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Information on EC 5.3.1.6 - ribose-5-phosphate isomerase for references in articles please use BRENDA:EC5.3.1.6Word Map on EC 5.3.1.6
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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ribose-5-phosphate isomerase
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D-Ribose 5-phosphate = D-ribulose 5-phosphate
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intramolecular oxidoreduction
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Bifidobacterium shunt
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Calvin-Benson-Bassham cycle
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formaldehyde assimilation II (assimilatory RuMP Cycle)
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formaldehyde assimilation III (dihydroxyacetone cycle)
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pentose phosphate pathway (non-oxidative branch)
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pentose phosphate pathway
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Pentose phosphate pathway
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Fructose and mannose metabolism
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Carbon fixation in photosynthetic organisms
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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Biosynthesis of antibiotics
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D-ribose-5-phosphate aldose-ketose-isomerase
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
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5-phosphate ketol-isomerase
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5-Phosphoribose isomerase
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D-Ribose 5-phosphate isomerase
D-ribose-5-phosphate isomerase
D-ribose-5-phosphate isomerase A
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D-ribose-5-phosphate isomerase B
D-ribose-5-phosphate ketol-isomerase
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D-xylose ketol-isomerase
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Isomerase, ribose phosphate
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Phosphopentoisomerase
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Phosphopentose isomerase
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ribose 5-phosphate isomerase A
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Ribose phosphate isomerase
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Ribose-5-P isomerase
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ribose-5-phosphate isomerase
ribose-5-phosphate isomerase B
ribose-5-phosphate isomerase type B
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Ribosephosphate isomerase A
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Ribosephosphate isomerase B
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type B ribose 5-phosphate isomerase
type B ribose-5-phosphate isomerase
CTRpiB
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D-Ribose 5-phosphate isomerase
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D-Ribose 5-phosphate isomerase
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D-Ribose 5-phosphate isomerase
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D-ribose-5-phosphate isomerase
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D-ribose-5-phosphate isomerase
D1NPG0;
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D-ribose-5-phosphate isomerase B
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D-ribose-5-phosphate isomerase B
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Phosphoriboisomerase
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ribose-5-phosphate isomerase
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ribose-5-phosphate isomerase
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ribose-5-phosphate isomerase
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ribose-5-phosphate isomerase
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ribose-5-phosphate isomerase
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ribose-5-phosphate isomerase B
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ribose-5-phosphate isomerase B
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ribose-5-phosphate isomerase B
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ribose-5-phosphate isomerase B
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RPI
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RpiA
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RpiB
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type B ribose 5-phosphate isomerase
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type B ribose 5-phosphate isomerase
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type B ribose 5-phosphate isomerase
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type B ribose 5-phosphate isomerase
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type B ribose-5-phosphate isomerase
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type B ribose-5-phosphate isomerase
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type B Rpi
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gene RPI2, At2g01290
UniProt
brenda
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brenda
Chromatium sp.
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
strain DSM 2661
UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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Uniprot
brenda
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brenda
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brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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brenda
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brenda
HB8
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brenda
HB8
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brenda
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brenda
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brenda
gene rpiA
UniProt
brenda
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brenda
calf; ox
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brenda
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brenda
physical interaction between phosphoribulokinase and phosphoriboisomerase in the presence of substrate
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brenda
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brenda
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Uniprot
brenda
gene rpiB
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brenda
two enzyme forms: constitutive isomerase A and inducible isomerase B
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brenda
two 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 RpiB
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brenda
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brenda
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SwissProt
brenda
gene rpiB
SwissProt
brenda
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SwissProt
brenda
gene rpiB
SwissProt
brenda
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brenda
phosphoribulokinase and phosphoriboisomerase are associated to a complex
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brenda
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brenda
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UniProt
brenda
RpiB; gene rpiB
D1NPG0
UniProt
brenda
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brenda
three electrophoretic forms
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brenda
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UniProt
brenda
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SwissProt
brenda
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UniProt
brenda
type B enzyme
UniProt
brenda
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UniProt
brenda
type B enzyme
UniProt
brenda
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malfunction
deficiency in a cytosolic ribose-5-phosphate isomerase causes chloroplast dysfunction, late flowering and premature cell death in Arabidopsis thaliana
metabolism
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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 pathway
metabolism
two 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 sources
metabolism
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ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
metabolism
ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
metabolism
the 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 metabolism
metabolism
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the enzyme plays an essential role in the pentose phosphate pathway and the Calvin cycle of photosynthesis
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D-allose 6-phosphate
D-allulose 6-phosphate
D-Glucose 6-phosphate
?
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?
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
D-ribose 5-phosphate
D-ribulose 5-phosphate
D-ribose 5-triphosphate
D-ribulose 5-triphosphate
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?
D-ribose-5-phosphate
D-ribulose-5-phosphate
D-ribulose 5-diphosphate
D-ribose 5-diphosphate
D-ribulose 5-phosphate
D-ribose 5-phosphate
L-Mannose
L-Fructose
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r
additional information
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D-Allose
D-Psicose
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r
D-Allose
D-Psicose
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r
D-Allose
D-Psicose
D1NPG0;
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r
D-Allose
D-Psicose
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r
D-Allose
D-Psicose
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?
D-Allose
D-Psicose
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substrates D-allose and D-psicose are preferred over ribose 5-phosphate
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r
D-Allose
D-Psicose
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?
D-Allose
D-Psicose
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r
D-allose 6-phosphate
D-allulose 6-phosphate
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r
D-allose 6-phosphate
D-allulose 6-phosphate
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r
D-gulose
D-sorbose
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r
D-gulose
D-sorbose
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r
D-psicose
D-allose
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r
D-psicose
D-allose
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the enzyme convertes D-psicose to D-allose maximally at 75°C and pH 8.0 with a 32% conversion yield
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D-psicose
D-allose
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the enzyme convertes D-psicose to D-allose maximally at 75°C and pH 8.0 with a 32% conversion yield
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D-psicose
D-allose
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substrates D-allose and D-psicose are preferred over ribose 5-phosphate
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r
D-psicose
D-allose
the conversion yield of D-psicose to D-allose is 32% for the R132E mutant enzyme and 25% for the wild type enzyme after 80 min
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r
D-psicose
D-allose
the conversion yield of D-psicose to D-allose is 32% for the R132E mutant enzyme and 25% for the wild type enzyme after 80 min
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D-psicose
D-allose
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D-Ribose
D-Ribulose
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r
D-Ribose
D-Ribulose
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D-Ribose
D-Ribulose
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D-Ribose
D-Ribulose
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?
