia coli--703070
Isomerase, ribose phosphate----
MJ1603Methanocaldococcus jannaschiiQ58998-701503
MtRpiBMycobacterium tuberculosis--703070
Phosphopentoisomerase----
Phosphopentose isomerase----
Phosphoriboisomerase----
PhosphoriboisomeraseSynechococcus elongatus PCC 7942--661234
ribose 5-phosphate isomerase AVibrio vulnificusQ7MHL9-705731
Ribose phosphate isomerase----
Ribose-5-P isomerase----
ribose-5-phosphate isomeraseClostridium thermocellumA3DIL8-713894
ribose-5-phosphate isomeraseClostridium thermocellum ATCC 27405A3DIL8--
ribose-5-phosphate isomeraseStreptococcus pneumoniae--717008
ribose-5-phosphate isomeraseTrypanosoma cruziA1BTJ7-714990
ribose-5-phosphate isomeraseTrypanosoma cruzi BrennerA1BTJ7--
ribose-5-phosphate isomerase BClostridium thermocellumA3DIL8-713908
ribose-5-phosphate isomerase BClostridium thermocellum ATCC 27405A3DIL8--
ribose-5-phosphate isomerase BMycobacterium tuberculosis--662445
Ribosephosphate isomerase A----
Ribosephosphate isomerase B----
RPI----
RPIArabidopsis thalianaQ9ZU38-706109
RPIClostridium thermocellumA3DIL8-713908
RPIClostridium thermocellum ATCC 27405A3DIL8--
RPISpinacia oleracea--649425, 663426
RPIThermus thermophilus--652484
RPI2 proteinArabidopsis thalianaQ9ZU38-706109
RpiAEscherichia coli--653838, 693661
RpiAMethanocaldococcus jannaschiiQ58998-701503
RpiAVibrio vulnificusQ7MHL9-705731
RpiBClostridium thermocellum--693296
RpiBClostridium thermocellumD1NPG0-693296, 701498
RpiBEscherichia coli--703070
RpiBMycobacterium tuberculosis--662445, 663427, 703070
RpiBMycobacterium tuberculosisQ79FD7-693661
RpiBSpinacia oleracea--663427
RpiBStreptococcus pneumoniae--717008
RpiBTrypanosoma cruziA1BTJ7-714990
RpiBTrypanosoma cruzi BrennerA1BTJ7--
type B ribose 5-phosphate isomeraseEscherichia coli, Mycobacterium tuberculosis--703070
type B ribose 5-phosphate isomeraseTrypanosoma cruziA1BTJ7-714990
type B ribose 5-phosphate isomeraseTrypanosoma cruzi BrennerA1BTJ7--
type B ribose-5-phosphate isomeraseMycobacterium tuberculosis, Spinacia oleracea--663427
type B RpiEscherichia coli, Mycobacterium tuberculosis--703070

CAS REGISTRY NUMBERCOMMENTARY
9023-83-0-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis thalianagene RPI2, At2g01290706109Q9ZU38UniProtManually annotated by BRENDA team
Bacillus caldolyticus-2783, 2787--Manually annotated by BRENDA team
Bos taurus-2778, 2780--Manually annotated by BRENDA team
Bos tauruscalf; ox2775--Manually annotated by BRENDA team
Chromatium sp.strain D2787--Manually annotated by BRENDA team
Chromatium sp. Dstrain D2787--Manually annotated by BRENDA team
Clostridium thermocellum-678884, 693296--Manually annotated by BRENDA team
Clostridium thermocellum-713894, 713908A3DIL8UniProtManually annotated by BRENDA team
Clostridium thermocellumRpiB; gene rpiB693296, 701498D1NPG0UniProtManually annotated by BRENDA team
Clostridium thermocellum ATCC 27405-713894, 713908A3DIL8UniProtManually annotated by BRENDA team
Cyberlindnera jadinii-2776, 2781, 2782, 2784, 2785, 2790--Manually annotated by BRENDA team
Cyberlindnera jadiniiphysical interaction between phosphoribulokinase and phosphoriboisomerase in the presence of substrate2789--Manually annotated by BRENDA team
Echinococcus granulosus-2624--Manually annotated by BRENDA team
Enterobacter aerogenes-2624--Manually annotated by BRENDA team
Escherichia coli-2787, 693661--Manually annotated by BRENDA team
Escherichia coli-653911P0A7Z0UniprotManually annotated by BRENDA team
Escherichia coligene rpiB703070--Manually annotated by BRENDA team
Escherichia colistrain K12, two enzyme forms: constitutive isomerase A and inducible isomerase B2779--Manually annotated by BRENDA team
Escherichia colitwo ribose 5-phosphate isomerases, RpiA and RpiB. RpiA is constitutively expressed, accounts for about 99% of the total ribose 5-phosphate isomerase activity for strains grown in nutrient broth. Escherichia coli strains defective in rpiA gene are still able to use ribose as a carbon source due to the presence of the second RPI, a ribose-inducible RpiB653838--Manually annotated by BRENDA team
Escherichia coli K12strain K12, two enzyme forms: constitutive isomerase A and inducible isomerase B2779--Manually annotated by BRENDA team
Halothiobacillus neapolitanus-2787--Manually annotated by BRENDA team
Homo sapiens-2624--Manually annotated by BRENDA team
Macrotyloma uniflorum-2795--Manually annotated by BRENDA team
Methanocaldococcus jannaschiistrain DSM 2661701503Q58998UniProtManually annotated by BRENDA team
Mycobacterium tuberculosis-652933, 663427--Manually annotated by BRENDA team
Mycobacterium tuberculosis-662445, 693661Q79FD7SwissProtManually annotated by BRENDA team
Mycobacterium tuberculosisgene rpiB703070Q79FD7SwissProtManually annotated by BRENDA team
Pediococcus pentosaceus-2624--Manually annotated by BRENDA team
Pisum sativum-2792, 676674--Manually annotated by BRENDA team
Pisum sativumphosphoribulokinase and phosphoriboisomerase are associated to a complex2788--Manually annotated by BRENDA team
Plasmodium falciparum-677394--Manually annotated by BRENDA team
Pyrococcus horikoshii-653906O50083UniprotManually annotated by BRENDA team
Rattus norvegicus-2777--Manually annotated by BRENDA team
Rhodospirillum rubrum-2624, 2787--Manually annotated by BRENDA team
Saccharomyces cerevisiae-2624, 2793, 660967, 661287--Manually annotated by BRENDA team
Spinacia oleracea-2624, 2786, 2794, 649425, 663425, 663426, 663427--Manually annotated by BRENDA team
Spinacia oleraceathree electrophoretic forms2777--Manually annotated by BRENDA team
Streptococcus pneumoniae-717008--Manually annotated by BRENDA team
Sus scrofa-2797--Manually annotated by BRENDA team
Synechococcus elongatus PCC 7942-661234--Manually annotated by BRENDA team
Thermus thermophilusHB8652484--Manually annotated by BRENDA team
Thiobacillus thioparus-2783, 2787--Manually annotated by BRENDA team
Trypanosoma brucei-2791--Manually annotated by BRENDA team
Trypanosoma cruzi-714990A1BTJ7SwissProtManually annotated by BRENDA team
Trypanosoma cruzitype B enzyme678047A1BTJ7SwissProtManually annotated by BRENDA team
Trypanosoma cruzi Brenner-714990A1BTJ7SwissProtManually annotated by BRENDA team
Vibrio vulnificusstrain YJ016, gene rpiA705731Q7MHL9UniProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
malfunctionArabidopsis thalianaQ9ZU38deficiency in a cytosolic ribose-5-phosphate isomerase causes chloroplast dysfunction, late flowering and premature cell death in Arabidopsis thaliana706109
metabolismClostridium thermocellum-Rpi is involved in D-allose metabolism by converting D-ribose-5-phosphate to D-ribulose-5-phosphate and vice versa in a branch of the pentose phosphate pathway701498
metabolismMethanocaldococcus jannaschiiQ58998two evolutionary distinct forms of the enzyme, RpiA and RpiB, with different amino acid sequences and molecular weights exist, that both catalyze the reversible conversion of ribose 5-phosphate to ribulose 5-phosphate. RpiA is found in the bacterial, plant and animal kingdoms, whereas RpiB is less widespread and is found in bacterial sources701503
metabolismEscherichia coli, Mycobacterium tuberculosis-ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway703070
metabolismMycobacterium tuberculosisQ79FD7ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway703070
metabolismArabidopsis thalianaQ9ZU38the cytosolic ribose-5-phosphate isomerase catalyzes the reversible interconversion of ribulose-5-phosphate and ribose-5-phosphate in the non-oxidative phase of the oxidative pentose phosphate pathway, which is part of central metabolism706109

