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Information on EC 5.3.1.6 - ribose-5-phosphate isomerase and Organism(s) Escherichia coli and UniProt Accession P0A7Z0

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IUBMB Comments
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A7Z0
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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-
-
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D-xylose ketol-isomerase
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-
-
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Isomerase, ribose phosphate
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-
-
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Phosphopentoisomerase
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-
-
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Phosphopentose isomerase
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-
-
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Phosphoriboisomerase
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-
-
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Ribose phosphate isomerase
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-
-
-
Ribose-5-P isomerase
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-
-
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Ribosephosphate isomerase A
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-
-
-
Ribosephosphate isomerase B
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-
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RPI
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-
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type B ribose 5-phosphate isomerase
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type B Rpi
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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-
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intramolecular oxidoreduction
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-ribose-5-phosphate aldose-ketose-isomerase
Also acts on D-ribose 5-diphosphate and D-ribose 5-triphosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-83-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-ribose 5-diphosphate
D-ribulose 5-diphosphate
show the reaction diagram
-
-
?
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
D-ribose 5-triphosphate
D-ribulose 5-triphosphate
show the reaction diagram
-
-
?
D-allose 6-phosphate
D-allulose 6-phosphate
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
the enzyme plays essential roles in carbohydrate anabolism and catabolism
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
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
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arabinose 5-phosphate
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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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6-phosphogluconate
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fructose 6-phosphate
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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
-
-
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.1
D-ribose 5-phosphate
-
0.83 - 4.4
D-ribose 5-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2100
D-ribose 5-phosphate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
-
pH 7.5, 37°C, RpiB, substrate is D-allose 5-phosphate
0.18
N-(5-phospho-D-ribonoyl)-methylamine
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 1.33
5-phospho-D-ribonamide
1.31
5-phospho-D-ribonate
Escherichia coli
-
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
9
N-(5-phospho-D-ribonoyl)-glycine
Escherichia coli
-
pH 7.5, 37°C, RpiB, substrate is D-ribose 5-phosphate
0.35 - 0.36
N-(5-phospho-D-ribonoyl)-methylamine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
ribose 5-phosphate isomerase is a key enzyme of the pentose phosphate pathway
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000 - 34000
-
ribosephosphate isomerase B, gel filtration
45000
-
ribosephosphate isomerase A, gel filtration
50000
-
dynamic light scattering
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
30 min, ribosephosphate isomerase A retains 90% of its activity, ribosephosphate isomerase B retains 60% of its activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression as a His-tagged Se-Met-labeled protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
55
323-332
1975
Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
11
31-42
2003
Escherichia coli (P0A7Z0), Escherichia coli
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team