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IUBMB Comments Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
rpi, ribose-5-phosphate isomerase, phosphoriboisomerase, ribose phosphate isomerase, ctrpi, d-ribose-5-phosphate isomerase, ribosephosphate isomerase b, ribosephosphate isomerase a, ribose-5-phosphate isomerase b, ribose 5-phosphate isomerase a,
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5-Phosphoribose isomerase
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D-Ribose 5-phosphate isomerase
D-ribose-5-phosphate isomerase A
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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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Phosphoriboisomerase
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Ribose phosphate isomerase
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Ribose-5-P isomerase
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Ribosephosphate isomerase A
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Ribosephosphate isomerase B
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type B 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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intramolecular oxidoreduction
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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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D-ribose 5-diphosphate
D-ribulose 5-diphosphate
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?
D-ribose 5-phosphate
D-ribulose 5-phosphate
D-ribose 5-triphosphate
D-ribulose 5-triphosphate
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?
D-allose 6-phosphate
D-allulose 6-phosphate
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r
D-ribose 5-phosphate
D-ribulose 5-phosphate
additional information
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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 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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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
additional information
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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
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additional information
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enzyme substrate synthesis, overview
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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
additional information
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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
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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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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
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5-phospho-D-ribonamide
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5-phospho-D-ribonate
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competitive inhibitor of a Rpi, displays specific inhibition of Mycobacterium tuberculosis RpiB versus Escherichia coli RpiB, inhibition kinetics, overview
5-phospho-D-ribonohydroxamic acid
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iodoacetate
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1.25 mM, 100% loss of ribosephosphate isomerase B, no effect on ribosephosphate isomerase A
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
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N-(5-phospho-D-ribonoyl)-glycine
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poor inhibition with substrate D-ribose 5-phosphate, no inhibition with substrate D-allose 5-phosphate
N-(5-phospho-D-ribonoyl)-hydrazine
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N-(5-phospho-D-ribonoyl)-methylamine
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additional information
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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
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3.1
D-ribose 5-phosphate
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0.83 - 4.4
D-ribose 5-phosphate
0.83
D-ribose 5-phosphate
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ribosephosphate isomerase B
4.4
D-ribose 5-phosphate
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ribosephosphate isomerase A
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2100
D-ribose 5-phosphate
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0.07
5-phospho-D-ribonamide
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.09 - 0.43
5-phospho-D-ribonohydroxamic acid
1.9
N-(5-phospho-D-ribonoyl)-hydrazine
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pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.18
N-(5-phospho-D-ribonoyl)-methylamine
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.09
5-phospho-D-ribonohydroxamic acid
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.43
5-phospho-D-ribonohydroxamic acid
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pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
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0.2 - 1.33
5-phospho-D-ribonamide
1.31
5-phospho-D-ribonate
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.17 - 0.62
5-phospho-D-ribonohydroxamic acid
1.6 - 2
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
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N-(5-phospho-D-ribonoyl)-glycine
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.35 - 0.36
N-(5-phospho-D-ribonoyl)-methylamine
0.2
5-phospho-D-ribonamide
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
1.33
5-phospho-D-ribonamide
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.17
5-phospho-D-ribonohydroxamic acid
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.62
5-phospho-D-ribonohydroxamic acid
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
1.6
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
2
N-(5-phospho-D-ribonoyl)-gamma-aminobutanoate
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.35
N-(5-phospho-D-ribonoyl)-methylamine
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.36
N-(5-phospho-D-ribonoyl)-methylamine
Escherichia coli
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pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
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Uniprot
brenda
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metabolism
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ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
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32000 - 34000
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ribosephosphate isomerase B, gel filtration
45000
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ribosephosphate isomerase A, gel filtration
50000
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dynamic light scattering
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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
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hanging drop vapor diffusion method, structure of a complex with arabinose 5-phosphate at 1.25 A resolution
hanging drop vapor diffusion method, enzyme form RpiA
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45
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30 min, ribosephosphate isomerase A retains 90% of its activity, ribosephosphate isomerase B retains 60% of its activity
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ribosephosphate isomerase B: half-life 2.2 min, independent of enzyme and protein concentration
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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
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overexpression as a His-tagged Se-Met-labeled protein
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Essenberg, 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 roles
Eur. J. Biochem.
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323-332
1975
Escherichia coli
brenda
MacElroy, R.D.; Middaugh, C.R.
Bacterial ribosephosphate isomerase
Methods Enzymol.
89
571-579
1982
[Bacillus] caldolyticus, Chromatium sp., Escherichia coli, Rhodospirillum rubrum, Halothiobacillus neapolitanus, Thiobacillus thioparus, Chromatium sp. D
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Rangarajan, E.S.; Sivaraman, J.; Matte, A.; Cygler, M.
Crystal structure of D-ribose-5-phosphate isomerase (RpiA) from Escherichia coli
Proteins
48
737-740
2002
Escherichia coli
brenda
Zhang, 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 cycle
Structure
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31-42
2003
Escherichia coli (P0A7Z0), Escherichia coli
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Roos, A.K.; Mariano, S.; Kowalinski, E.; Salmon, L.; Mowbray, S.L.
D-ribose-5-phosphate isomerase B from Escherichia coli is also a functional D-allose-6-phosphate isomerase, while the Mycobacterium tuberculosis enzyme is not
J. Mol. Biol.
382
667-679
2008
Escherichia coli, Mycobacterium tuberculosis (P9WKD7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKD7)
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Mariano, S.; Roos, A.K.; Mowbray, S.L.; Salmon, L.
Competitive inhibitors of type B ribose 5-phosphate isomerases: design, synthesis and kinetic evaluation of new D-allose and D-allulose 6-phosphate derivatives
Carbohydr. Res.
344
869-880
2009
Escherichia coli, Mycobacterium tuberculosis (P9WKD7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WKD7)
brenda