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-AlloseD-Psicose
show the reaction diagram
Streptococcus pneumoniae--717008--r
D-AlloseD-Psicose
show the reaction diagram
Clostridium thermocellumD1NPG0-693296--r
D-AlloseD-Psicose
show the reaction diagram
Clostridium thermocellum--701498--r
D-AlloseD-Psicose
show the reaction diagram
Clostridium thermocellum--713908--?
D-AlloseD-Psicose
show the reaction diagram
Clostridium thermocellum-substrates D-allose and D-psicose are preferred over ribose 5-phosphate678884--r
D-AlloseD-Psicose
show the reaction diagram
Clostridium thermocellum ATCC 27405--713908--?
D-allose 6-phosphateD-allulose 6-phosphate
show the reaction diagram
Escherichia coli, Mycobacterium tuberculosis--703070--r
D-allose 6-phosphateD-allulose 6-phosphate
show the reaction diagram
Mycobacterium tuberculosisQ79FD7-703070--r
D-Glucose 6-phosphate?
show the reaction diagram
Streptococcus pneumoniae--717008--?
D-guloseD-sorbose
show the reaction diagram
Streptococcus pneumoniae--717008--r
D-psicoseD-allose
show the reaction diagram
Streptococcus pneumoniae--717008--r
D-psicoseD-allose
show the reaction diagram
Clostridium thermocellum-substrates D-allose and D-psicose are preferred over ribose 5-phosphate678884--r
D-psicoseD-allose
show the reaction diagram
Clostridium thermocellum, Clostridium thermocellum ATCC 27405A3DIL8the conversion yield of D-psicose to D-allose is 32% for the R132E mutant enzyme and 25% for the wild type enzyme after 80 min713894--r
D-RiboseD-Ribulose
show the reaction diagram
Streptococcus pneumoniae--717008--r
D-RiboseD-Ribulose
show the reaction diagram
Clostridium thermocellum--701498--r
D-RiboseD-Ribulose
show the reaction diagram
Clostridium thermocellum--713908--?
D-RiboseD-Ribulose
show the reaction diagram
Clostridium thermocellumD1NPG0-69329638% conversion to D-ribose 5-phosphate yield after approximately 90 min-r
D-RiboseD-Ribulose
show the reaction diagram
Clostridium thermocellumD1NPG039% conversion yield after approximately 90 min693296--r
D-RiboseD-Ribulose
show the reaction diagram
Clostridium thermocellum ATCC 27405--713908--?
D-ribose 5-diphosphateD-ribulose 5-diphosphate
show the reaction diagram
Escherichia coliP0A7Z0-653911-653911?
D-ribose 5-diphosphateD-ribulose 5-diphosphate
show the reaction diagram
Trypanosoma cruziA1BTJ7-678047--r
D-ribose 5-diphosphateD-ribulose 5-diphosphate
show the reaction diagram
Clostridium thermocellum-substrates D-allose and D-psicose are preferred over ribose 5-phosphate678884--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Cyberlindnera jadinii--2776-2776-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Cyberlindnera jadinii--2781-2781-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Cyberlindnera jadinii--2782-2782-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Cyberlindnera jadinii--2784-2784-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Cyberlindnera jadinii--2785-2785-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Cyberlindnera jadinii--2789-2789-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Cyberlindnera jadinii--2790-2790-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coli--2779-2779-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coli--2787-2787-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coli--693661--?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coliP0A7Z0-653911-653911r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coli--703070--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Homo sapiens--2624-2624-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Rattus norvegicus--2777-2777-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Sus scrofa--2797-2797-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Saccharomyces cerevisiae--2624-2624-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Bos taurus--2775-2775-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Bos taurus--2778-2778-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Bos taurus--2780-2780-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Spinacia oleracea--2624-2624-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Spinacia oleracea--2777-2777-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Spinacia oleracea--2786-2786-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Spinacia oleracea--2794-2794-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Spinacia oleracea--649425-649425?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Pisum sativum--2788-2788-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Pisum sativum--2792-2792-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Enterobacter aerogenes--2624-2624-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Trypanosoma brucei--2791-2791-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Mycobacterium tuberculosis--652933-652933?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Mycobacterium tuberculosisQ79FD7-662445--?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Mycobacterium tuberculosisQ79FD7-703070--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Pediococcus pentosaceus--2624-2624-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Thiobacillus thioparus--2783-2783-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Thiobacillus thioparus--2787-2787-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Bacillus caldolyticus--2783-2783-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Bacillus caldolyticus--2787-2787-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Rhodospirillum rubrum--2624-2624-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Rhodospirillum rubrum, Chromatium sp., Halothiobacillus neapolitanus--2787-2787-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Macrotyloma uniflorum--2795-2795-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Echinococcus granulosus--2624-2624-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Pyrococcus horikoshiiO50083-653906-653906r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Clostridium thermocellumD1NPG0-693296--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Mycobacterium tuberculosis--693661--?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Methanocaldococcus jannaschiiQ58998-701503--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Vibrio vulnificusQ7MHL9-705731--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Clostridium thermocellum--713908--?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Saccharomyces cerevisiae-diastereotopic specificity2793-2793-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Clostridium thermocellumD1NPG0preferred substrate693296--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Clostridium thermocellum-preferred substrate701498--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Clostridium thermocellumD1NPG0preferred substrate69329638% conversion to D-ribose 5-phosphate yield after approximately 90 min at 50C-r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Pyrococcus horikoshiiO50083direct or indirect catalytic role for the residues E107, D85 and K98653906-653906r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Streptococcus pneumoniae-highest specific activity717008--?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coli-enzyme is involved in the first step of the non-oxidative branch of the pentose phosphate pathway. Two ribose 5-phosphate isomerase, RpiA and RpiB. RpiA is constitutively expressed, accounts for about 99% of the total ribose 5-phosphate isomerase activity for strains grown in nutrient broth. Escherichia coli strains defective in rpiA gene are still able to use ribose as a carbon source due to the presence of the second RPI, a ribose-inducible RpiB653838-653838r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Thermus thermophilus-key enzyme in the oxidative and reductive pentose-phosphate pathway for the conversion of ribose-5-phosphate to ribulose-5-phosphatre and vice versa652484-652484r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coliP0A7Z0the enzyme plays essential roles in carbohydrate anabolism and catabolism653911-653911r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Saccharomyces cerevisiae-ribose 5-phosphate ketol-isomerase, the translation product of the RKI1 gene plays a crucial role in pyridoxine synthesis in yeast660967--?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Vibrio vulnificusQ7MHL9binding mode of substrate, overview705731--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Methanocaldococcus jannaschiiQ58998the open configuration of ribose 5-phosphate is required for isomerization and is reversibly converted to ribulose 5-phosphate701503--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Chromatium sp. D--2787-2787-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coli K12--2779-2779-
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Clostridium thermocellum ATCC 27405--713908--?
D-ribose 5-triphosphateD-ribulose 5-triphosphate
show the reaction diagram
Escherichia coliP0A7Z0-653911-653911?
D-ribose-5-phosphateD-ribulose-5-phosphate
show the reaction diagram
Arabidopsis thalianaQ9ZU38the cytosolic ribose-5-phosphate isomerase catalyzes the reversible interconversion of ribulose-5-phosphate and ribose-5-phosphate in the non-oxidative phase of the oxidative pentose phosphate pathway706109---
D-ribuloseD-ribose
show the reaction diagram
Streptococcus pneumoniae--717008--r
D-ribulose 5-diphosphateD-ribose 5-diphosphate
show the reaction diagram
Trypanosoma cruziA1BTJ7-678047--r
D-ribulose 5-phosphateD-ribose 5-phosphate
show the reaction diagram
Trypanosoma cruziA1BTJ7-714990--?
D-ribulose 5-phosphateD-ribose 5-phosphate
show the reaction diagram
Clostridium thermocellumA3DIL8-713894--r
D-ribulose 5-phosphateD-ribose 5-phosphate
show the reaction diagram
Trypanosoma cruzi BrennerA1BTJ7-714990--?
D-ribulose 5-phosphateD-ribose 5-phosphate
show the reaction diagram
Clostridium thermocellum ATCC 27405A3DIL8-713894--r
D-sorboseD-gulose
show the reaction diagram
Streptococcus pneumoniae-lowest activity with L-sorbose717008--r
D-taloseD-tagatose
show the reaction diagram
Clostridium thermocellumD1NPG0-693296--r
D-taloseD-tagatose
show the reaction diagram
Clostridium thermocellum--701498--r
D-taloseD-tagatose
show the reaction diagram
Clostridium thermocellum, Clostridium thermocellum ATCC 27405--713908--?
L-alloseL-psicose
show the reaction diagram
Clostridium thermocellumD1NPG0-693296--r
L-alloseL-psicose
show the reaction diagram
Clostridium thermocellum--701498--r
L-fructoseL-mannose
show the reaction diagram
Streptococcus pneumoniae--717008--r
L-LyxoseL-Xylulose
show the reaction diagram
Streptococcus pneumoniae-particularly high activity with L-lyxose717008--r
L-MannoseL-Fructose
show the reaction diagram
Streptococcus pneumoniae--717008--r
L-riboseL-ribulose
show the reaction diagram
Clostridium thermocellumD1NPG0-693296--r
L-riboseL-ribulose
show the reaction diagram
Clostridium thermocellum--701498--r
L-tagatoseL-talose
show the reaction diagram
Streptococcus pneumoniae-particularly high activity with L-tagatose717008--r
L-taloseL-tagatose
show the reaction diagram
Clostridium thermocellum-preferred substrate701498--r
L-taloseL-tagatose
show the reaction diagram
Clostridium thermocellumD1NPG089% conversion yield after approximately 90 min693296--r
L-taloseL-tagatose
show the reaction diagram
Clostridium thermocellumD1NPG0the enzyme prefers the forward reaction, high activity, 89% conversion to L-tagatose yield after approximately 90 min at 50C693296--r
L-taloseL-tagatose
show the reaction diagram
Streptococcus pneumoniae-particularly high activity with L-talose717008--r
L-xyluloseL-lyxose
show the reaction diagram
Streptococcus pneumoniae-particularly high activity with L-lyxose717008--r
additional information?-Escherichia coli-the constitutive ribosephosphate isomerase A catalyzes the formation of ribose 5-phosphate from ribulose 5-phosphate and also participates in the reverse reaction during ribose and adenosine catabolism. The normal physiological role of the inducible ribosephosphate isomerase B is still uncertain2779---
additional information?-Cyberlindnera jadinii-ribose 5-phosphate isomerase and ribulose-5-phosphate kinase produce and utilize, respectively, a form of ribulose 5-phosphate which is not the predominant form in the aqueous solution. The effect of this specificity will be channelling of ribulose 5-phosphate from the isomerase to the kinase during photosynthesis2790---
additional information?-Cyberlindnera jadinii-physical interaction between phosphoribulokinase and ribose-5-phosphate isomerase in the presence of substrate can facilitate direct transfer of ribulose 5-phosphate between the two enzymes2789---
additional information?-Spinacia oleracea-the enzyme catalyzes the interconversion of D-ribose-5-phosphate and D-ribulose-5-phosphate in the reductive and oxidative pentose phosphate pathways and thus plays an important role in the primary metabolism of both photosynthetic and non-photosynthetic organisms2794---
additional information?-Clostridium thermocellum-no substrate: D-xylose, L-rhamnose, D-altrose, D-galactose678884---
additional information?-Mycobacterium tuberculosis-no activity with D-allose 6-phosphate693661---
additional information?-Clostridium thermocellum-CTRPI has a narrow substrate specificity for rare sugars and reversibly converts aldose substrates containing hydroxyl groups oriented in the same direction to one of the corresponding ketoses. CTRPI prefers aldose substrates such as L-talose, D-ribose and D-allose701498---
additional information?-Escherichia coli, Mycobacterium tuberculosis-enzyme substrate synthesis, overview703070---
additional information?-Mycobacterium tuberculosisQ79FD7enzyme substrate synthesis, overview703070---
additional information?-Clostridium thermocellumD1NPG0RpiB also displays activity with L-talose, D-ribose, D-allose, L-allose, L-ribose, and D-talose in decreasing order. The enzyme shows specificity for aldose substrates possessing hydroxyl groups oriented in the same direction at the C2, C3, and C4 positions. The substrate specificity through substrate interactions with residues Tyr42, His98, and His9, which interact with the hydroxyl groups of C2, C3, and C4, respectively, oriented in the same direction, homology molecular modeling, overview693296---
additional information?-Streptococcus pneumoniae-no activity is observed with D-mannose-6-phosphate717008---
additional information?-Trypanosoma cruzi, Trypanosoma cruzi BrennerA1BTJ7the enzyme cannot isomerizes D-allose 6-phosphate714990---
additional information?-Escherichia coli K12-the constitutive ribosephosphate isomerase A catalyzes the formation of ribose 5-phosphate from ribulose 5-phosphate and also participates in the reverse reaction during ribose and adenosine catabolism. The normal physiological role of the inducible ribosephosphate isomerase B is still uncertain2779---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-AlloseD-Psicose
show the reaction diagram
Clostridium thermocellum--701498--r
D-RiboseD-Ribulose
show the reaction diagram
Clostridium thermocellum--701498--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coli, Mycobacterium tuberculosis--703070--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Mycobacterium tuberculosisQ79FD7-703070--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Pyrococcus horikoshiiO50083-653906-653906r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Methanocaldococcus jannaschiiQ58998-701503--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Vibrio vulnificusQ7MHL9-705731--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Clostridium thermocellumD1NPG0preferred substrate693296--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Clostridium thermocellum-preferred substrate701498--r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Streptococcus pneumoniae-highest specific activity717008--?
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coli-enzyme is involved in the first step of the non-oxidative branch of the pentose phosphate pathway. Two ribose 5-phosphate isomerase, RpiA and RpiB. RpiA is constitutively expressed, accounts for about 99% of the total ribose 5-phosphate isomerase activity for strains grown in nutrient broth. Escherichia coli strains defective in rpiA gene are still able to use ribose as a carbon source due to the presence of the second RPI, a ribose-inducible RpiB653838-653838r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Thermus thermophilus-key enzyme in the oxidative and reductive pentose-phosphate pathway for the conversion of ribose-5-phosphate to ribulose-5-phosphatre and vice versa652484-652484r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Escherichia coliP0A7Z0the enzyme plays essential roles in carbohydrate anabolism and catabolism653911-653911r
D-ribose 5-phosphateD-ribulose 5-phosphate
show the reaction diagram
Saccharomyces cerevisiae-ribose 5-phosphate ketol-isomerase, the translation product of the RKI1 gene plays a crucial role in pyridoxine synthesis in yeast660967--?
D-ribose-5-phosphateD-ribulose-5-phosphate
show the reaction diagram
Arabidopsis thalianaQ9ZU38the cytosolic ribose-5-phosphate isomerase catalyzes the reversible interconversion of ribulose-5-phosphate and ribose-5-phosphate in the non-oxidative phase of the oxidative pentose phosphate pathway706109---
D-taloseD-tagatose
show the reaction diagram
Clostridium thermocellum--701498--r
L-alloseL-psicose
show the reaction diagram
Clostridium thermocellum--701498--r
L-riboseL-ribulose
show the reaction diagram
Clostridium thermocellum--701498--r
L-taloseL-tagatose
show the reaction diagram
Clostridium thermocellum-preferred substrate701498--r
additional information?-Escherichia coli-the constitutive ribosephosphate isomerase A catalyzes the formation of ribose 5-phosphate from ribulose 5-phosphate and also participates in the reverse reaction during ribose and adenosine catabolism. The normal physiological role of the inducible ribosephosphate isomerase B is still uncertain2779---
additional information?-Cyberlindnera jadinii-ribose 5-phosphate isomerase and ribulose-5-phosphate kinase produce and utilize, respectively, a form of ribulose 5-phosphate which is not the predominant form in the aqueous solution. The effect of this specificity will be channelling of ribulose 5-phosphate from the isomerase to the kinase during photosynthesis2790---
additional information?-Cyberlindnera jadinii-physical interaction between phosphoribulokinase and ribose-5-phosphate isomerase in the presence of substrate can facilitate direct transfer of ribulose 5-phosphate between the two enzymes2789---
additional information?-Spinacia oleracea-the enzyme catalyzes the interconversion of D-ribose-5-phosphate and D-ribulose-5-phosphate in the reductive and oxidative pentose phosphate pathways and thus plays an important role in the primary metabolism of both photosynthetic and non-photosynthetic organisms2794---
additional information?-Clostridium thermocellum-CTRPI has a narrow substrate specificity for rare sugars and reversibly converts aldose substrates containing hydroxyl groups oriented in the same direction to one of the corresponding ketoses. CTRPI prefers aldose substrates such as L-talose, D-ribose and D-allose701498---
additional information?-Escherichia coli K12-the constitutive ribosephosphate isomerase A catalyzes the formation of ribose 5-phosphate from ribulose 5-phosphate and also participates in the reverse reaction during ribose and adenosine catabolism. The normal physiological role of the inducible ribosephosphate isomerase B is still uncertain2779---

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Co2+Cyberlindnera jadinii-activates2784
Mg2+Cyberlindnera jadinii-activates2784
additional informationMacrotyloma uniflorum-salinity shock causes decline in activity2795
additional informationTrypanosoma cruziA1BTJ7enzyme is not metal-dependent678047
additional informationClostridium thermocellum-no activation by mono- or divalent cations678884
additional informationStreptococcus pneumoniae-the enzyme is not activated by monovalent or divalent cations717008