D-Ribose
D-Ribulose
D1NPG0;
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38% conversion to D-ribose 5-phosphate yield after approximately 90 min
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r
D-Ribose
D-Ribulose
D1NPG0;
39% conversion yield after approximately 90 min
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r
D-Ribose
D-Ribulose
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?
D-Ribose
D-Ribulose
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r
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
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?
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
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substrates D-allose and D-psicose are preferred over ribose 5-phosphate
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r
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
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r
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
Chromatium sp.
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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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 RpiB
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
the enzyme plays essential roles in carbohydrate anabolism and catabolism
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
the open configuration of ribose 5-phosphate is required for isomerization and is reversibly converted to ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
direct or indirect catalytic role for the residues E107, D85 and K98
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
D1NPG0;
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
D1NPG0;
preferred substrate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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preferred substrate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
D1NPG0;
preferred substrate
38% conversion to D-ribose 5-phosphate yield after approximately 90 min at 50°C
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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diastereotopic specificity
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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ribose 5-phosphate ketol-isomerase, the translation product of the RKI1 gene plays a crucial role in pyridoxine synthesis in yeast
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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highest specific activity
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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key enzyme in the oxidative and reductive pentose-phosphate pathway for the conversion of ribose-5-phosphate to ribulose-5-phosphatre and vice versa
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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key enzyme in the oxidative and reductive pentose-phosphate pathway for the conversion of ribose-5-phosphate to ribulose-5-phosphatre and vice versa
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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D-ribose 5-phosphate
D-ribulose 5-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
binding mode of substrate, overview
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r
D-ribose-5-phosphate
D-ribulose-5-phosphate
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D-ribose-5-phosphate
D-ribulose-5-phosphate
the 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
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D-ribulose
D-ribose
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r
D-ribulose
D-ribose
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r
D-ribulose 5-diphosphate
D-ribose 5-diphosphate
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r
D-ribulose 5-diphosphate
D-ribose 5-diphosphate
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r
D-ribulose 5-phosphate
D-ribose 5-phosphate
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r
D-ribulose 5-phosphate
D-ribose 5-phosphate
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r
D-ribulose 5-phosphate
D-ribose 5-phosphate
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?
D-ribulose 5-phosphate
D-ribose 5-phosphate
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?
D-sorbose
D-gulose
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r
D-sorbose
D-gulose
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lowest activity with L-sorbose
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r
D-talose
D-tagatose
D1NPG0;
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r
D-talose
D-tagatose
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r
D-talose
D-tagatose
-
-
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?
D-talose
D-tagatose
-
-
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?
L-allose
L-psicose
D1NPG0;
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r
L-allose
L-psicose
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r
L-fructose
L-mannose
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r
L-fructose
L-mannose
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r
L-Lyxose
L-Xylulose
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r
L-Lyxose
L-Xylulose
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r
L-Lyxose
L-Xylulose
-
particularly high activity with L-lyxose
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r
L-ribose
L-ribulose
D1NPG0;
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r
L-ribose
L-ribulose
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r
L-tagatose
L-talose
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r
L-tagatose
L-talose
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particularly high activity with L-tagatose
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r
L-talose
L-tagatose
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r
L-talose
L-tagatose
-
preferred substrate
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r
L-talose
L-tagatose
D1NPG0;
89% conversion yield after approximately 90 min
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r
L-talose
L-tagatose
D1NPG0;
the enzyme prefers the forward reaction, high activity, 89% conversion to L-tagatose yield after approximately 90 min at 50°C
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r
L-talose
L-tagatose
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particularly high activity with L-talose
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r
L-xylulose
L-lyxose
-
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r
L-xylulose
L-lyxose
-
particularly high activity with L-lyxose
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r
additional information
?
-
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enzyme displays activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as D-ribose, D-allose, L-talose, L-lyxose, D-gulose, and L-mannose. The specific activity decreases in the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
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-
additional information
?
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enzyme displays activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as D-ribose, D-allose, L-talose, L-lyxose, D-gulose, and L-mannose. The specific activity decreases in the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
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-
-
additional information
?
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-
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 photosynthesis
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-
additional information
?
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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 enzymes
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-
additional information
?
-
-
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 uncertain
-
-
-
additional information
?
-
-
enzyme substrate synthesis, overview
-
-
-
additional information
?
-
-
no activity with D-allose 6-phosphate
-
-
-
additional information
?
-
enzyme substrate synthesis, overview
-
-
-
additional information
?
-
-
no activity with D-allose 6-phosphate
-
-
-
additional information
?
-
-
no substrate: D-xylose, L-rhamnose, D-altrose, D-galactose
-
-
-
additional information
?
-
-
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-allose
-
-
-
additional information
?
-
D1NPG0;
RpiB 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, overview
-
-
-
additional information
?
-
-
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 organisms
-
-
-
additional information
?
-
-
no activity is observed with D-mannose-6-phosphate
-
-
-
additional information
?
-
the enzyme cannot isomerizes D-allose 6-phosphate
-
-
-
additional information
?
-
-
the enzyme cannot isomerizes D-allose 6-phosphate
-
-
-
additional information
?
-
the enzyme cannot isomerizes D-allose 6-phosphate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-Allose
D-Psicose
-
-
-
-
r
D-Ribose
D-Ribulose
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
D-ribose-5-phosphate
D-ribulose-5-phosphate
Q9ZU38
the 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
-
-
-
D-talose
D-tagatose
-
-
-
-
r
L-allose
L-psicose
-
-
-
-
r
L-ribose
L-ribulose
-
-
-
-
r
L-talose
L-tagatose
-
preferred substrate
-
-
r
additional information
?
-
D-ribose 5-phosphate
D-ribulose 5-phosphate
P0CL19
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
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 RpiB
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
P0A7Z0
the enzyme plays essential roles in carbohydrate anabolism and catabolism
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
Q58998
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
P9WKD7
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
O50083
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
D1NPG0
preferred substrate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
preferred substrate
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
ribose 5-phosphate ketol-isomerase, the translation product of the RKI1 gene plays a crucial role in pyridoxine synthesis in yeast
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
Q8DRS5, Q8DTT9
-
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
highest specific activity
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
key enzyme in the oxidative and reductive pentose-phosphate pathway for the conversion of ribose-5-phosphate to ribulose-5-phosphatre and vice versa
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
-
key enzyme in the oxidative and reductive pentose-phosphate pathway for the conversion of ribose-5-phosphate to ribulose-5-phosphatre and vice versa
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
Q7MHL9
-
-
-
r
additional information
?
-
-
enzyme displays activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as D-ribose, D-allose, L-talose, L-lyxose, D-gulose, and L-mannose. The specific activity decreases in the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
-
-
additional information
?
