Information on EC 5.3.1.6 - ribose-5-phosphate isomerase

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

EC NUMBER
COMMENTARY hide
5.3.1.6
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RECOMMENDED NAME
GeneOntology No.
ribose-5-phosphate isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Ribose 5-phosphate = D-ribulose 5-phosphate
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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-
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isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Bifidobacterium shunt
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Calvin-Benson-Bassham cycle
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formaldehyde assimilation II (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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Rubisco shunt
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pentose phosphate pathway
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photosynthesis
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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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Metabolic pathways
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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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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
animal
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Automatic Mining of ENzyme DAta
gene RPI2, At2g01290
UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Chromatium sp.
strain D
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Manually annotated by BRENDA team
Chromatium sp. D
strain D
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
strain K12, two enzyme forms: constitutive isomerase A and inducible isomerase B
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
Peptoclostridium difficile
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Manually annotated by BRENDA team
Peptoclostridium difficile ATCC BAA-1382D-5
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
plant
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
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UniProt
Manually annotated by BRENDA team
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Automatic Mining of ENzyme DAta
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Automatic Mining of ENzyme DAta
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
deficiency in a cytosolic ribose-5-phosphate isomerase causes chloroplast dysfunction, late flowering and premature cell death in Arabidopsis thaliana
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Allose
D-Psicose
show the reaction diagram
D-allose 6-phosphate
D-allulose 6-phosphate
show the reaction diagram
D-Glucose 6-phosphate
?
show the reaction diagram
-
-
-
-
?
D-gulose
D-sorbose
show the reaction diagram
D-psicose
D-allose
show the reaction diagram
D-Ribose
D-Ribulose
show the reaction diagram
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-ribose-5-phosphate
D-ribulose-5-phosphate
show the reaction diagram
D-ribulose
D-ribose
show the reaction diagram
D-ribulose 5-diphosphate
D-ribose 5-diphosphate
show the reaction diagram
-
-
-
r
D-ribulose 5-phosphate
D-ribose 5-phosphate
show the reaction diagram
D-sorbose
D-gulose
show the reaction diagram
D-talose
D-tagatose
show the reaction diagram
L-allose
L-psicose
show the reaction diagram
L-fructose
L-mannose
show the reaction diagram
L-Lyxose
L-Xylulose
show the reaction diagram
L-Mannose
L-Fructose
show the reaction diagram
-
-
-
-
r
L-ribose
L-ribulose
show the reaction diagram
L-tagatose
L-talose
show the reaction diagram
L-talose
L-tagatose
show the reaction diagram
L-xylulose
L-lyxose
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-Allose
D-Psicose
show the reaction diagram
-
-
-
-
r
D-Ribose
D-Ribulose
show the reaction diagram
-
-
-
-
r
D-ribose 5-phosphate
D-ribulose 5-phosphate
show the reaction diagram
D-ribose-5-phosphate
D-ribulose-5-phosphate
show the reaction diagram
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
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D-talose
D-tagatose
show the reaction diagram
-
-
-
-
r
L-allose
L-psicose
show the reaction diagram
-
-
-
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r
L-ribose
L-ribulose
show the reaction diagram
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-
-
-
r
L-talose
L-tagatose
show the reaction diagram
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preferred substrate
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r
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates
Mg2+
-
activates
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-phosphoglycerate