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
3'-AMPCyberlindnera jadinii--2782, 2784 2D-image
3'-CMPCyberlindnera jadinii--2782 2D-image
3'-GMPCyberlindnera jadinii--2782 2D-image
3'-UMPCyberlindnera jadinii--2782 2D-image
3-phosphoglyceratePisum sativum--2792 2D-image
4-deoxy-4-phosphonomethyl-D-erythronateSpinacia oleracea-stable and potent competitive inhibitor663425 2D-image
4-phospho-D-erythronamideSpinacia oleracea-competitive663426 2D-image
4-phospho-D-erythronateMycobacterium tuberculosis--662445 2D-image
4-phospho-D-erythronateTrypanosoma cruziA1BTJ7-678047 2D-image
4-phospho-D-erythronhydrazideTrypanosoma cruziA1BTJ7-678047 2D-image
4-phospho-D-erythronohydrazideSpinacia oleracea-competitive663426 2D-image
4-phospho-D-erythronohydroxamic acidTrypanosoma cruziA1BTJ7competitive678047 2D-image
4-phosphoerythronateSpinacia oleracea-strong competitive2786 2D-image
4-phosphono-D-erythronateSpinacia oleracea--663426 2D-image
4-phosphono-D-erythronohydroxamateMycobacterium tuberculosis--662445 2D-image
4-phosphono-D-erythronohydroxamic acidSpinacia oleracea-competitive663426 2D-image
5'-AMPCyberlindnera jadinii-competitive2782 2D-image
5'-AMPCyberlindnera jadinii--2784 2D-image
5'-CMPCyberlindnera jadinii--2782 2D-image
5'-GMPCyberlindnera jadinii--2782 2D-image
5'-UMPCyberlindnera jadinii--2782 2D-image
5-deoxy-5-phospho-D-ribonohydroxamateMycobacterium tuberculosis--693661 2D-image
5-deoxy-5-phospho-D-ribonohydroxamic acidMycobacterium tuberculosis-competitive and selective inhibitor of type B ribose-5-phosphate isomerase from Mycobacterium tuberculosis663427 2D-image
5-deoxy-5-phospho-D-ribonohydroxamic acidSpinacia oleracea-weak663427 2D-image
5-phospho-D-ribonamideEscherichia coli, Mycobacterium tuberculosis--703070 2D-image
5-phospho-D-ribonamideMycobacterium tuberculosisQ79FD7-703070 2D-image
5-phospho-D-ribonateEscherichia coli-competitive inhibitor of a Rpi, displays specific inhibition of Mycobacterium tuberculosis RpiB versus Escherichia coli RpiB, inhibition kinetics, overview703070 2D-image
5-phospho-D-ribonateMycobacterium tuberculosisQ79FD7very strong competitive inhibitor of a Rpi, specific inhibition of Mycobacterium tuberculosis RpiB versus Escherichia coli RpiB, inhibition kinetics, overview703070 2D-image
5-phospho-D-ribonohydroxamic acidTrypanosoma cruziA1BTJ7-678047 2D-image
5-phospho-D-ribonohydroxamic acidEscherichia coli, Mycobacterium tuberculosis--703070 2D-image
5-phospho-D-ribonohydroxamic acidMycobacterium tuberculosisQ79FD7-703070 2D-image
6-phosphogluconateCyberlindnera jadinii-competitive2782 2D-image
6-phosphogluconateBacillus caldolyticus, Thiobacillus thioparus-temperature-dependent inhibition2783 2D-image
6-phosphogluconateBacillus caldolyticus, Escherichia coli, Thiobacillus thioparus--2787 2D-image
6-phosphogluconatePisum sativum-noncompetitive2792 2D-image
Ag+Bacillus caldolyticus, Thiobacillus thioparus-1 mM2783 2D-image
AMPBacillus caldolyticus, Thiobacillus thioparus-temperature-dependent inhibition2783 2D-image
AMPBacillus caldolyticus, Escherichia coli--2787 2D-image
AMPRhodospirillum rubrum-10 mM2787 2D-image
AMPThiobacillus thioparus--2787 2D-image
arabinose 5-phosphateSpinacia oleracea--649425 2D-image
arabinose 5-phosphateEscherichia coliP0A7Z0-653911 2D-image
arabinose 5-phosphateVibrio vulnificusQ7MHL9RpiA binds arabinose 5-phosphate located at the opening of the active site, the sugar ring of the inhibitor interacts with the Asp4, Lys7, Ser30, Asp118, and Lys121 residues, the phosphate group of arabinose 5-phosphate interacts with two water molecules, W51 and W82, binding mode of inhibitor, overview705731 2D-image
citrateRhodospirillum rubrum-10 mM2787 2D-image
Co2+Bacillus caldolyticus, Thiobacillus thioparus-1 mM2783 2D-image
D-5-Phosphoribonic acidSpinacia oleracea--2786 2D-image
D-Allose 6-phosphateMycobacterium tuberculosis--693661 2D-image
D-Allose 6-phosphateTrypanosoma cruziA1BTJ7weak competitive inhibitor714990 2D-image
D-allulose 6-phosphateMycobacterium tuberculosis--693661 2D-image
D-arabinose 5-phosphateSpinacia oleracea-effective649425 2D-image
D-arabinose 5-phosphateThermus thermophilus--652484 2D-image
EDTACyberlindnera jadinii--2782, 2784 2D-image
erythrose 4-phosphatePisum sativum-competitive2792 2D-image
fructose 6-phosphateEscherichia coli--2787 2D-image
glyceraldehyde 3-phosphatePisum sativum-competitive2792 2D-image
Hg2+Cyberlindnera jadinii--2784 2D-image
iodoacetamideCyberlindnera jadinii--2776 2D-image
iodoacetamideBos taurus--2778 2D-image
iodoacetamideTrypanosoma cruziA1BTJ75 mM, complete inhibition678047 2D-image
iodoacetateEscherichia coli-1.25 mM, 100% loss of ribosephosphate isomerase B, no effect on ribosephosphate isomerase A2779 2D-image
iodoacetateMycobacterium tuberculosis--652933 2D-image
Mg2+Bacillus caldolyticus, Thiobacillus thioparus-0.01 M2783 2D-image
Mg2+Pisum sativum-MgCl2, noncompetitive2792 2D-image
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoateEscherichia coli, Mycobacterium tuberculosis--703070 2D-image
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoateMycobacterium tuberculosisQ79FD7-703070 2D-image
N-(5-phospho-D-ribonoyl)-glycineEscherichia coli-poor inhibition with substrate D-ribose 5-phosphate, no inhibition with substrate D-allose 5-phosphate703070 2D-image
N-(5-phospho-D-ribonoyl)-glycineMycobacterium tuberculosisQ79FD7-703070 2D-image
N-(5-phospho-D-ribonoyl)-hydrazineEscherichia coli, Mycobacterium tuberculosis--703070 2D-image
N-(5-phospho-D-ribonoyl)-hydrazineMycobacterium tuberculosisQ79FD7-703070 2D-image
N-(5-phospho-D-ribonoyl)-methylamineEscherichia coli, Mycobacterium tuberculosis--703070 2D-image
N-(5-phospho-D-ribonoyl)-methylamineMycobacterium tuberculosisQ79FD7-703070 2D-image
NAD+Rhodospirillum rubrum-10 mM2787 2D-image
NEMCyberlindnera jadinii--2776 2D-image
NEMBos taurus--2778 2D-image
Organic mercurialsBos taurus--2780-
Organic mercurialsCyberlindnera jadinii--2781-
PCMBCyberlindnera jadinii--2776 2D-image
PCMBBos taurus--2778 2D-image
PhenylmercuriacetateBacillus caldolyticus, Thiobacillus thioparus-reversible by 0.02-10 mM 2-mercaptoethanol, and by 10 mM Cys2783 2D-image
phosphateSpinacia oleracea-competitive649425 2D-image
phosphateMycobacterium tuberculosis-weak652933 2D-image
phosphateEscherichia coliP0A7Z0-653911 2D-image
ribulose diphosphateRhodospirillum rubrum-1.0 mM, strong2787 2D-image
sedoheptulose bisphosphatePisum sativum-competitive2792 2D-image
Sodium mersalylBacillus caldolyticus, Thiobacillus thioparus-reversible by 2-mercaptoethanol, 0.02-10 mM, and by Cys, 10 mM2783 2D-image
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acidCyberlindnera jadinii--2776 2D-image
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acidBos taurus--2778 2D-image
sulfhydryl reagentsBos taurus--2780 2D-image
sulfhydryl reagentsCyberlindnera jadinii--2781 2D-image
Xylulose 5-phosphateSpinacia oleracea--649425 2D-image
Zn2+Bacillus caldolyticus, Thiobacillus thioparus-0.01 M2783 2D-image
Mn2+Cyberlindnera jadinii-slight inhibition of enzyme form I and II, strong inhibition of enzyme form III2784 2D-image
additional informationClostridium thermocellum-EDTA is not inhibitory678884-
additional informationEscherichia coli, Mycobacterium tuberculosis-substrate-derived enzyme inhibitor design and synthesis of analogues of the 6-carbon high-energy intermediate postulated for the D-allose 6-phosphate to D-allulose 6-phosphate isomerization reaction, overview703070-
additional informationMycobacterium tuberculosisQ79FD7substrate-derived enzyme inhibitor design and synthesis of analogues of the 6-carbon high-energy intermediate postulated for the D-allose 6-phosphate to D-allulose 6-phosphate isomerization reaction, overview703070-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2-mercaptoethanolBacillus caldolyticus, Thiobacillus thioparus-stimulates2783, 2787 2D-image
EDTABacillus caldolyticus, Thiobacillus thioparus-stimulates2783, 2787 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
106-D-AlloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
43-D-psicoseClostridium thermocellum-mutant enzyme R132E, pH 7.5, 80C713894 2D-image
46-D-psicoseClostridium thermocellum-mutant enzyme R132D, pH 7.5, 80C713894 2D-image
53-D-psicoseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
53-D-psicoseClostridium thermocellum-mutant enzyme R132K, pH 7.5, 80C; wild type enzyme, pH 7.5, 80C713894 2D-image
54-D-psicoseClostridium thermocellum-mutant enzyme R132Q, pH 7.5, 80C713894 2D-image
56-D-psicoseClostridium thermocellum-mutant enzyme R132A, pH 7.5, 80C713894 2D-image
78-D-psicoseClostridium thermocellum-mutant enzyme R132I, pH 7.5, 80C713894 2D-image
44-D-riboseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
23D-Ribose 5-diphosphateTrypanosoma cruziA1BTJ7muant H11A, pH 8.4, 25C678047 2D-image
2-D-Ribose 5-diphosphateTrypanosoma cruziA1BTJ7mutant H102A, pH 8.4, 25C678047 2D-image
4-D-Ribose 5-diphosphateTrypanosoma cruziA1BTJ7wild-type, pH 8.4, 25C678047 2D-image
10-D-Ribose 5-diphosphateTrypanosoma cruziA1BTJ7mutant H138A, pH 8.4, 25C678047 2D-image
0.017-D-ribose 5-phosphateClostridium thermocellum-pH 7.5, 65C, recombinant enzyme693296 2D-image
0.108-D-ribose 5-phosphateCyberlindnera jadinii--2782 2D-image
0.16-D-ribose 5-phosphateCyberlindnera jadinii-enzyme form III2784 2D-image
0.17-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, mutant enzyme D85N653906 2D-image
0.43-D-ribose 5-phosphateRhodospirillum rubrum--2624 2D-image
0.67-D-ribose 5-phosphateCyberlindnera jadinii-enzyme form II2784 2D-image
0.74-D-ribose 5-phosphateSaccharomyces cerevisiae--2624 2D-image
0.77-D-ribose 5-phosphateCyberlindnera jadinii-enzyme form I2784 2D-image
0.83-D-ribose 5-phosphateEscherichia coli-ribosephosphate isomerase B2779 2D-image
0.88-D-ribose 5-phosphatePisum sativum--2792 2D-image
1-D-ribose 5-phosphateMycobacterium tuberculosis-in 50 mM Tris-HCl, pH 7.5, at 37C693661 2D-image
1.17-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, wild-type enzyme653906 2D-image
1.63-D-ribose 5-phosphateThermus thermophilus--652484 2D-image
1.8-D-ribose 5-phosphateEnterobacter aerogenes--2624 2D-image
1.8-D-ribose 5-phosphateMycobacterium tuberculosis--662445 2D-image
2-D-ribose 5-phosphateBos taurus--2780 2D-image
2.2-D-ribose 5-phosphateHomo sapiens--2624 2D-image
2.39-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, mutant enzyme D168N653906 2D-image
2.5-D-ribose 5-phosphateCyberlindnera jadinii--2776, 2781 2D-image
2.6-D-ribose 5-phosphateBos taurus-calf spleen2775 2D-image
2.7-D-ribose 5-phosphateEchinococcus granulosus--2624 2D-image
2.8-D-ribose 5-phosphatePediococcus pentosaceus--2624 2D-image
3.1-D-ribose 5-phosphateEscherichia coliP0A7Z0-653911 2D-image
3.3-D-ribose 5-phosphateSpinacia oleracea--2786 2D-image
3.7-D-ribose 5-phosphateMycobacterium tuberculosis--652933 2D-image
4.4-D-ribose 5-phosphateEscherichia coli-ribosephosphate isomerase A2779 2D-image
4.6-D-ribose 5-phosphateSpinacia oleracea--2624 2D-image
5.1-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, mutant enzyme K125A653906 2D-image
6.5-D-ribose 5-phosphateBos taurus-ox muscle2775 2D-image
7.13-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, mutant enzyme R100A653906 2D-image
9.110.2D-ribose 5-phosphateBos taurus-calf liver2775 2D-image
17-D-ribose 5-phosphateClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
0.52-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme D90A649425 2D-image
0.56-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme D87A649425 2D-image
0.63-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, wild-type enzyme649425 2D-image
1.17-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme E91A649425 2D-image
4.41-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme K100A649425 2D-image
34-D-ribuloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
1.4-D-ribulose 5-diphosphateTrypanosoma cruziA1BTJ7wild-type, pH 8.4, 25C678047 2D-image
2.5-D-ribulose 5-diphosphateTrypanosoma cruziA1BTJ7mutant H102A, pH 8.4, 25C678047 2D-image
0.015-D-ribulose 5-phosphateClostridium thermocellum-pH 7.5, 65C, recombinant enzyme693296 2D-image
0.66-D-ribulose 5-phosphatePisum sativum--2792 2D-image
5-D-ribulose 5-phosphateTrypanosoma cruziA1BTJ7in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30C714990 2D-image
15-D-ribulose 5-phosphateClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
232-D-taloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
98-L-alloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
173-L-riboseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
319-L-ribuloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
125-L-tagatoseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
37-L-taloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
additional information-additional informationPyrococcus horikoshiiO50083dramatic increase of Km-value at temperatures above 80C653906-
additional information-additional informationClostridium thermocellum-kinetics with aldose and ketose substrates, recombinant enzyme, overview693296-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2682-D-AlloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
1962-D-psicoseClostridium thermocellum-mutant enzyme R132K, pH 7.5, 80C713894 2D-image
2211-D-psicoseClostridium thermocellum-mutant enzyme R132I, pH 7.5, 80C713894 2D-image
2335-D-psicoseClostridium thermocellum-mutant enzyme R132Q, pH 7.5, 80C713894 2D-image
2347-D-psicoseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
2347-D-psicoseClostridium thermocellum-wild type enzyme, pH 7.5, 80C713894 2D-image
2580-D-psicoseClostridium thermocellum-mutant enzyme R132A, pH 7.5, 80C713894 2D-image
2674-D-psicoseClostridium thermocellum-mutant enzyme R132D, pH 7.5, 80C713894 2D-image
2743-D-psicoseClostridium thermocellum-mutant enzyme R132E, pH 7.5, 80C713894 2D-image
11880-D-riboseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
1-D-Ribose 5-diphosphateTrypanosoma cruziA1BTJ7mutant H102A, pH 8.4, 25C678047 2D-image
10-D-Ribose 5-diphosphateTrypanosoma cruziA1BTJ7mutant H138A, pH 8.4, 25C678047 2D-image
12-D-Ribose 5-diphosphateTrypanosoma cruziA1BTJ7wild-type, pH 8.4, 25C678047 2D-image
97-D-Ribose 5-diphosphateTrypanosoma cruziA1BTJ7muant H11A, pH 8.4, 25C678047 2D-image
8.3-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, mutant enzyme D85N653906 2D-image
47-D-ribose 5-phosphateMycobacterium tuberculosis-in 50 mM Tris-HCl, pH 7.5, at 37C693661 2D-image
120-D-ribose 5-phosphateMycobacterium tuberculosis--652933 2D-image
151-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, mutant enzyme K125A653906 2D-image
177-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, mutant enzyme R100A653906 2D-image
312-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, mutant enzyme D168N653906 2D-image
320-D-ribose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, wild-type enzyme653906 2D-image
625-D-ribose 5-phosphatePyrococcus horikoshiiO5008393C, pH 6, wild-type enzyme653906 2D-image
1070-D-ribose 5-phosphateThermus thermophilus-50C, pH 7.5652484 2D-image
1072-D-ribose 5-phosphateThermus thermophilus-50C, pH 7.5652484 2D-image
2100-D-ribose 5-phosphateEscherichia coliP0A7Z0-653911 2D-image
52000-D-ribose 5-phosphateClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C; pH 7.5, 65C, recombinant enzyme693296 2D-image
0.0421-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme D87A649425 2D-image
2.54D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme K100A649425 2D-image
2.54-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme K100A649425 2D-image
13.2-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme D90A649425 2D-image
946-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, mutant enzyme E91A649425 2D-image
3440-D-ribose-5-phosphateSpinacia oleracea-pH 8.0, 25C, wild-type enzyme649425 2D-image
9193-D-ribuloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
4.7-D-ribulose 5-diphosphateTrypanosoma cruziA1BTJ7wild-type, pH 8.4, 25C678047 2D-image
10.7-D-ribulose 5-diphosphateTrypanosoma cruziA1BTJ7mutant H102A, pH 8.4, 25C678047 2D-image
28D-ribulose 5-phosphateTrypanosoma cruziA1BTJ7in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30C714990 2D-image
50-D-ribulose 5-phosphatePyrococcus horikoshiiO5008350C, pH 6.0, wild-type enzyme653906 2D-image
39530-D-ribulose 5-phosphateClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C; pH 7.5, 65C, recombinant enzyme693296 2D-image
119-D-taloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
1506-L-alloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
322-L-riboseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
17-L-ribuloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
1822-L-tagatoseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image
13420-L-taloseClostridium thermocellum-in 50 mM Tris-HCl buffer (pH 7.5), at 65C693296 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
28-D-psicoseClostridium thermocellum-mutant enzyme R132I, pH 7.5, 80C7138949337
37-D-psicoseClostridium thermocellum-mutant enzyme R132K, pH 7.5, 80C7138949337
43-D-psicoseClostridium thermocellum-mutant enzyme R132Q, pH 7.5, 80C7138949337
44-D-psicoseClostridium thermocellum-wild type enzyme, pH 7.5, 80C7138949337
46-D-psicoseClostridium thermocellum-mutant enzyme R132A, pH 7.5, 80C7138949337
58-D-psicoseClostridium thermocellum-mutant enzyme R132D, pH 7.5, 80C7138949337
64-D-psicoseClostridium thermocellum-mutant enzyme R132E, pH 7.5, 80C7138949337
3029-D-ribose 5-phosphateClostridium thermocellum-pH 7.5, 65C, recombinant enzyme6932969351
2589-D-ribulose 5-phosphateClostridium thermocellum-pH 7.5, 65C, recombinant enzyme6932969356