-
-
enzyme displays activity only with aldose substrates possessing hydroxyl groups oriented in the right-handed configuration (Fischer projections) at the C2 and C3 positions, such as D-ribose, D-allose, L-talose, L-lyxose, D-gulose, and L-mannose. The specific activity decreases in the order D-ribose, D-allose, L-talose, L-lyxose, D-gulose, L-mannose
-
-
-
additional information
?
-
-
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 photosynthesis
-
-
-
additional information
?
-
-
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 enzymes
-
-
-
additional information
?
-
-
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 uncertain
-
-
-
additional information
?
-
-
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-allose
-
-
-
additional information
?
-
-
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 organisms
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
-
salinity shock causes decline in activity
additional information
-
1 mM Co2+, Mn2+, Mg2+, Ni2+, Zn2+, Ca2+, Cu2+, and EDTA do not influence enzyme activity
additional information
-
no activation by mono- or divalent cations
additional information
-
the enzyme is not activated by monovalent or divalent cations
additional information
enzyme is not metal-dependent
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-deoxy-4-phosphonomethyl-D-erythronate
-
stable and potent competitive inhibitor
4-phospho-D-erythronamide
-
competitive
4-phospho-D-erythronhydrazide
-
4-phospho-D-erythronohydrazide
-
competitive
4-phospho-D-erythronohydroxamic acid
competitive
4-phosphoerythronate
-
strong competitive
4-phosphono-D-erythronate
-
-
4-phosphono-D-erythronohydroxamate
-
-
4-phosphono-D-erythronohydroxamic acid
-
competitive
5-deoxy-5-phospho-D-ribonohydroxamate
-
-
5-deoxy-5-phospho-D-ribonohydroxamic acid
5-phospho-D-ribonohydroxamic acid
D-5-Phosphoribonic acid
-
-
D-allulose 6-phosphate
-
-
erythrose 4-phosphate
-
competitive
glyceraldehyde 3-phosphate
-
competitive
iodoacetic acid
suicide inhibitor
Mn2+
-
slight inhibition of enzyme form I and II, strong inhibition of enzyme form III
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
N-(5-phospho-D-ribonoyl)-glycine
N-(5-phospho-D-ribonoyl)-hydrazine
N-(5-phospho-D-ribonoyl)-methylamine
ribulose diphosphate
-
1.0 mM, strong
sedoheptulose bisphosphate
-
competitive
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acid
4-phospho-D-erythronate
-
-
4-phospho-D-erythronate
-
5'-AMP
-
competitive
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
competitive and selective inhibitor of type B ribose-5-phosphate isomerase from Mycobacterium tuberculosis
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
weak
5-phospho-D-ribonamide
-
-
5-phospho-D-ribonate
-
competitive inhibitor of a Rpi, displays specific inhibition of Mycobacterium tuberculosis RpiB versus Escherichia coli RpiB, inhibition kinetics, overview
5-phospho-D-ribonate
very strong competitive inhibitor of a Rpi, specific inhibition of Mycobacterium tuberculosis RpiB versus Escherichia coli RpiB, inhibition kinetics, overview
5-phospho-D-ribonohydroxamic acid
-
-
5-phospho-D-ribonohydroxamic acid
-
5-phospho-D-ribonohydroxamic acid
-
6-phosphogluconate
-
temperature-dependent inhibition
6-phosphogluconate
-
competitive
6-phosphogluconate
-
noncompetitive
6-phosphogluconate
-
temperature-dependent inhibition
Ag+
-
1 mM
AMP
-
temperature-dependent inhibition
AMP
-
temperature-dependent inhibition
arabinose 5-phosphate
-
arabinose 5-phosphate
-
-
arabinose 5-phosphate
RpiA 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, overview
Co2+
-
1 mM
D-Allose 6-phosphate
-
-
D-Allose 6-phosphate
weak competitive inhibitor
D-arabinose 5-phosphate
-
effective
D-arabinose 5-phosphate
-
-
iodoacetamide
-
-
iodoacetamide
5 mM, complete inhibition
iodoacetate
-
1.25 mM, 100% loss of ribosephosphate isomerase B, no effect on ribosephosphate isomerase A
Mg2+
-
0.01 M
Mg2+
-
MgCl2, noncompetitive
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
-
-
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
-
N-(5-phospho-D-ribonoyl)-glycine
-
poor inhibition with substrate D-ribose 5-phosphate, no inhibition with substrate D-allose 5-phosphate
N-(5-phospho-D-ribonoyl)-glycine
-
N-(5-phospho-D-ribonoyl)-hydrazine
-
-
N-(5-phospho-D-ribonoyl)-hydrazine
-
N-(5-phospho-D-ribonoyl)-methylamine
-
-
N-(5-phospho-D-ribonoyl)-methylamine
-
NEM
-
-
Organic mercurials
-
-
-
PCMB
-
-
Phenylmercuriacetate
-
reversible by 0.02-10 mM 2-mercaptoethanol, and by 10 mM Cys
Phenylmercuriacetate
-
reversible by 0.02-10 mM 2-mercaptoethanol, and by 10 mM Cys
phosphate
-
Sodium mersalyl
-
reversible by 2-mercaptoethanol, 0.02-10 mM, and by Cys, 10 mM
Sodium mersalyl
-
reversible by 2-mercaptoethanol, 0.02-10 mM, and by Cys, 10 mM
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acid
-
-
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acid
-
-
sulfhydryl reagents
-
-
Zn2+
-
0.01 M
additional information
-
enzyme is not affected by metal ions and not inhibited by EDTA
-
additional information
-
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, overview
-
additional information
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, overview
-
additional information
-
EDTA is not inhibitory
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-mercaptoethanol
-
stimulates
2-mercaptoethanol
-
stimulates
EDTA
-
stimulates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 - 10
D-Ribose 5-diphosphate
0.017 - 30
D-ribose 5-phosphate
0.52 - 4.41
D-ribose-5-phosphate
34
D-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
1.4 - 2.5
D-ribulose 5-diphosphate
0.015 - 15
D-ribulose 5-phosphate
232
D-talose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
98
L-allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
173
L-ribose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
319
L-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
125
L-tagatose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
additional information
additional information
-
106
D-Allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
460
D-Allose
-
pH 7.5, 40°C
43
D-psicose
-
mutant enzyme R132E, pH 7.5, 80°C
46
D-psicose
-
mutant enzyme R132D, pH 7.5, 80°C
53
D-psicose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
53
D-psicose
-
mutant enzyme R132K, pH 7.5, 80°C; wild type enzyme, pH 7.5, 80°C
54
D-psicose
-
mutant enzyme R132Q, pH 7.5, 80°C
56
D-psicose
-
mutant enzyme R132A, pH 7.5, 80°C
64
D-psicose
-
at pH 8.0 and 75°C
78
D-psicose
-
mutant enzyme R132I, pH 7.5, 80°C
44
D-ribose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
270
D-ribose
-
pH 7.5, 40°C
2
D-Ribose 5-diphosphate
mutant H102A, pH 8.4, 25°C
2 - 3
D-Ribose 5-diphosphate
muant H11A, pH 8.4, 25°C
4
D-Ribose 5-diphosphate
wild-type, pH 8.4, 25°C
10
D-Ribose 5-diphosphate
mutant H138A, pH 8.4, 25°C
0.017
D-ribose 5-phosphate
-
pH 7.5, 65°C, recombinant enzyme
0.108
D-ribose 5-phosphate
-
-
0.16
D-ribose 5-phosphate
-
enzyme form III
0.17
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme D85N
0.43
D-ribose 5-phosphate
-
-
0.67
D-ribose 5-phosphate
-
enzyme form II
0.74
D-ribose 5-phosphate
-
-
0.77
D-ribose 5-phosphate
-
enzyme form I
0.83
D-ribose 5-phosphate
-