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.074-4-deoxy-4-phosphonomethyl-D-erythronateSpinacia oleracea-25C663425 2D-image
2.5-4-phospho-D-erythronamideSpinacia oleracea-25C, pH 7.5663426 2D-image
1.7-4-phospho-D-erythronateMycobacterium tuberculosis--662445 2D-image
1.8-4-phospho-D-erythronohydrazideSpinacia oleracea-25C, pH 7.5663426 2D-image
1.2-4-phospho-D-erythronohydroxamic acidTrypanosoma cruziA1BTJ7pH 8.4, 25C678047 2D-image
0.028-4-phosphono-D-erythronateSpinacia oleracea-25C, pH 7.5663426 2D-image
0.057-4-phosphono-D-erythronohydroxamateMycobacterium tuberculosis--662445 2D-image
0.029-4-phosphono-D-erythronohydroxamic acidSpinacia oleracea-25C, pH 7.5663426 2D-image
0.4-5-deoxy-5-phospho-D-ribonohydroxamic acidMycobacterium tuberculosis--663427 2D-image
6.2-5-deoxy-5-phospho-D-ribonohydroxamic acidSpinacia oleracea--663427 2D-image
0.04-5-phospho-D-ribonamideMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.07-5-phospho-D-ribonamideEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.009-5-phospho-D-ribonateMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.09-5-phospho-D-ribonohydroxamic acidEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.26-5-phospho-D-ribonohydroxamic acidMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.43-5-phospho-D-ribonohydroxamic acidEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate703070 2D-image
0.7-arabinose 5-phosphateSpinacia oleracea-pH 8.0, 25C649425 2D-image
15-D-Allose 6-phosphateTrypanosoma cruziA1BTJ7in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30C714990 2D-image
0.89-D-arabinose 5-phosphateThermus thermophilus-50C, pH 7.5652484 2D-image
0.34-N-(5-phospho-D-ribonoyl)-glycineMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
1.9-N-(5-phospho-D-ribonoyl)-hydrazineEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate703070 2D-image
0.11-N-(5-phospho-D-ribonoyl)-methylamineMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.18-N-(5-phospho-D-ribonoyl)-methylamineEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
7.9-phosphateSpinacia oleracea-pH 8.0, 25C649425 2D-image
8-phosphateEscherichia coliP0A7Z0-653911 2D-image
130-phosphateMycobacterium tuberculosis--652933 2D-image
4-Xylulose 5-phosphateSpinacia oleracea-pH 8.0, 25C649425 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
5-4-phospho-D-erythronateTrypanosoma cruziA1BTJ7pH 8.4, 25C678047 2D-image
0.7-4-phospho-D-erythronohydroxamic acidTrypanosoma cruziA1BTJ7pH 8.4, 25C678047 2D-image
0.2-5-phospho-D-ribonamideEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.22-5-phospho-D-ribonamideMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
1.33-5-phospho-D-ribonamideEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate703070 2D-image
0.031-5-phospho-D-ribonateMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
1.31-5-phospho-D-ribonateEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.17-5-phospho-D-ribonohydroxamic acidEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.44-5-phospho-D-ribonohydroxamic acidMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.62-5-phospho-D-ribonohydroxamic acidEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate703070 2D-image
2-D-Allose 6-phosphateMycobacterium tuberculosis-in 50 mM Tris-HCl, pH 7.5, at 37C693661 2D-image
1.42-N-(5-phospho-D-ribonoyl)-gamma-aminobutanoateMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
1.6-N-(5-phospho-D-ribonoyl)-gamma-aminobutanoateEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate703070 2D-image
2-N-(5-phospho-D-ribonoyl)-gamma-aminobutanoateEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.57-N-(5-phospho-D-ribonoyl)-glycineMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
9-N-(5-phospho-D-ribonoyl)-glycineEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
1-N-(5-phospho-D-ribonoyl)-hydrazineMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.19-N-(5-phospho-D-ribonoyl)-methylamineMycobacterium tuberculosisQ79FD7pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
0.35-N-(5-phospho-D-ribonoyl)-methylamineEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate703070 2D-image
0.36-N-(5-phospho-D-ribonoyl)-methylamineEscherichia coli-pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate703070 2D-image
6.3-D-allulose 6-phosphateMycobacterium tuberculosis-in 50 mM Tris-HCl, pH 7.5, at 37C693661 2D-image
additional information-additional informationTrypanosoma cruziA1BTJ7IC50 values of 5-phospho-D-ribonohydroxamic acid and 4-phospho-D-erythronhydrazide are above 10 mM678047-

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.0005-Streptococcus pneumoniae-using D-sorbose as substrate, at 35C and pH 7.5717008
0.0011-Streptococcus pneumoniae-using L-fructose as substrate, at 35C and pH 7.5717008
0.0013-Streptococcus pneumoniae-using L-tagatose as substrate, at 35C and pH 7.5717008
0.0019-Streptococcus pneumoniae-using D-allose as substrate, at 35C and pH 7.5717008
0.0021-Streptococcus pneumoniae-using D-psicose as substrate, at 35C and pH 7.5717008
0.0025-Streptococcus pneumoniae-using D-ribose as substrate, at 35C and pH 7.5717008
0.0053-Streptococcus pneumoniae-using D-gulose as substrate, at 35C and pH 7.5717008
0.0096-Streptococcus pneumoniae-using L-lyxose as substrate, at 35C and pH 7.5717008
0.019-Streptococcus pneumoniae-using L-talose as substrate, at 35C and pH 7.5717008
0.027-Streptococcus pneumoniae-using L-lyxose as substrate, at 35C and pH 7.5717008
0.048-Streptococcus pneumoniae-using D-ribulose as substrate, at 35C and pH 7.5717008
0.058-Streptococcus pneumoniae-using D-glucose 6-phosphate as substrate, at 35C and pH 7.5717008
0.121-Streptococcus pneumoniae-using L-xylulose as substrate, at 35C and pH 7.5717008
0.21-Clostridium thermocellum-purified enzyme, using D-tagatose as substrate, at 65C and pH 7.5693296
0.259-Clostridium thermocellum-mutant enzyme H98A, using D-psicose as substrate, pH 7.5, 80C713894
0.299-Clostridium thermocellum-mutant enzyme H133A, using D-psicose as substrate, pH 7.5, 80C; mutant enzyme R136A, using D-psicose as substrate, pH 7.5, 80C713894
0.388-Streptococcus pneumoniae-using D-ribose 5-phosphate as substrate, at 35C and pH 7.5717008
0.53-Clostridium thermocellum-purified enzyme, using L-allose as substrate, at 65C and pH 7.5693296
0.698-Clostridium thermocellum-mutant enzyme N99A, using D-psicose as substrate, pH 7.5, 80C713894
0.917-Clostridium thermocellum-mutant enzyme T67A, using D-psicose as substrate, pH 7.5, 80C713894
1.256-Clostridium thermocellum-mutant enzyme H9A, using D-psicose as substrate, pH 7.5, 80C713894
1.815-Clostridium thermocellum-mutant enzyme T135A, using D-psicose as substrate, pH 7.5, 80C713894
1.994-Clostridium thermocellum-wild type enzyme, using D-psicose as substrate, pH 7.5, 80C713894
2.313-Clostridium thermocellum-mutant enzyme R132A, using D-psicose as substrate, pH 7.5, 80C713894
12-Clostridium thermocellum-purified enzyme, using L-psicose as substrate, at 65C and pH 7.5693296
50-Clostridium thermocellum-purified enzyme, using D-talose as substrate, at 65C and pH 7.5693296
52.7-Bacillus caldolyticus--2783, 2787
272-Clostridium thermocellum-purified enzyme, using L-ribose as substrate, at 65C and pH 7.5693296
356-Cyberlindnera jadinii--2776
544-Thiobacillus thioparus--2783, 2787
600-Clostridium thermocellum-purified enzyme, using L-allose as substrate, at 65C and pH 7.5693296
720-Clostridium thermocellum-purified enzyme, using L-ribulose as substrate, at 65C and pH 7.5693296
1037-Clostridium thermocellum-purified enzyme, using D-psicose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-psicose693296
1352-Clostridium thermocellum-purified enzyme, using D-allose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-allose693296
1700-Pisum sativum--2792
5374-Clostridium thermocellum-purified enzyme, using D-ribulose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribulose693296
5800-Clostridium thermocellum-purified enzyme, using D-ribose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribose693296
7363-Clostridium thermocellum-purified enzyme, using L-talose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate L-talose693296
19680-Clostridium thermocellum-purified enzyme, using D-ribulose 5-phosphate as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribulose 5-phosphate693296
25690-Clostridium thermocellum-purified enzyme, using D-ribose 5-phosphate as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribose 5-phosphate693296
additional information-Bos taurus--2778, 2780
additional information-Cyberlindnera jadinii--2781, 2784

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
6-Pyrococcus horikoshiiO50083at 50C653906
6.59Bacillus caldolyticus, Thiobacillus thioparus--2783
79Bos taurus--2778
7.4-Arabidopsis thalianaQ9ZU38assay at706109
7.5-Cyberlindnera jadinii--2782
7.5-Clostridium thermocellum-optimum for synthesis of D-allose678884
7.5-Clostridium thermocellum-assay at693296
7.5-Escherichia coli, Mycobacterium tuberculosis-assay at703070
7.5-Mycobacterium tuberculosisQ79FD7assay at703070
7.5-Clostridium thermocellum--713894
7.5-Streptococcus pneumoniae--717008
7.77.8Pisum sativum-D-ribulose 5-phosphate, D-ribose 5-phosphate2792
810Trypanosoma cruziA1BTJ7broad678047
8.4-Cyberlindnera jadinii--2776, 2781

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
69Clostridium thermocellum--713894
69.9Cyberlindnera jadinii-pH 6: about 40% of maximal activity, pH 9.9: about 65% of maximal activity2776
6.58.5Streptococcus pneumoniae--717008

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
35-Streptococcus pneumoniae--717008
37-Escherichia coli, Mycobacterium tuberculosis-assay at703070
37-Mycobacterium tuberculosisQ79FD7assay at703070
37-Arabidopsis thalianaQ9ZU38assay at706109
50-Cyberlindnera jadinii--2776, 2782
65-Bos taurus--2778
65-Clostridium thermocellum-optimum for synthesis of D-allose678884
65-Clostridium thermocellum-assay at693296
80-Clostridium thermocellum--713894
85-Sus scrofa--2797
95-Pyrococcus horikoshiiO50083-653906

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
2045Streptococcus pneumoniae--717008
3080Bos taurus-30C: about 50% of maximal activity, 80C: about 45% of maximal activity2778
6090Clostridium thermocellum--713894

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
4.77-Vibrio vulnificusQ7MHL9isoelectric focusing705731
5.1-Spinacia oleracea-isoelectric focusing649425

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
amastigoteTrypanosoma cruziA1BTJ7-678047Manually annotated by BRENDA team
bloodRattus norvegicus-one electrophorectic form2777Manually annotated by BRENDA team
bloodstream formTrypanosoma brucei--2791Manually annotated by BRENDA team
brainRattus norvegicus-two electrophorectic forms2777Manually annotated by BRENDA team
epimastigoteTrypanosoma cruziA1BTJ7highest expression678047Manually annotated by BRENDA team
erythrocyteHomo sapiens--2624Manually annotated by BRENDA team
heartRattus norvegicus-two electrophorectic forms2777Manually annotated by BRENDA team
kidneyRattus norvegicus-one electrophorectic form2777Manually annotated by BRENDA team
leafMacrotyloma uniflorum--2795Manually annotated by BRENDA team
leafSpinacia oleracea--649425Manually annotated by BRENDA team
leafPisum sativum--676674Manually annotated by BRENDA team
liverBos taurus--2775Manually annotated by BRENDA team
liverRattus norvegicus-one electrophorectic form2777Manually annotated by BRENDA team
lungRattus norvegicus-one electrophorectic form2777Manually annotated by BRENDA team
muscleBos taurus--2775Manually annotated by BRENDA team
muscleRattus norvegicus-two electrophorectic forms2777Manually annotated by BRENDA team
muscleBos taurus-skeletal2778, 2780Manually annotated by BRENDA team
procyclic formTrypanosoma brucei--2791Manually annotated by BRENDA team
shootPisum sativum--2788Manually annotated by BRENDA team
small intestineRattus norvegicus-two electrophorectic forms2777Manually annotated by BRENDA team
spleenBos taurus--2775Manually annotated by BRENDA team
spleenRattus norvegicus-two electrophoretic forms2777Manually annotated by BRENDA team
spleenSus scrofa--2797Manually annotated by BRENDA team
trypomastigoteTrypanosoma cruziA1BTJ7metacyclic and in cell-culture678047Manually annotated by BRENDA team
uterusRattus norvegicus-two electrophorectic forms2777Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastPisum sativum--95072788, 2792Manually annotated by BRENDA team
chloroplastSpinacia oleracea--95072794Manually annotated by BRENDA team
chloroplastPisum sativum-co-localization of enzyme with phosphoribulokinase and Rubisco9507676674Manually annotated by BRENDA team
cytosolArabidopsis thalianaQ9ZU38-5829706109Manually annotated by BRENDA team
mitochondrial membraneCyberlindnera jadinii--319662776Manually annotated by BRENDA team
mitochondrial membraneRattus norvegicus--319662777Manually annotated by BRENDA team
thylakoid membraneSynechococcus elongatus PCC 7942--42651661234Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
4em8, downloadSCOP (4em8)CATH (4em8)Anaplasma phagocytophilum (strain HZ)
3hhe, downloadSCOP (3hhe)CATH (3hhe)Bartonella henselae (strain ATCC 49882 / Houston 1)
3u7j, downloadSCOP (3u7j)CATH (3u7j)Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
3uw1, downloadSCOP (3uw1)CATH (3uw1)Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
3he8, downloadSCOP (3he8)CATH (3he8)Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
3hee, downloadSCOP (3hee)CATH (3hee)Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
3ph3, downloadSCOP (3ph3)CATH (3ph3)Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
3ph4, downloadSCOP (3ph4)CATH (3ph4)Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
1ks2, downloadSCOP (1ks2)CATH (1ks2)Escherichia coli (strain K12)
1lkz, downloadSCOP (1lkz)CATH (1lkz)Escherichia coli (strain K12)
1nn4, downloadSCOP (1nn4)CATH (1nn4)Escherichia coli (strain K12)
1o8b, downloadSCOP (1o8b)CATH (1o8b)Escherichia coli (strain K12)
2vvr, downloadSCOP (2vvr)CATH (2vvr)Escherichia coli (strain K12)
3kwm, downloadSCOP (3kwm)CATH (3kwm)Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
4io1, downloadSCOP (4io1)CATH (4io1)Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
4m8l, downloadSCOP (4m8l)CATH (4m8l)Francisella tularensis subsp. tularensis (strain WY96-3418)
3s5p, downloadSCOP (3s5p)CATH (3s5p)Giardia intestinalis (strain ATCC 50803 / WB clone C6)
1m0s, downloadSCOP (1m0s)CATH (1m0s)Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
4gmk, downloadSCOP (4gmk)CATH (4gmk)Lactobacillus salivarius (strain UCC118)
3ixq, downloadSCOP (3ixq)CATH (3ixq)Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
2f8m, downloadSCOP (2f8m)CATH (2f8m)Plasmodium falciparum (isolate 3D7)
1lk5, downloadSCOP (1lk5)CATH (1lk5)Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
1lk7, downloadSCOP (1lk7)CATH (1lk7)Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
1xtz, downloadSCOP (1xtz)CATH (1xtz)Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
3l7o, downloadSCOP (3l7o)CATH (3l7o)Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
1o1x, downloadSCOP (1o1x)CATH (1o1x)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
1uj4, downloadSCOP (1uj4)CATH (1uj4)Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
1uj5, downloadSCOP (1uj5)CATH (1uj5)Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
1uj6, downloadSCOP (1uj6)CATH (1uj6)Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
4nml, downloadSCOP (4nml)CATH (4nml)Toxoplasma gondii ME49
3k7o, downloadSCOP (3k7o)CATH (3k7o)Trypanosoma cruzi (strain CL Brener)
3k7p, downloadSCOP (3k7p)CATH (3k7p)Trypanosoma cruzi (strain CL Brener)
3k7s, downloadSCOP (3k7s)CATH (3k7s)Trypanosoma cruzi (strain CL Brener)
3k8c, downloadSCOP (3k8c)CATH (3k8c)Trypanosoma cruzi (strain CL Brener)
3m1p, downloadSCOP (3m1p)CATH (3m1p)Trypanosoma cruzi (strain CL Brener)
3enq, downloadSCOP (3enq)CATH (3enq)Vibrio vulnificus (strain YJ016)
3env, downloadSCOP (3env)CATH (3env)Vibrio vulnificus (strain YJ016)
3enw, downloadSCOP (3enw)CATH (3enw)Vibrio vulnificus (strain YJ016)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
3000035000Mycobacterium tuberculosis-gel filtration652933
3200034000Escherichia coli-ribosephosphate isomerase B, gel filtration2779
32000-Mycobacterium tuberculosis-dynamic light scattering652933
34000-Mycobacterium tuberculosis-non-denaturing PAGE652933
34000-Clostridium thermocellum-gel filtration693296
35000-Clostridium thermocellum-about, native PAGE, recombinant enzyme701498
39600-Trypanosoma cruziA1BTJ7gel filtration678047
40000-Bacillus caldolyticus, Thiobacillus thioparus-gel filtration2783
40000-Bacillus caldolyticus, Thiobacillus thioparus-gel filtration2787
45000-Escherichia coli-ribosephosphate isomerase A, gel filtration2779
45000-Vibrio vulnificusQ7MHL9recombinant detagged RpiA, dynamic light scattering and gel filtration705731
49000-Spinacia oleracea-gel filtration649425
50000-Escherichia coli-dynamic light scattering653838
53000-Spinacia oleracea-high-speed equilibrium centrifugation2624
54000-Chromatium sp.--2787
57000-Rhodospirillum rubrum-gel filtration2624
57000-Rhodospirillum rubrum--2787
96000-Streptococcus pneumoniae-gel filtration717008
98000-Pyrococcus horikoshiiO50083gel filtration653906
105000-Cyberlindnera jadinii-gel filtration2776
183000-Cyberlindnera jadinii-gel filtration2782
228000-Bos taurus-analytical ultracentrifugation2778