ribosephosphate isomerase B
0.88
D-ribose 5-phosphate
-
-
1
D-ribose 5-phosphate
-
in 50 mM Tris-HCl, pH 7.5, at 37°C
1 - 2.1
D-ribose 5-phosphate
-
at 80°C and pH 7.0
1.17
D-ribose 5-phosphate
50°C, pH 6.0, wild-type enzyme
1.63
D-ribose 5-phosphate
-
-
1.8
D-ribose 5-phosphate
-
-
1.8
D-ribose 5-phosphate
-
-
2
D-ribose 5-phosphate
-
-
2.2
D-ribose 5-phosphate
-
-
2.39
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme D168N
2.5
D-ribose 5-phosphate
-
-
2.6
D-ribose 5-phosphate
-
calf spleen
2.7
D-ribose 5-phosphate
-
-
2.8
D-ribose 5-phosphate
-
-
3.1
D-ribose 5-phosphate
-
3.3
D-ribose 5-phosphate
-
-
3.7
D-ribose 5-phosphate
-
-
4.4
D-ribose 5-phosphate
-
ribosephosphate isomerase A
4.6
D-ribose 5-phosphate
-
-
5.1
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme K125A
6.5
D-ribose 5-phosphate
-
ox muscle
7.13
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme R100A
7.6
D-ribose 5-phosphate
-
at 60°C and pH 7.0
9.1 - 10.2
D-ribose 5-phosphate
-
calf liver
17
D-ribose 5-phosphate
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
30
D-ribose 5-phosphate
-
pH 7.5, 40°C
0.52
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme D90A
0.56
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme D87A
0.63
D-ribose-5-phosphate
-
pH 8.0, 25°C, wild-type enzyme
1.17
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme E91A
4.41
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme K100A
1.4
D-ribulose 5-diphosphate
wild-type, pH 8.4, 25°C
2.5
D-ribulose 5-diphosphate
mutant H102A, pH 8.4, 25°C
0.015
D-ribulose 5-phosphate
-
pH 7.5, 65°C, recombinant enzyme
0.66
D-ribulose 5-phosphate
-
-
5
D-ribulose 5-phosphate
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30°C
15
D-ribulose 5-phosphate
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
5 - 20
L-talose
-
pH 7.5, 40°C
37
L-talose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
additional information
additional information
dramatic increase of Km-value at temperatures above 80°C
-
additional information
additional information
-
dramatic increase of Km-value at temperatures above 80°C
-
additional information
additional information
-
kinetics with aldose and ketose substrates, recombinant enzyme, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1 - 97
D-Ribose 5-diphosphate
8.3 - 52000
D-ribose 5-phosphate
0.0421 - 3440
D-ribose-5-phosphate
9193
D-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
4.7 - 10.7
D-ribulose 5-diphosphate
2 - 39530
D-ribulose 5-phosphate
119
D-talose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
1506
L-allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
322
L-ribose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
17
L-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
1822
L-tagatose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
200
D-Allose
-
pH 7.5, 40°C
2682
D-Allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
0.116
D-psicose
-
at pH 8.0 and 75°C
1962
D-psicose
-
mutant enzyme R132K, pH 7.5, 80°C
2211
D-psicose
-
mutant enzyme R132I, pH 7.5, 80°C
2335
D-psicose
-
mutant enzyme R132Q, pH 7.5, 80°C
2347
D-psicose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
2347
D-psicose
-
wild type enzyme, pH 7.5, 80°C
2580
D-psicose
-
mutant enzyme R132A, pH 7.5, 80°C
2674
D-psicose
-
mutant enzyme R132D, pH 7.5, 80°C
2743
D-psicose
-
mutant enzyme R132E, pH 7.5, 80°C
160
D-ribose
-
pH 7.5, 40°C
11880
D-ribose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
1
D-Ribose 5-diphosphate
mutant H102A, pH 8.4, 25°C
10
D-Ribose 5-diphosphate
mutant H138A, pH 8.4, 25°C
12
D-Ribose 5-diphosphate
wild-type, pH 8.4, 25°C
97
D-Ribose 5-diphosphate
muant H11A, pH 8.4, 25°C
8.3
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme D85N
47
D-ribose 5-phosphate
-
in 50 mM Tris-HCl, pH 7.5, at 37°C
120
D-ribose 5-phosphate
-
-
151
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme K125A
177
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme R100A
312
D-ribose 5-phosphate
50°C, pH 6.0, mutant enzyme D168N
320
D-ribose 5-phosphate
50°C, pH 6.0, wild-type enzyme
540
D-ribose 5-phosphate
-
at 60°C and pH 7.0
625
D-ribose 5-phosphate
93°C, pH 6, wild-type enzyme
1070
D-ribose 5-phosphate
-
50°C, pH 7.5
1072
D-ribose 5-phosphate
-
50°C, pH 7.5
1192
D-ribose 5-phosphate
-
at 80°C and pH 7.0
2100
D-ribose 5-phosphate
-
15100
D-ribose 5-phosphate
-
pH 7.5, 40°C
52000
D-ribose 5-phosphate
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C; pH 7.5, 65°C, recombinant enzyme
0.0421
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme D87A
2.5 - 4
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme K100A
2.54
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme K100A
13.2
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme D90A
946
D-ribose-5-phosphate
-
pH 8.0, 25°C, mutant enzyme E91A
3440
D-ribose-5-phosphate
-
pH 8.0, 25°C, wild-type enzyme
4.7
D-ribulose 5-diphosphate
wild-type, pH 8.4, 25°C
10.7
D-ribulose 5-diphosphate
mutant H102A, pH 8.4, 25°C
2 - 8
D-ribulose 5-phosphate
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30°C
50
D-ribulose 5-phosphate
50°C, pH 6.0, wild-type enzyme
39530
D-ribulose 5-phosphate
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C; pH 7.5, 65°C, recombinant enzyme
140
L-talose
-
pH 7.5, 40°C
13420
L-talose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.4
D-Allose
-
pH 7.5, 40°C
0.6
D-ribose
-
pH 7.5, 40°C
500 - 3029
D-ribose 5-phosphate
2589
D-ribulose 5-phosphate
-
pH 7.5, 65°C, recombinant enzyme
0.3
L-talose
-
pH 7.5, 40°C
0.0018
D-psicose
-
at pH 8.0 and 75°C
28
D-psicose
-
mutant enzyme R132I, pH 7.5, 80°C
37
D-psicose
-
mutant enzyme R132K, pH 7.5, 80°C
43
D-psicose
-
mutant enzyme R132Q, pH 7.5, 80°C
44
D-psicose
-
wild type enzyme, pH 7.5, 80°C
46
D-psicose
-
mutant enzyme R132A, pH 7.5, 80°C
58
D-psicose
-
mutant enzyme R132D, pH 7.5, 80°C
64
D-psicose
-
mutant enzyme R132E, pH 7.5, 80°C
500
D-ribose 5-phosphate
-
pH 7.5, 40°C
3029
D-ribose 5-phosphate
-
pH 7.5, 65°C, recombinant enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.074
4-deoxy-4-phosphonomethyl-D-erythronate
-
25°C
2.5
4-phospho-D-erythronamide
-
25°C, pH 7.5
1.7
4-phospho-D-erythronate
-
-
1.8
4-phospho-D-erythronohydrazide
-
25°C, pH 7.5
1.2
4-phospho-D-erythronohydroxamic acid
pH 8.4, 25°C
0.028
4-phosphono-D-erythronate
-
25°C, pH 7.5
0.057
4-phosphono-D-erythronohydroxamate
-
-
0.029
4-phosphono-D-erythronohydroxamic acid
-
25°C, pH 7.5
0.4 - 6.2
5-deoxy-5-phospho-D-ribonohydroxamic acid
0.04 - 0.07
5-phospho-D-ribonamide
0.009
5-phospho-D-ribonate
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.09 - 0.43
5-phospho-D-ribonohydroxamic acid
0.7
arabinose 5-phosphate
-
pH 8.0, 25°C
15
D-Allose 6-phosphate
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30°C
0.89
D-arabinose 5-phosphate
-
50°C, pH 7.5
0.34
N-(5-phospho-D-ribonoyl)-glycine
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.9
N-(5-phospho-D-ribonoyl)-hydrazine
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.11 - 0.18
N-(5-phospho-D-ribonoyl)-methylamine
4
Xylulose 5-phosphate
-
pH 8.0, 25°C
0.4
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
-
6.2
5-deoxy-5-phospho-D-ribonohydroxamic acid
-
-
0.04
5-phospho-D-ribonamide