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Pisum sativum-x * 26400, SDS-PAGE2792
?Spinacia oleracea-x * 25300, SDS-PAGE2794
dimerSpinacia oleracea-2 * 26000, SDS-PAGE2624
dimerSpinacia oleracea-2 * 25000, SDS-PAGE; 2 * 25066, calculation from nucleotide sequence649425
dimerMycobacterium tuberculosis-2 * 17300, calculation from nucleotide sequence652933
dimerEscherichia coliP0A7Z0the two subunits in the dimer have different conformations, the result of motion of two largely rigid domains with respect to each other in the subunit653911
dimerTrypanosoma cruziA1BTJ72 * 17400, calculated, 2 * 18000, SDS-PAGE678047
dimerClostridium thermocellum-2 x 17500, about, recombinant enzyme, RpiB has an active-site interface between the dimer structures701498
dimerVibrio vulnificusQ7MHL92 * 20000-25000, RpiA705731
homodimerClostridium thermocellum-2 * 17000, gel filtration693296
homodimerClostridium thermocellum-2 * 17000, X-ray crystallography713908
homodimerClostridium thermocellum ATCC 27405-2 * 17000, X-ray crystallography-
tetramerCyberlindnera jadinii-4 * 26000, SDS-PAGE2776
tetramerBos taurus-4 * 58000, SDS-PAGE2778
tetramerPyrococcus horikoshiiO500834 * 25163, calculation from nucleotide sequence; 4 * 26000, in crystal and in solution, each monomer has a new fold consisting of two alpha/beta domains, SDS-PAGE653906
tetramerMethanocaldococcus jannaschiiQ58998RpiA crystal structure, overview701503
tetramerTrypanosoma cruziA1BTJ7x-ray crystallography714990
tetramerTrypanosoma cruzi Brenner-x-ray crystallography-
trimerCyberlindnera jadinii-1 * 75000, alpha, + 2 * 54000, beta, SDS-PAGE2782
homotetramerStreptococcus pneumoniae-4 * 23724, calculated from amino acid sequence; 4 * 24000, SDS-PAGE717008
additional informationClostridium thermocellum-homology modeling of RpiB, substrate binding structure, overview693296

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

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
in complex with ribose 5-phosphate, ribose or allose, sitting drop vapor diffusion method, using 0.05 M Tris pH 7.0, 10% (w/v) PEG 8000, 0.15 M magnesium chloride, and 0.2 M potassium chlorideClostridium thermocellum-713908
purified recombinant RpiB, sitting drop vapour diffusion method, 0.001 ml of 7 mg/ml protein in mM Tris-HCl buffer pH 7.5 is mixed with 0.001 ml of reservoir solution, containing 0.05 M Tris, pH 7.0, 10% PEG 8000, 0.15 M MgCl2 and 0.2 M KCl, and equilibrated against 1 ml of reservoir solution, 3 weeks, flash-cooling in liquid nitrogen with a cryoprotectant solution containing 65 mM Tris pH 7.0, 13% PEG 8000, 195 mM MgCl2, 260 mM KCl and 20% glycerol, X-ray diffraction structure determination and analysis at 1.9 A resolution, modelingClostridium thermocellum-701498
hanging drop vapor diffusion method, enzyme form RpiAEscherichia coli-653838
hanging drop vapor diffusion method, structure of a complex with arabinose 5-phosphate at 1.25 A resolutionEscherichia coliP0A7Z0653911
purified recombinant MJ1603, microbatch-under-oil method, 0.0005 ml of 8.1 mg/ml protein in 20 mM Tris-HCl buffer, pH 8.0, containing 200 mM NaCl are mixed with 0.0005 ml of crystallization reagent, consisting of 0.1 M acetate, pH 4.5 containing 40% v/v 1,2-propanediol and 0.05 M calcium acetate, 18C. The mixture is covered with 0.015 ml silicone and paraffin oil, X-ray diffraction structure determination and analysis at 1.78 A resolution, molecular replacement and modelingMethanocaldococcus jannaschiiQ58998701503
hanging drop vapour diffusion method, X-ray structure of ribose-5-phosphate isomerase B in complex with the inhibitors 4-phosphono-D-erythronohydroxamate and 4-phospho-D-erythronate refined to resolutions of 2.1 and 2.2 AMycobacterium tuberculosis-662445
in complex with 5-deoxy-5-phospho-D-ribonohydroxamate, hanging drop vapour diffusion method, with 15% PEG 8000, 0.1 M MES buffer, pH 6, 5% PEG 1000, and 0.2 M Li2SO4, or in complex with D-ribose 5-phosphate, sitting drop vapour diffusion method, with 20% PEG 3K, 0.1 M Tris, pH 7, and 0.2 M Ca acetateMycobacterium tuberculosis-693661
sitting drop vapour diffusion methodMycobacterium tuberculosis-652933
molecular replacement at 2.9 A resolutionPlasmodium falciparum-677394
hanging drop vapor diffusion method, crystal structure of the free enzyme and the complex with D-4-phosphoerythronic acidPyrococcus horikoshiiO50083653906
2.1 A resolution crystal structure. Crystals are cryo-protected by transfering through crystallization solution with progressively higher ethylene glycol concentration up to 30% v/v and then flash cooled in liquid nitrogen. The protein crystallizes in space group F432 with cell dimensions a = b = c = 209A, corresponding to one molecule per asymmetric unit and a solvent content of 47%Saccharomyces cerevisiae-661287
crystal structure of enzyme complexed with the open chain form of the ribose 5-phosphate and the open chain form of the C2 epimeric inhibitor arabinose 5-phosphate as well as the apo form at high resolutionThermus thermophilus-652484
RpiB (wild type or C69A mutant enzyme), sitting drop vapor diffusion method, using 0.5% (v/v) Jeffamine ED-2001, 0.1 M HEPES, 1.1 M Na-malonate (pH 7.0) for the wild type enzyme in complex with phosphate, or 0.8 M Na?K phosphate (pH 8.2) for the mutant enzyme C69A in complex with phosphate, or 20% (w/v) poly(ethyleneglycol) 550 monomethyl ether, 0.1 M NaCl, 0.1 M bicine (pH 9.0) for the wild type enzyme in complex with D-ribose 5-phosphate, or 20% (w/v) poly(ethylene glycol) 6000, 0.2 M ammonium chloride, 0.1 M Tris-HCl (pH 8.0) for wild type enzyme in complex with 4-phospho-D-erythronohydroxamic acid, or 20% (w/v) poly(ethylene glycol) 3350, 0.2 M sodium acetate, 0.1 M bis-Tris propane (pH 8.5) for mutant enzyme C69A in complex with allose 6-phosphateTrypanosoma cruziA1BTJ7714990
open form RpiA in complex with substrate ribose 5-phosphate, the closed form complexed with arabinose-5-phosphate, and the apo-RpiA, hanging drop vapor diffusion method, 0.002 ml of 30 mg/ml protein in 20 mM HEPES, pH 7.5, and 150 mM KCl are mixed with 0.002 ml of a reservoir solution containing 50 mM succinate, pH 4.1, 180 mM ammonium sulfate, and 8% PEG 4000, 3 days, 20C, for complexed enzyme addition of 20 mM ligand, X-ray diffraction structure determination and analysis at 1.49-2.07 A resolution, molecular replacementVibrio vulnificusQ7MHL9705731

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
510Bacillus caldolyticus-65C, stable for at least 30 min2783
510Thiobacillus thioparus-45C, stable for at least 30 min2783

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
3550Streptococcus pneumoniae-enzyme activity is stable for 48 h at 35C, and shows half-lives of 15 h at 40C, and 6 h at 50C717008
45-Escherichia coli-30 min, ribosephosphate isomerase A retains 90% of its activity, ribosephosphate isomerase B retains 60% of its activity2779
45-Thiobacillus thioparus-pH 5-10, stable for at least 30 min2783
50-Clostridium thermocellum-half-life 96 h678884
57-Thiobacillus thioparus-1 h, 50% loss of activity2783
6075Clostridium thermocellum-the half-lives of the wild type enzyme at 60C, 65C, 70C, 75C, and 80C are 11, 7.0, 4.2, 1.5, and 0.6 h, respectively713894
60-Escherichia coli-ribosephosphate isomerase A: complex dependence on protein concentration, at 1.0 mg/ml protein and greater, all activity is lost. At 0.05-0.75 mg/ml protein, 20-30% of the original activity is left after 30 min; ribosephosphate isomerase B: half-life 2.2 min, independent of enzyme and protein concentration2779
65-Bacillus caldolyticus-pH 5-10, stable for at least 30 min2783
65-Clostridium thermocellum-half-life 4.7 h678884
91-Bacillus caldolyticus-1 h, 50% loss of activity2783
100-Pyrococcus horikoshiiO50083stability and integrity up to, needs at least 250 mM NaCl to maintain its hyperthermostability653906

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
(NH4)2SO4, NaCl, KCl and LiCl increase thermal stability. LiBr, CaCl2, methanol, ethanol, and 1-propanol decrease thermal stability. Alcohols decrease the stability in the following order: methanol, ethanol, propanolBacillus caldolyticus-2783
ethylene glycol increases stabilityBacillus caldolyticus-2783
freezing and thawing destroys activityCyberlindnera jadinii-2776, 2781
(NH4)2SO4, NaCl, KCl and LiCl increase thermal stability. LiBr, CaCl2, methanol, ethanol, and 1-propanol decrease thermal stability. Alcohols decrease the stability in the following order: methanol, ethanol, propanolThiobacillus thioparus-2783
ethylene glycol has little effect on the mesophilic enzymeThiobacillus thioparus-2783
freeze-labileThiobacillus thioparus-2787

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
4C, stable for 2 weeksBacillus caldolyticus-2787
-20C, stable for several monthsBos taurus-2778
-20C, stable for several weeksBos taurus-2780
2C, stable for several monthsCyberlindnera jadinii-2776
4C, stable for several monthsCyberlindnera jadinii-2781
-20C, 2 months, stablePisum sativum-2792
4C, stable for 6-8 weeksThiobacillus thioparus-2787

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bacillus caldolyticus-2783, 2787
-Bos taurus-2780
ox muscle, calf spleen and liver, partialBos taurus-2775
HisTrap HP column chromatographyClostridium thermocellumA3DIL8713894, 713908
HisTrap HP column chromatography; recombinant RpiB from Escherichia coli strain ER2566 by His affinity chromatographyClostridium thermocellum-693296
recombinant RpiB from Escherichia coli strain ER2566 by His affinity chromatographyClostridium thermocellum-701498
-Cyberlindnera jadinii-2776, 2782
3 forms: I, I, IIICyberlindnera jadinii-2784
affinity chromatographic methodCyberlindnera jadinii-2785
recombinant MJ1603 from Escherichia coli strain Rosetta (DE3) by anion exchange and hydroxyapatite chromatography, and gel filtrationMethanocaldococcus jannaschiiQ58998701503
-Mycobacterium tuberculosis-652933
gel filtrationMycobacterium tuberculosis-693661
-Pisum sativum-2792
-Pyrococcus horikoshiiO50083653906
-Saccharomyces cerevisiae-661287
-Spinacia oleracea-2794
recombinant enzymeSpinacia oleracea-649425
HiTrap Q anion exchange column chromatography and Sephacryl S-300 gel filtrationStreptococcus pneumoniae-717008
-Thiobacillus thioparus-2783
Superdex 75 gel filtrationTrypanosoma cruziA1BTJ7714990
recombinant His-tagged RpiA from Escherichia coli strain BL21(DE3) by nickel affinity chromatography. The His-tag is cleaved off and removed, folowed by anion exchange chromatography and gel filtrationVibrio vulnificusQ7MHL9705731

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
gene RPI2, phylogenetic analysisArabidopsis thalianaQ9ZU38706109
expressed in Escherichia coli ER2566 cellsClostridium thermocellumA3DIL8713894, 713908
expressed in Escherichia coli ER2566 cells; gene rpiB, expression in Escherichia coli strain ER2566Clostridium thermocellum-693296
expression in Escherichia coliClostridium thermocellum-678884
gene rpiB, expression in Escherichia coli strain ER2566Clostridium thermocellum-701498
overexpression as a His-tagged Se-Met-labeled proteinEscherichia coliP0A7Z0653911
expression of MJ1603 in Escherichia coli strain Rosetta (DE3)Methanocaldococcus jannaschiiQ58998701503
expressed in Escherichia coli Top10 cellsMycobacterium tuberculosis-693661
overexpression in Escherichia coliMycobacterium tuberculosis-652933
-Plasmodium falciparum-677394
overexpression in Escherichia coliPyrococcus horikoshiiO50083653906
-Saccharomyces cerevisiae-661287
-Spinacia oleracea-2794
overexpression in Escherichia coliSpinacia oleracea-649425
expressed in Escherichia coli ER2566 cellsStreptococcus pneumoniae-717008
-Trypanosoma cruziA1BTJ7678047
expressed in Escherichia coli ER2566 cellsTrypanosoma cruziA1BTJ7714990
gene rpiA, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)Vibrio vulnificusQ7MHL9705731