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.07
5-phospho-D-ribonamide
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.09
5-phospho-D-ribonohydroxamic acid
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.26
5-phospho-D-ribonohydroxamic acid
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.43
5-phospho-D-ribonohydroxamic acid
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.11
N-(5-phospho-D-ribonoyl)-methylamine
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.18
N-(5-phospho-D-ribonoyl)-methylamine
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
7.9
phosphate
-
pH 8.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5
4-phospho-D-erythronate
Trypanosoma cruzi;
Q4CQE2
pH 8.4, 25°C
0.7
4-phospho-D-erythronohydroxamic acid
Trypanosoma cruzi;
Q4CQE2
pH 8.4, 25°C
0.2 - 1.33
5-phospho-D-ribonamide
0.031 - 1.31
5-phospho-D-ribonate
0.17 - 0.62
5-phospho-D-ribonohydroxamic acid
2
D-Allose 6-phosphate
Mycobacterium tuberculosis;
-
in 50 mM Tris-HCl, pH 7.5, at 37°C
6.3
D-allulose 6-phosphate
Mycobacterium tuberculosis;
-
in 50 mM Tris-HCl, pH 7.5, at 37°C
1.42 - 2
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
0.57 - 9
N-(5-phospho-D-ribonoyl)-glycine
1
N-(5-phospho-D-ribonoyl)-hydrazine
Mycobacterium tuberculosis;
P9WKD7
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.19 - 0.36
N-(5-phospho-D-ribonoyl)-methylamine
additional information
additional information
Trypanosoma cruzi;
Q4CQE2
IC50 values of 5-phospho-D-ribonohydroxamic acid and 4-phospho-D-erythronhydrazide are above 10 mM
-
0.2
5-phospho-D-ribonamide
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.22
5-phospho-D-ribonamide
Mycobacterium tuberculosis;
P9WKD7
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.33
5-phospho-D-ribonamide
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.031
5-phospho-D-ribonate
Mycobacterium tuberculosis;
P9WKD7
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.31
5-phospho-D-ribonate
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.17
5-phospho-D-ribonohydroxamic acid
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.44
5-phospho-D-ribonohydroxamic acid
Mycobacterium tuberculosis;
P9WKD7
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.62
5-phospho-D-ribonohydroxamic acid
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
1.42
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
Mycobacterium tuberculosis;
P9WKD7
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.6
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
2
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.57
N-(5-phospho-D-ribonoyl)-glycine
Mycobacterium tuberculosis;
P9WKD7
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
9
N-(5-phospho-D-ribonoyl)-glycine
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.19
N-(5-phospho-D-ribonoyl)-methylamine
Mycobacterium tuberculosis;
P9WKD7
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.35
N-(5-phospho-D-ribonoyl)-methylamine
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.36
N-(5-phospho-D-ribonoyl)-methylamine
Escherichia coli;
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0005
-
using D-sorbose as substrate, at 35°C and pH 7.5
0.0011
-
using L-fructose as substrate, at 35°C and pH 7.5
0.0013
-
using L-tagatose as substrate, at 35°C and pH 7.5
0.0019
-
using D-allose as substrate, at 35°C and pH 7.5
0.0021
-
using D-psicose as substrate, at 35°C and pH 7.5
0.0025
-
using D-ribose as substrate, at 35°C and pH 7.5
0.0053
-
using D-gulose as substrate, at 35°C and pH 7.5
0.0096
-
using L-lyxose as substrate, at 35°C and pH 7.5
0.019
-
using L-talose as substrate, at 35°C and pH 7.5
0.027
-
using L-lyxose as substrate, at 35°C and pH 7.5
0.048
-
using D-ribulose as substrate, at 35°C and pH 7.5
0.058
-
using D-glucose 6-phosphate as substrate, at 35°C and pH 7.5
0.121
-
using L-xylulose as substrate, at 35°C and pH 7.5
0.2
-
after 9.1fold purification, at pH 8.0 and 75°C
0.21
-
purified enzyme, using D-tagatose as substrate, at 65°C and pH 7.5
0.259
-
mutant enzyme H98A, using D-psicose as substrate, pH 7.5, 80°C
0.299
-
mutant enzyme H133A, using D-psicose as substrate, pH 7.5, 80°C; mutant enzyme R136A, using D-psicose as substrate, pH 7.5, 80°C
0.388
-
using D-ribose 5-phosphate as substrate, at 35°C and pH 7.5
0.53
-
purified enzyme, using L-allose as substrate, at 65°C and pH 7.5
0.698
-
mutant enzyme N99A, using D-psicose as substrate, pH 7.5, 80°C
0.917
-
mutant enzyme T67A, using D-psicose as substrate, pH 7.5, 80°C
1
-
substrate D-sorbose, pH 7.5, 40°C
1.256
-
mutant enzyme H9A, using D-psicose as substrate, pH 7.5, 80°C
1.815
-
mutant enzyme T135A, using D-psicose as substrate, pH 7.5, 80°C
1.994
-
wild type enzyme, using D-psicose as substrate, pH 7.5, 80°C
2.313
-
mutant enzyme R132A, using D-psicose as substrate, pH 7.5, 80°C
3
-
substrate D-psicose, pH 7.5, 40°C
7
-
substrate L-lyxose, pH 7.5, 40°C
9
-
substrate L-fructose, pH 7.5, 40°C
12
-
purified enzyme, using L-psicose as substrate, at 65°C and pH 7.5
14
-
substrate D-ribulose, pH 7.5, 40°C
15
-
substrate D-allose, pH 7.5, 40°C
28
-
substrate L-talose, pH 7.5, 40°C
45
-
substrate L-talose, pH 7.5, 40°C
50
-
purified enzyme, using D-talose as substrate, at 65°C and pH 7.5
53
-
substrate D-ribose, pH 7.5, 40°C
57
-
substrate L-xylulose, pH 7.5, 40°C
120
-
substrate D-gulose, pH 7.5, 40°C
187
-
cell lysate, at 50°C and pH 7.0
272
-
purified enzyme, using L-ribose as substrate, at 65°C and pH 7.5
290
-
after purification, at 50°C and pH 7.0
600
-
purified enzyme, using L-allose as substrate, at 65°C and pH 7.5
720
-
purified enzyme, using L-ribulose as substrate, at 65°C and pH 7.5
1037
-
purified enzyme, using D-psicose as substrate, at 65°C and pH 7.5; purified recombinant enzyme, substrate D-psicose
1352
-
purified enzyme, using D-allose as substrate, at 65°C and pH 7.5; purified recombinant enzyme, substrate D-allose
5374
-
purified enzyme, using D-ribulose as substrate, at 65°C and pH 7.5; purified recombinant enzyme, substrate D-ribulose
5800
-
purified enzyme, using D-ribose as substrate, at 65°C and pH 7.5; purified recombinant enzyme, substrate D-ribose
7363
-
purified enzyme, using L-talose as substrate, at 65°C and pH 7.5; purified recombinant enzyme, substrate L-talose
19680
-
purified enzyme, using D-ribulose 5-phosphate as substrate, at 65°C and pH 7.5; purified recombinant enzyme, substrate D-ribulose 5-phosphate
25690
-
purified enzyme, using D-ribose 5-phosphate as substrate, at 65°C and pH 7.5; purified recombinant enzyme, substrate D-ribose 5-phosphate
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.7 - 7.8
-
D-ribulose 5-phosphate, D-ribose 5-phosphate
7.5
-
-
7.5
-
optimum for synthesis of D-allose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6 - 9.9
-
pH 6: about 40% of maximal activity, pH 9.9: about 65% of maximal activity
6 - 9
-
more than 80% of its maximal activity is maintained at pH values from 6.0 to 9.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37
assay at
65
-
-
65
-
optimum for synthesis of D-allose
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30 - 80
-
30°C: about 50% of maximal activity, 80°C: about 45% of maximal activity
40 - 99
-
enzyme activity increases significantly when the temperature increases until 80°C. The optimum temperature is 80°C. The activity at 30°C is 25% of that at 80°C. The enzyme activity decreases after 80°C. It is still highly active when the temperature reaches 99°C, 90% activity of that of 80°C. This enzyme shows relatively high activity (above 50% of its maximum activity) over a large temperature range of 40-99°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4.77
isoelectric focusing
5.1
-
isoelectric focusing
6.4
-
isoelectric focusing
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
one electrophorectic form
brenda
-
-
brenda
-
two electrophorectic forms
brenda
-
-
brenda
-
two electrophorectic forms
brenda
-
one electrophorectic form
brenda
-
one electrophorectic form
brenda
-
-
brenda
-
-
brenda
-
two electrophorectic forms
brenda
-
two electrophorectic forms
brenda
-
brenda
-
-
-
brenda
highest expression
brenda
-
highest expression
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
one electrophorectic form
brenda
-
-
brenda
-
skeletal
brenda
-
two electrophorectic forms
brenda
-
-
brenda
-
two electrophoretic forms
brenda
-
-
brenda
metacyclic and in cell-culture
brenda
-
metacyclic and in cell-culture
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
brenda
-
-
brenda
-
-
brenda
-
co-localization of enzyme with phosphoribulokinase and Rubisco
brenda
-
-
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Q2GK74
Anaplasma phagocytophilum (strain HZ);
Q6G3V6
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1);
Q8YCV4
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094);
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264);
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372);
Escherichia coli (strain K12);
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4);
A4IYN5
Francisella tularensis subsp. tularensis (strain WY96-3418);
A8B2K2
Giardia intestinalis (strain ATCC 50803 / WB clone C6);
P44725
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
Q1WR87
Lactobacillus salivarius (strain UCC118);
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513);
Q58998
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440);
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P47636
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195);
B4RL16
Neisseria gonorrhoeae (strain NCCP11945);
Q8I3W2
Plasmodium falciparum;
Q9I6G1
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3);
Q12189
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
Q8DTT9
Streptococcus mutans serotype c (strain ATCC 700610 / UA159);
Q9X0G9
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099);
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039);
S8GQK2
Toxoplasma gondii (strain ATCC 50611 / Me49);
Trypanosoma cruzi (strain CL Brener);
Vibrio vulnificus (strain YJ016);
Q2SVL4
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264);
Q2SVL4
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264);
A3DIL8
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372);
A3DIL8
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372);
A3DIL8
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372);
P0A7Z0
Escherichia coli (strain K12);
P0A7Z0
Escherichia coli (strain K12);
P37351
Escherichia coli (strain K12);
P0A7Z0
Escherichia coli (strain K12);
P37351
Escherichia coli (strain K12);
Q5NFM5
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4);
Q5NFM5
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4);
Q5ZZB7
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513);
Q5ZZB7
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513);
P9WKD7
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WKD7
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WKD7
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WKD7
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WKD7
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P9WKD7
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
O50083
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3);
O50083
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3);
Q72J47
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039);
Q72J47
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039);
Q72J47
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039);
Q4CQE2
Trypanosoma cruzi (strain CL Brener);
Q4CQE2
Trypanosoma cruzi (strain CL Brener);
Q4CQE2
Trypanosoma cruzi (strain CL Brener);
Q4CQE2
Trypanosoma cruzi (strain CL Brener);
Q4CQE2
Trypanosoma cruzi (strain CL Brener);
Q7MHL9
Vibrio vulnificus (strain YJ016);
Q7MHL9
Vibrio vulnificus (strain YJ016);
Q7MHL9
Vibrio vulnificus (strain YJ016);
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
15867
-
x * 15867, calculated from amino acid sequence
16000
-
x * 16000, SDS-PAGE
16015
-
2 * 16015, calculated from amino acid sequence
16800
-
2 * 16800, SDS-PAGE
17200
-
2 * 17217, calculated, 2 * 17200, SD-PAGE
17217
-
2 * 17217, calculated, 2 * 17200, SD-PAGE
17300
-
2 * 17300, calculation from nucleotide sequence
17400
2 * 17400, calculated, 2 * 18000, SDS-PAGE
18000
2 * 17400, calculated, 2 * 18000, SDS-PAGE
23400
x * 23400, isoform RpiB, calculated from amino acid sequence
23724
-
4 * 23724, calculated from amino acid sequence
24000
-
4 * 24000, SDS-PAGE
24570
x * 24570, isoform RpiA, calculated from amino acid sequence
25000
-
2 * 25000, SDS-PAGE
25066
-
2 * 25066, calculation from nucleotide sequence
25163
4 * 25163, calculation from nucleotide sequence
25300
-
x * 25300, SDS-PAGE
26400
-
x * 26400, SDS-PAGE
30000 - 35000
-
gel filtration
32000
-
dynamic light scattering
32000 - 34000
-
ribosephosphate isomerase B, gel filtration
35000
-
about, native PAGE, recombinant enzyme
50000
-
dynamic light scattering
53000
-
high-speed equilibrium centrifugation
58000
-
4 * 58000, SDS-PAGE
75000
-
1 * 75000, alpha, + 2 * 54000, beta, SDS-PAGE
228000
-
analytical ultracentrifugation
17000
-
2 * 17000, gel filtration
17000
-
2 * 17000, X-ray crystallography
26000
-
2 * 26000, SDS-PAGE
26000
-
4 * 26000, SDS-PAGE
26000
4 * 26000, in crystal and in solution, each monomer has a new fold consisting of two alpha/beta domains, SDS-PAGE
34000
-
non-denaturing PAGE
40000
-
gel filtration
45000
-
ribosephosphate isomerase A, gel filtration
45000
recombinant detagged RpiA, dynamic light scattering and gel filtration
54000
-
1 * 75000, alpha, + 2 * 54000, beta, SDS-PAGE
57000
-
gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homotetramer
-
4 * 23724, calculated from amino acid sequence; 4 * 24000, SDS-PAGE
trimer
-
1 * 75000, alpha, + 2 * 54000, beta, SDS-PAGE
additional information
-
homology modeling of RpiB, substrate binding structure, overview
?
-
x * 26400, SDS-PAGE
?
x * 23400, isoform RpiB, calculated from amino acid sequence; x * 24570, isoform RpiA, calculated from amino acid sequence
?
-
x * 15867, calculated from amino acid sequence; x * 16000, SDS-PAGE
dimer
-
2 * 17217, calculated, 2 * 17200, SD-PAGE
dimer
-
2 * 17217, calculated, 2 * 17200, SD-PAGE
-
dimer
the two subunits in the dimer have different conformations, the result of motion of two largely rigid domains with respect to each other in the subunit
dimer
-
2 * 17300, calculation from nucleotide sequence
dimer
-
2 x 17500, about, recombinant enzyme, RpiB has an active-site interface between the dimer structures