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
C65AClostridium thermocellum-the mutant shows no activity for D-psicose713894
D8AClostridium thermocellum-the mutant shows no activity for D-psicose713894
H133AClostridium thermocellum-the mutant shows 15% activity compared to the wild type enzyme713894
H98AClostridium thermocellum-the mutant shows 13% activity compared to the wild type enzyme713894
H9AClostridium thermocellum-the mutant shows 63% activity compared to the wild type enzyme713894
N99AClostridium thermocellum-the mutant shows 35% activity compared to the wild type enzyme713894
R132AClostridium thermocellum-the mutant exhibits an increase in D-psicose isomerization activity (116% activity compared to the wild type enzyme)713894
R132DClostridium thermocellum-the mutant shows increased catalytic efficiency toward D-psicose compared to the wild type enzyme713894
R132EClostridium thermocellum-the mutant shows increased catalytic efficiency toward D-psicose compared to the wild type enzyme; the specific activity and catalytic efficiency (kcat/Km) of the R132E mutant for D-psicose are 1.4 and 1.5fold higher than those of the wild type enzyme, respectively713894
R132IClostridium thermocellum-the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme713894
R132KClostridium thermocellum-the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme713894
R132QClostridium thermocellum-the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme713894
R136AClostridium thermocellum-the mutant shows 15% activity compared to the wild type enzyme713894
T135AClostridium thermocellum-the mutant shows 91% activity compared to the wild type enzyme713894
T67AClostridium thermocellum-the mutant shows 46% activity compared to the wild type enzyme713894
Y42AClostridium thermocellum-the mutant shows no activity for D-psicose713894
C65AClostridium thermocellum ATCC 27405-the mutant shows no activity for D-psicose-
H9AClostridium thermocellum ATCC 27405-the mutant shows 63% activity compared to the wild type enzyme-
N99AClostridium thermocellum ATCC 27405-the mutant shows 35% activity compared to the wild type enzyme-
R136AClostridium thermocellum ATCC 27405-the mutant shows 15% activity compared to the wild type enzyme-
T135AClostridium thermocellum ATCC 27405-the mutant shows 91% activity compared to the wild type enzyme-
R189KSaccharomyces cerevisiae-6% of the wild-type activity. Loss of the structural integrity of the protein seems to be responsible for the greatly diminished activity660967
D87ASpinacia oleracea-turnover number with D-ribose-5-phosphate is 0.0012% of value for the the wild-type enzyme, moderate change in Km-value649425
D90ASpinacia oleracea-turnover number with D-ribose-5-phosphate is 0.38% of value for the the wild-type enzyme, moderate change in Km-value649425
E91ASpinacia oleracea-turnover number with D-ribose-5-phosphate is 27.5% of value for the the wild-type enzyme, moderate change in Km-value649425
K100ASpinacia oleracea-turnover number with D-ribose-5-phosphate is 0.074% of value for the the wild-type enzyme, moderate change in Km-value649425
C69ATrypanosoma cruziA1BTJ7no catalytic activity678047
C69ATrypanosoma cruziA1BTJ7inactive714990
H102ATrypanosoma cruziA1BTJ7kinetics severeyl impaired with substrate ribose 5-phosphate, but not affected with substrate ribulose 5-phosphate678047
H11ATrypanosoma cruziA1BTJ76fold increase in Km value, 8fold increase in kcat value, decrease in stability to freezing and thawing678047
H138ATrypanosoma cruziA1BTJ7little variations in kinetics compared to wild-type678047
C69ATrypanosoma cruzi Brenner-inactive-
additional informationArabidopsis thalianaQ9ZU38construction of T-DNA knockout mutants of the RPI2 gene, which encodes the cytosolic ribose-5-phosphate isomerase. Knockout of the RPI2 gene does not significantly change the total RPI activity in the mutant plants, but knockout of RPI2 interferes with chloroplast structure and decreases chloroplast photosynthetic capacity. Rpi2 mutants accumulate less starch in the leaves and flower significantly later than wild-type when grown under short-day conditions, and rpi2 mutants display premature cell death in the leaves when grown at an above-normal temperature of 26C, phenotypes, detailed overview706109

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

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisClostridium thermocellum-production of D-allose from D-psicose by enzyme. At pH 7.5 and 50C, synthesis of 165 g D-allose per l within 6 h678884
synthesisStreptococcus pneumoniae-RpiB is a potential producer of L-form monosaccharides717008

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
AdenomaIs intravenous urography mandatory in the management of benign prostatic hyperplasia? PubMed
Alzheimer DiseaseRelease from proactive interference in early Alzheimer's disease. PubMed
AmblyopiaRetinitis pigmentosa inversa with unilateral high myopia with fellow eye optic disc pitting. PubMed
AnemiaClinical significance of immature reticulocyte fraction determined by automated reticulocyte counting. PubMed
Anemia, Iron-DeficiencyClinical significance of immature reticulocyte fraction determined by automated reticulocyte counting. PubMed
AtherosclerosisDietary rice protein isolate attenuates atherosclerosis in apoE-deficient mice by upregulating antioxidant enzymes. PubMed,  PubMed
Autoimmune DiseasesAnti-RNA polymerase I antibodies in the sera of MRL lupus mice at the initial stages of disease are directed primarily against phosphorylation-dependent epitopes. PubMed
Bacterial InfectionsRetrograde peri-implantitis: a case report introducing an approach to its management. PubMed
Brain NeoplasmsAssessment of vascular supply of hypervascular extra-axial brain tumors with 3T MR regional perfusion imaging. PubMed
Breast NeoplasmsIn vitro actions on human cancer cells and the liquid chromatography-mass spectrometry/mass spectrometry fingerprint of phytochemicals in rice protein isolate. PubMed
CarcinogenesisA rice protein isolate alters 7,12-dimethylbenz[alpha]anthracene-induced mammary tumor development in female rats. PubMed
CarcinomaBasal cell carcinoma with perineural invasion: reexcision perineural invasion? PubMed
Carcinoma, Basal CellBasal cell carcinoma with perineural invasion: reexcision perineural invasion? PubMed
Carcinoma, Hepatocellular[Experimental and clinical studies on ribosephosphate isomerase (author's transl)]. PubMed
Chagas DiseaseRibose 5-phosphate isomerase type B from Trypanosoma cruzi: kinetic properties and site-directed mutagenesis reveal information about the reaction mechanism. PubMed
CystsStudies on the metabolism of Echinococcus granulosus. V. The phosphopentose isomerase of hydatid cyst scolices. PubMed
EchinococcosisStudies on the metabolism of Echinococcus granulosus. V. The phosphopentose isomerase of hydatid cyst scolices. PubMed
EndocarditisIn vivo activities and penetration of the two components of the streptogramin RP 59500 in cardiac vegetations of experimental endocarditis. PubMed
Hepatitis[Experimental and clinical studies on ribosephosphate isomerase (author's transl)]. PubMed
HIV InfectionsRetrograde peri-implantitis: a case report introducing an approach to its management. PubMed
Huntington DiseaseReduced neuronal expression of ribose-5-phosphate isomerase enhances tolerance to oxidative stress, extends lifespan, and attenuates polyglutamine toxicity in Drosophila. PubMed
HypercholesterolemiaRice protein isolate improves lipid and glucose homeostasis in rats fed high fat/high cholesterol diets. PubMed
HypertensionBiofeedback of R-wave-to-pulse interval normalizes blood pressure. PubMed
HypotensionBiofeedback of R-wave-to-pulse interval normalizes blood pressure. PubMed
InfectionClinical significance of immature reticulocyte fraction determined by automated reticulocyte counting. PubMed
InfectionComparative efficacies of procalcitonin and conventional inflammatory markers for prediction of renal parenchymal inflammation in pediatric first urinary tract infection. PubMed
InfectionRetrograde peri-implantitis: a case report introducing an approach to its management. PubMed
Insulin ResistanceRice protein isolate improves lipid and glucose homeostasis in rats fed high fat/high cholesterol diets. PubMed
Intermittent ClaudicationPathophysiologic classification of peripheral vascular disease by positional changes in regional transcutaneous oxygen tension. PubMed
Intermittent ClaudicationUse of a transcutaneous PO2 regional perfusion index to quantify tissue perfusion in peripheral vascular disease. PubMed
LeukoencephalopathiesRibose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy. PubMed
Leukoencephalopathies[A newly discovered metabolic diseases due to defects in the pentose pathway]. PubMed
Lupus Erythematosus, SystemicAnti-RNA polymerase I antibodies in the sera of MRL lupus mice at the initial stages of disease are directed primarily against phosphorylation-dependent epitopes. PubMed
MeningiomaAssessment of vascular supply of hypervascular extra-axial brain tumors with 3T MR regional perfusion imaging. PubMed
Myelodysplastic SyndromesClinical significance of immature reticulocyte fraction determined by automated reticulocyte counting. PubMed
MyopiaRetinitis pigmentosa inversa with unilateral high myopia with fellow eye optic disc pitting. PubMed
Neoplasm Metastasis[Experimental and clinical studies on ribosephosphate isomerase (author's transl)]. PubMed
NeoplasmsA rice protein isolate alters 7,12-dimethylbenz[alpha]anthracene-induced mammary tumor development in female rats. PubMed
NeoplasmsAssessment of vascular supply of hypervascular extra-axial brain tumors with 3T MR regional perfusion imaging. PubMed
NeoplasmsCritical evaluation of the usefulness of different reticulocyte parameters in monitoring the erythropoiesis reaction to cancer chemotherapy. PubMed
NeoplasmsIn vitro actions on human cancer cells and the liquid chromatography-mass spectrometry/mass spectrometry fingerprint of phytochemicals in rice protein isolate. PubMed
NeoplasmsThe relative proliferation index as a more sensitive parameter for evaluating lymphoproliferative responses of cancer patients to mitogens and alloantigens. PubMed
Neoplasms[Experimental and clinical studies on ribosephosphate isomerase (author's transl)]. PubMed
Night BlindnessRetinitis pigmentosa inversa with unilateral high myopia with fellow eye optic disc pitting. PubMed
PainPathophysiologic classification of peripheral vascular disease by positional changes in regional transcutaneous oxygen tension. PubMed
PainTransabdominal versus retroperitoneal incision for abdominal aortic surgery: report of a prospective randomized trial. PubMed
Peripheral Nervous System DiseasesRibose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy. PubMed
Pre-EclampsiaErythrocyte changes in preeclampsia: relationship between maternal and cord blood erythrocyte damage. PubMed
Pressure UlcerReproducibility of transcutaneous oxygen pressure measurements in persons with spinal cord injury. PubMed
ProteinuriaErythrocyte changes in preeclampsia: relationship between maternal and cord blood erythrocyte damage. PubMed
PyelonephritisAn ultrasonographic renal parenchymal index. PubMed
Retinitis PigmentosaRetinitis pigmentosa inversa with unilateral high myopia with fellow eye optic disc pitting. PubMed
ribose-5-phosphate isomerase deficiencyAnalysis of polyols in urine by liquid chromatography-tandem mass spectrometry: a useful tool for recognition of inborn errors affecting polyol metabolism. PubMed
ribose-5-phosphate isomerase deficiencyRibose-5-phosphate isomerase deficiency: new inborn error in the pentose phosphate pathway associated with a slowly progressive leukoencephalopathy. PubMed
ribose-5-phosphate isomerase deficiencyThe difference between rare and exceptionally rare: molecular characterization of ribose 5-phosphate isomerase deficiency. PubMed
transaldolase deficiencyAnalysis of polyols in urine by liquid chromatography-tandem mass spectrometry: a useful tool for recognition of inborn errors affecting polyol metabolism. PubMed
TuberculosisCompetitive inhibitors of Mycobacterium tuberculosis ribose-5-phosphate isomerase B reveal new information about the reaction mechanism. PubMed
TuberculosisCompetitive inhibitors of type B ribose 5-phosphate isomerases: design, synthesis and kinetic evaluation of new D-allose and D-allulose 6-phosphate derivatives. PubMed
TuberculosisD-ribose-5-phosphate isomerase B from Escherichia coli is also a functional D-allose-6-phosphate isomerase, while the Mycobacterium tuberculosis enzyme is not. PubMed
TuberculosisMycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active site. PubMed
Urinary Tract InfectionsComparative efficacies of procalcitonin and conventional inflammatory markers for prediction of renal parenchymal inflammation in pediatric first urinary tract infection. PubMed

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2624Noltmann, E.A.Aldose-ketose isomerasesThe Enzymes, 3rd Ed. (Boyer, P.D., ed.)6271-3541972Echinococcus granulosus, Enterobacter aerogenes, Homo sapiens, Pediococcus pentosaceus, Rhodospirillum rubrum, Saccharomyces cerevisiae, Spinacia oleracea-
2775Kiely, M.E.; Stuart, A.L.; Wood, T.Partial purification and kinetic properties of ribose-5-phosphate ketol-isomerase and ribulose-5-phosphate 3-epimerase from various sourcesBiochim. Biophys. Acta293534-5411973Bos taurus PubMed
2776Domagk, G.F.; Doering, K.M.; Chilla, R.Purification and properties of ribose-phosphate isomerase from Candida utilisEur. J. Biochem.38259-2641973Cyberlindnera jadinii PubMed
2777Wood, T.The detection and occurence of multiple forms of D-ribose 5-phosphate ketol isomeraseArch. Biochem. Biophys.16040-461974Rattus norvegicus, Spinacia oleracea PubMed
2778Domagk, G.F.; Alexander, W.R.; Doering, K.M.Purification and properties of ribosephosphate isomerase from skeletal muscleHoppe-Seyler's Z. Physiol. Chem.355781-7861984Bos taurus-
2779Essenberg, M.K.; Cooper, R.A.Two ribose-5-phosphate isomerases from Escherichia coli K12: partial characterization of the enzymes and consideration of their possible physiological rolesEur. J. Biochem.55323-3321975Escherichia coli, Escherichia coli (P17169), Escherichia coli K12 PubMed
2780Domagk, G.F.; Alexander, W.R.D-Ribose-5-phosphate isomerase from skeletal muscleMethods Enzymol.41A424-4261975Bos taurus PubMed
2781Domagk, G.F.; Doering, K.M.D-Ribose-5-phosphate isomerase from Candida utilisMethods Enzymol.41B427-4291975Cyberlindnera jadinii PubMed
2782Horitsu, H.; Sasaki, I.; Kikuchi, T.; Suzuki, H.; Sumida, M.; Tomoyeda, M.Purification, properties and structure of ribose 5-phosphate ketol isomerase from Candida utilisAgric. Biol. Chem.40257-2641976Cyberlindnera jadinii-
2783Middaugh, C.R.; MacElroy, R.D.The effect of temperature on ribose-5-phosphate isomerase from mesophile Thiobacillus thioparus, and a thermophile, Bacillus caldolyticusJ. Biochem.791331-13441976Bacillus caldolyticus, Thiobacillus thioparus PubMed
2784Horitsu, H.; Sumida, M.; Banno, Y.; Tomoyeda, M.Three forms of Candida utilis ribose 5-phosphate ketol isomeraseAgric. Biol. Chem.422195-22011978Cyberlindnera jadinii-
2785Horitsu, H.; Banno, Y.; Kimura, S.; Shimizu, H.; Tomoyeda, M.Chromatographic purification of ribose 5-phosphate ketol isomerase from Candida utilis on p-mercuribenzoate-6-aminohexyl-Sepharose 4B adsorbentAgric. Biol. Chem.43663-6641979Cyberlindnera jadinii-
2786Woodruff, W.W.; Wolfenden, R.Inhibition of ribose-5-phosphate isomerase by 4-phosphoerythronateJ. Biol. Chem.2545866-58671979Spinacia oleracea PubMed
2787MacElroy, R.D.; Middaugh, C.R.Bacterial ribosephosphate isomeraseMethods Enzymol.89571-5791982Bacillus caldolyticus, Chromatium sp., Chromatium sp. D, Escherichia coli, Escherichia coli (P0AB71), Halothiobacillus neapolitanus, Rhodospirillum rubrum, Thiobacillus thioparus PubMed
2788Sainis, J.K.; Harris, G.C.The association of ribulose-1,5-bisphosphate carboxylase with phosphoriboisomerase and phosphoribulokinaseBiochem. Biophys. Res. Commun.139947-9541986Pisum sativum PubMed
2789Skrukrud, C.L.; Anderson, L.E.Chloroplast phosphoribulokinase associates with yeast phosphoriboisomerase in the presence of substrateFEBS Lett.280259-2611991Cyberlindnera jadinii PubMed
2790Anderson, L.E.Ribose-5-phosphate isomerase and ribulose-5-phosphate kinase show apparent specificity for a specific ribulose 5-phosphate speciesFEBS Lett.21245-481987Cyberlindnera jadinii PubMed
2791Cronin, C.N.; Nolan, D.P.; Voorheis, H.P.The enzymes of the classical pentose phosphate pathway display differential activities in procyclic and bloodstream forms of Trypanosoma bruceiFEBS Lett.24426-301989Trypanosoma brucei PubMed
2792Skrukrud, C.L.; Gordon, I.M.; Dorwin, S.; Yuan, X.H.; Johansson, G.; Anderson, L.E.Purification and characterization of pea chloroplastic phosphoriboseisomerasePlant Physiol.97730-7351991Pisum sativum PubMed
2793Malaisse, W.J.; Zhner, D.; Malaisse-Lagae, F.; Verbruggen, I.; Kayser, F.; Biesemans, M.; Willem, R.Diastereotopic specificity of phosphoriboisomeraseMed. Sci. Res.22247-2491994Saccharomyces cerevisiae, Saccharomyces cerevisiae (P53323)-
2794Martin, W.; Henze, K.; Kellermann, J.; Flechner, A.; Scharrenberger, C.Microsequencing and cDNA cloning of the Calvin cycle/OPPP enzyme ribose-5-phosphate isomerase (EC 5.3.1.6) from spinach chloroplastsPlant Mol. Biol.30795-8051996Spinacia oleracea PubMed
2795Sudhakar, C.; Ramanjulu, S.; Srenivasuklu Reddy, P.; Veeranjaneyulu, K.Response of some Calvin cycle enzymes subjected to salinity shock in vitroIndian J. Exp. Biol.35665-6671997Macrotyloma uniflorum PubMed
2797Horitsu, K.Die Isolierung und der Bestandteil des seltenen sauren Proteins im sugetierischen Organ. Teil 3. Die Verfeinerung und die einigen chemischen Eigenschaften der Ribose-5-phosphate-isomerase aus der SchweinemilzBull. Tokyo Kasei University2851-561988Sus scrofa-
649425Jung, C.H.; Hartman, F.C.; Lu, T.Y.S.; Larimer, F.W.D-Ribose-5-phosphate isomerase from spinach: heterologous overexpression, purification, characterization, and site-directed mutagenesis of the recombinant enzymeArch. Biochem. Biophys.373409-4172000Spinacia oleracea PubMed
652484Hamada, K.; Ago, H.; Sugahara, M.; Nodake, Y.; Kuramitsu, S.; Miyano, M.Oxyanion hole-stabilized stereospecific isomerization in ribose-5-phosphate isomerase (Rpi)J. Biol. Chem.27849183-491902003Thermus thermophilus PubMed
652933Roos, A.K.; Andersson, C.E.; Bergfors, T.; Jacobsson, M.; Karlen, A.; Unge, T.; Jones, T.A.; Mowbray, S.L.Mycobacterium tuberculosis ribose-5-phosphate isomerase has a known fold, but a novel active siteJ. Mol. Biol.335799-8092004Mycobacterium tuberculosis PubMed
653838Rangarajan, E.S.; Sivaraman, J.; Matte, A.; Cygler, M.Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coliProteins48737-7402002Escherichia coli PubMed
653906Ishikawa, K.; Matsui, I.; Payan, F.; Cambillau, C.; Ishida, H.; Kawarabayasi, Y.; Kikuchi, H.; Roussel, A.A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structureStructure10877-8862002Pyrococcus horikoshii, Pyrococcus horikoshii (O50083) PubMed
653911Zhang, R.; Andersson, C.E.; Savchenko, A.; Skarina, T.; Evdokimova, E.; Beasley, S.; Arrowsmith, C.H.; Edwards, A.M.; Joachimiak, A.; Mowbray, S.L.Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycleStructure1131-422003Escherichia coli, Escherichia coli (P0A7Z0) PubMed
660967Kondo, H.; Nakamura, Y.; Dong, Y.X.; Nikawa, J.; Sueda, S.Pyridoxine biosynthesis in yeast: participation of ribose 5-phosphate ketol-isomeraseBiochem. J.37965-702004Saccharomyces cerevisiae PubMed
661234Dani, D.N.; Sainis, J.K.Isolation and characterization of a thylakoid membrane module showing partial light and dark reactionsBiochim. Biophys. Acta166943-522005Synechococcus elongatus PCC 7942 PubMed
661287Graille, M.; Meyer, P.; Leulliot, N.; Sorel, I.; Janin, J.; Van Tilbeurgh, H.; Quevillon-Cheruel, S.Crystal structure of the S. cerevisiae D-ribose-5-phosphate isomerase: comparison with the archaeal and bacterial enzymesBiochimie87763-7692005Saccharomyces cerevisiae PubMed
662445Roos, A.K.; Burgos, E.; Ericsson, D.J.; Salmon, L.; Mowbray, S.L.Competitive inhibitors of Mycobacterium tuberculosis ribose-5-phosphate isomerase B reveal new information about the reaction mechanismJ. Biol. Chem.2806416-64222005Mycobacterium tuberculosis, Mycobacterium tuberculosis (Q79FD7) PubMed
663425Burgos, E.; Salmon, L.Synthesis and kinetic evaluation of 4-deoxy-4-phosphonomethyl-D-erythronate, the first hydrolytically stable and potent competitive inhibitor of ribose-5-phosphate isomeraseTetrahedron Lett.453465-34692004Spinacia oleracea-
663426Burgos, E.; Salmon, L.Synthesis and evaluation of new 4-phospho-D-erythronic acid derivatives as competitive inhibitors of spinach ribose-5-phosphate isomeraseTetrahedron Lett.45753-7562004Spinacia oleracea-
663427Burgos, E.; Roos, A.K.; Mowbray, S.L.; Salmon, L.Synthesis of 5-deoxy-5-phospho-D-ribonohydroxamic acid: a new competitive and selective inhibitor of type B ribose-5-phosphate isomerase from Mycobacterium tuberculosisTetrahedron Lett.463691-36942005Mycobacterium tuberculosis, Spinacia oleracea-
676674Anderson, L.E.; Chrostowski, J.; Carol, A.A.Enzyme co-localization with transketolase, xylulose-5-P 3-epimerase and phosphoriboisomerase in pea leaf chloroplastsPlant Sci.171686-6982006Pisum sativum-
677394Holmes, M.A.; Buckner, F.S.; Van Voorhis, W.C.; Verlinde, C.L.; Mehlin, C.; Boni, E.; DeTitta, G.; Luft, J.; Lauricella, A.; Anderson, L.; Kalyuzhniy, O.; Zucker, F.; Schoenfeld, L.W.; Earnest, T.N.; Hol, W.G.; Merritt, E.A.Structure of ribose 5-phosphate isomerase from Plasmodium falciparumActa Crystallogr. Sect. FF62427-4312006Plasmodium falciparum PubMed
678047Stern, A.L.; Burgos, E.; Salmon, L.; Cazzulo, J.J.Ribose 5-phosphate isomerase type B from Trypanosoma cruzi: kinetic properties and site-directed mutagenesis reveal information about the reaction mechanismBiochem. J.401279-2852007Trypanosoma cruzi, Trypanosoma cruzi (A1BTJ7) PubMed
678884Park, C.S.; Yeom, S.J.; Kim, H.J.; Lee, S.H.; Lee, J.K.; Kim, S.W.; Oh, D.K.Characterization of ribose-5-phosphate isomerase of Clostridium thermocellum producing D-allose from D-psicoseBiotechnol. Lett.291387-13912007Clostridium thermocellum PubMed
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705731Kim, T.G.; Kwon, T.H.; Min, K.; Dong, M.S.; Park, Y.I.; Ban, C.Crystal structures of substrate and inhibitor complexes of ribose 5-phosphate isomerase A from Vibrio vulnificus YJ016Mol. Cells2799-1032009Vibrio vulnificus (Q7MHL9), Vibrio vulnificus PubMed
706109Xiong, Y.; DeFraia, C.; Williams, D.; Zhang, X.; Mou, Z.Deficiency in a cytosolic ribose-5-phosphate isomerase causes chloroplast dysfunction, late flowering and premature cell death in ArabidopsisPhysiol. Plant.137249-2632009Arabidopsis thaliana (Q9ZU38) PubMed
713894Yeom, S.J.; Seo, E.S.; Kim, Y.S.; Oh, D.K.Increased D-allose production by the R132E mutant of ribose-5-phosphate isomerase from Clostridium thermocellumAppl. Microbiol. Biotechnol.891859-18662011Clostridium thermocellum (A3DIL8), Clostridium thermocellum, Clostridium thermocellum ATCC 27405 (A3DIL8) PubMed
713908Jung, J.; Kim, J.K.; Yeom, S.J.; Ahn, Y.J.; Oh, D.K.; Kang, L.W.Crystal structure of Clostridium thermocellum ribose-5-phosphate isomerase B reveals properties critical for fast enzyme kineticsAppl. Microbiol. Biotechnol.90517-5272011Clostridium thermocellum (A3DIL8), Clostridium thermocellum, Clostridium thermocellum ATCC 27405 (A3DIL8) PubMed
714990Stern, A.L.; Naworyta, A.; Cazzulo, J.J.; Mowbray, S.L.Structures of type B ribose 5-phosphate isomerase from Trypanosoma cruzi shed light on the determinants of sugar specificity in the structural familyFEBS J.278793-8082011Trypanosoma cruzi, Trypanosoma cruzi (A1BTJ7), Trypanosoma cruzi Brenner (A1BTJ7) PubMed
717008Park, C.; Yeom, S.; Lim, Y.; Kim, Y.; Oh, D.Substrate specificity of a recombinant ribose-5-phosphate isomerase from Streptococcus pneumoniae and its application in the production of l-lyxose and l-tagatoseWorld J. Microbiol. Biotechnol.27743-7502011Streptococcus pneumoniae-

LINKS TO OTHER DATABASES (specific for EC-Number 5.3.1.6)
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)