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE; 2 * 25066, calculation from nucleotide sequence
dimer
2 * 17400, calculated, 2 * 18000, SDS-PAGE
dimer
-
2 * 17400, calculated, 2 * 18000, SDS-PAGE
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dimer
2 * 20000-25000, RpiA
homodimer
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2 * 16015, calculated from amino acid sequence; 2 * 16800, SDS-PAGE
homodimer
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2 * 16015, calculated from amino acid sequence; 2 * 16800, SDS-PAGE
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homodimer
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2 * 17000, gel filtration
homodimer
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2 * 17000, X-ray crystallography
homodimer
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2 * 17000, X-ray crystallography
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tetramer
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4 * 58000, SDS-PAGE
tetramer
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4 * 26000, SDS-PAGE
tetramer
RpiA crystal structure, overview
tetramer
4 * 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-PAGE
tetramer
x-ray crystallography
tetramer
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x-ray crystallography
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molecular dockng using L-xylose and D-ribose as the substrate. Residue M95 seems to be a determinant residue for the specificity on free sugars
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co-crystallization in the presence of 20 mM ribose-5-phosphate or 20 mM ribose-5-phosphate with 12 mM MnCl2, sitting drop vapor diffusion method, using 0.1 M Na citrate pH 5.0, 20% (w/v) PEG 6000
hanging drop vapor diffusion method, enzyme form RpiA
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hanging drop vapor diffusion method, structure of a complex with arabinose 5-phosphate at 1.25 A resolution
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, 18°C. 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 modeling
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 A
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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 acetate
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sitting drop vapour diffusion method
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molecular replacement at 2.9 A resolution
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hanging drop vapor diffusion method, crystal structure of the free enzyme and the complex with D-4-phosphoerythronic acid
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 chloride
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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, modeling
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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%
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sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium acetate, 0.1 M HEPES pH 7.5, 0.1 M NaCl, 2.0 M ammonium sulfate; sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris-HCl pH 8.5 and 25% (w/v) PEG 3350, 0.2 M MgCl2, 0.1 M Tris-HCl pH 8.5
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 resolution
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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-phosphate
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, 20°C, for complexed enzyme addition of 20 mM ligand, X-ray diffraction structure determination and analysis at 1.49-2.07 A resolution, molecular replacement
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5 - 10
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65°C, stable for at least 30 min
2783
5 - 10
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45°C, stable for at least 30 min
2783
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35 - 50
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enzyme activity is stable for 48 h at 35°C, and shows half-lives of 15 h at 40°C, and 6 h at 50°C
57
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1 h, 50% loss of activity
60
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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 concentration
60 - 75
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the half-lives of the wild type enzyme at 60°C, 65°C, 70°C, 75°C, and 80°C are 11, 7.0, 4.2, 1.5, and 0.6 h, respectively
60 - 80
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the purified enzyme at 0.1 mg/ml is very stable at 60 and 70°C but is deactivated at 80°C. The enzyme shows half lifetimes of 70.8, 53.1, 6.4, and 1.2 h at 60, 70, 80, and 90°C, respectively
75
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the half-life at 75°C is 3.3 h
91
-
1 h, 50% loss of activity
100
stability and integrity up to, needs at least 250 mM NaCl to maintain its hyperthermostability
45
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30 min, ribosephosphate isomerase A retains 90% of its activity, ribosephosphate isomerase B retains 60% of its activity
45
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pH 5-10, stable for at least 30 min
65
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pH 5-10, stable for at least 30 min
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(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, propanol
ethylene glycol has little effect on the mesophilic enzyme
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ethylene glycol increases stability
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freezing and thawing destroys activity
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maximum activities in sodium dihydrogen phosphate-ciitric acid buffer at pH 6.5-8.0 and in 50 mM Tris-HCl buffer pH 7.0-9.0. This enzyme retains about 65% activity from pH 8.8-11.0 in glycine-NaOH buffer
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(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, propanol
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(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, propanol
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-20°C, 2 months, stable
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-20°C, stable for several months
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-20°C, stable for several weeks
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2°C, stable for several months
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4°C, stable for 2 weeks
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4°C, stable for 6-8 weeks
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4°C, stable for several months
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affinity chromatographic method
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HisTrap HP column chromatography
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HisTrap HP column chromatography; recombinant RpiB from Escherichia coli strain ER2566 by His affinity chromatography
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HiTrap Q anion exchange column chromatography and Sephacryl S-300 gel filtration
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Ni-affinity column chromatography
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Ni-NTA column chromatography and Superdex 75 gel filtration
Ni2+-chelating column chromatography and Superdex S75 gel filtration; Ni2+-chelating column chromatography and Superdex S75 gel filtration
ox muscle, calf spleen and liver, partial
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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 filtration
recombinant MJ1603 from Escherichia coli strain Rosetta (DE3) by anion exchange and hydroxyapatite chromatography, and gel filtration
recombinant RpiB from Escherichia coli strain ER2566 by His affinity chromatography
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Superdex 75 gel filtration
-
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expressed in Escherichia coli BL21 (DE3) R3 Rosetta cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli ER2566 cells
expressed in Escherichia coli ER2566 cells; gene rpiB, expression in Escherichia coli strain ER2566
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expressed in Escherichia coli Top10 cells
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expression in Escherichia coli
expression of MJ1603 in Escherichia coli strain Rosetta (DE3)
gene RPI2, phylogenetic analysis
gene rpiA, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene rpiB, expression in Escherichia coli strain ER2566
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overexpression as a His-tagged Se-Met-labeled protein
overexpression in Escherichia coli
-
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli ER2566 cells
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expressed in Escherichia coli ER2566 cells
expressed in Escherichia coli ER2566 cells
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expression in Escherichia coli
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expression in Escherichia coli
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overexpression in Escherichia coli
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overexpression in Escherichia coli
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overexpression in Escherichia coli
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C65A
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the mutant shows no activity for D-psicose
D8A
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the mutant shows no activity for D-psicose
H133A
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the mutant shows 15% activity compared to the wild type enzyme
H98A
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the mutant shows 13% activity compared to the wild type enzyme
H9A
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the mutant shows 63% activity compared to the wild type enzyme
N99A
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the mutant shows 35% activity compared to the wild type enzyme
R132A
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the mutant exhibits an increase in D-psicose isomerization activity (116% activity compared to the wild type enzyme)
R132D
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the mutant shows increased catalytic efficiency toward D-psicose compared to the wild type enzyme
R132E
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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, respectively
R132I
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the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme
R132K
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the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme
R132Q
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the mutant shows decreased catalytic efficiency toward D-psicose compared to the wild type enzyme
R136A
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the mutant shows 15% activity compared to the wild type enzyme
T135A
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the mutant shows 91% activity compared to the wild type enzyme
T67A
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the mutant shows 46% activity compared to the wild type enzyme
Y42A
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the mutant shows no activity for D-psicose
C65A
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the mutant shows no activity for D-psicose
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H9A
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the mutant shows 63% activity compared to the wild type enzyme
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N99A
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the mutant shows 35% activity compared to the wild type enzyme
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R136A
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the mutant shows 15% activity compared to the wild type enzyme
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T135A
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the mutant shows 91% activity compared to the wild type enzyme
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R189K
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6% of the wild-type activity. Loss of the structural integrity of the protein seems to be responsible for the greatly diminished activity
D87A
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turnover number with D-ribose-5-phosphate is 0.0012% of value for the the wild-type enzyme, moderate change in Km-value
D90A
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turnover number with D-ribose-5-phosphate is 0.38% of value for the the wild-type enzyme, moderate change in Km-value
E91A
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turnover number with D-ribose-5-phosphate is 27.5% of value for the the wild-type enzyme, moderate change in Km-value
K100A
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turnover number with D-ribose-5-phosphate is 0.074% of value for the the wild-type enzyme, moderate change in Km-value
H102A
kinetics severeyl impaired with substrate ribose 5-phosphate, but not affected with substrate ribulose 5-phosphate
H11A
6fold increase in Km value, 8fold increase in kcat value, decrease in stability to freezing and thawing
H138A
little variations in kinetics compared to wild-type
C69A
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inactive; no catalytic activity
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H102A
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kinetics severeyl impaired with substrate ribose 5-phosphate, but not affected with substrate ribulose 5-phosphate
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H11A
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6fold increase in Km value, 8fold increase in kcat value, decrease in stability to freezing and thawing
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H138A
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little variations in kinetics compared to wild-type
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additional information
construction 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 26°C, phenotypes, detailed overview