-
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4-deoxy-4-phosphonomethyl-D-erythronate
-
stable and potent competitive inhibitor
4-phospho-D-erythronamide
-
competitive
4-phospho-D-erythronate
4-phospho-D-erythronhydrazide
-
4-phospho-D-erythronohydrazide
-
competitive
4-phospho-D-erythronohydroxamic acid
competitive
4-phosphoerythronate
-
strong competitive
4-phosphono-D-erythronate
-
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4-phosphono-D-erythronohydroxamate
-
-
4-phosphono-D-erythronohydroxamic acid
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competitive
5'-AMP
5-deoxy-5-phospho-D-ribonohydroxamate
-
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5-deoxy-5-phospho-D-ribonohydroxamic acid
5-phospho-D-ribonamide
5-phospho-D-ribonate
5-phospho-D-ribonohydroxamic acid
6-phosphogluconate
arabinose 5-phosphate
citrate
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10 mM
D-5-Phosphoribonic acid
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-
D-Allose 6-phosphate
D-allulose 6-phosphate
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D-arabinose 5-phosphate
erythrose 4-phosphate
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competitive
fructose 6-phosphate
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-
glyceraldehyde 3-phosphate
-
competitive
iodoacetamide
iodoacetate
iodoacetic acid
suicide inhibitor
Mn2+
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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
Organic mercurials
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Phenylmercuriacetate
phosphate
ribulose diphosphate
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1.0 mM, strong
sedoheptulose bisphosphate
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competitive
Sodium mersalyl
Sodium salt of 2-(ethylmercurimercapto)-benzoxazole-5-carboxylic acid
sulfhydryl reagents
Xylulose 5-phosphate
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-
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
106 - 460
D-Allose
43 - 78
D-psicose
44 - 270
D-ribose
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 65C
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 65C
98
L-allose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
173
L-ribose
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in 50 mM Tris-HCl buffer (pH 7.5), at 65C
319
L-ribulose
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
125
L-tagatose
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in 50 mM Tris-HCl buffer (pH 7.5), at 65C
5 - 37
L-talose
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
200 - 2682
D-Allose
0.116 - 2743
D-psicose
160 - 11880
D-ribose
1 - 97
D-Ribose 5-diphosphate
8.3 - 52000
D-ribose 5-phosphate
0.0421 - 3440
D-ribose-5-phosphate
9193
D-ribulose
Ruminiclostridium thermocellum
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in 50 mM Tris-HCl buffer (pH 7.5), at 65C
4.7 - 10.7
D-ribulose 5-diphosphate
2 - 39530
D-ribulose 5-phosphate
119
D-talose
Ruminiclostridium thermocellum
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in 50 mM Tris-HCl buffer (pH 7.5), at 65C
1506
L-allose
Ruminiclostridium thermocellum
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
322
L-ribose
Ruminiclostridium thermocellum
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
17
L-ribulose
Ruminiclostridium thermocellum
-
in 50 mM Tris-HCl buffer (pH 7.5), at 65C
1822
L-tagatose
Ruminiclostridium thermocellum
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in 50 mM Tris-HCl buffer (pH 7.5), at 65C
140 - 13420
L-talose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
D-Allose
Peptoclostridium difficile
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pH 7.5, 40C
945
0.0018 - 64
D-psicose
2077
0.6
D-ribose
Peptoclostridium difficile
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pH 7.5, 40C
292
500 - 3029
D-ribose 5-phosphate
183
2589
D-ribulose 5-phosphate
Ruminiclostridium thermocellum
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pH 7.5, 65C, recombinant enzyme
443
0.3
L-talose
Peptoclostridium difficile
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pH 7.5, 40C
6883
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.074
4-deoxy-4-phosphonomethyl-D-erythronate
-
25C
2.5
4-phospho-D-erythronamide
-
25C, pH 7.5
1.7
4-phospho-D-erythronate
-
-
1.8
4-phospho-D-erythronohydrazide
-
25C, pH 7.5
1.2
4-phospho-D-erythronohydroxamic acid
pH 8.4, 25C
0.028
4-phosphono-D-erythronate
-
25C, pH 7.5
0.057
4-phosphono-D-erythronohydroxamate
-
-
0.029
4-phosphono-D-erythronohydroxamic acid
-
25C, 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, 37C, RpiB, substrate is D-ribose 5-phosphate
0.09 - 0.43
5-phospho-D-ribonohydroxamic acid
0.7
arabinose 5-phosphate
-
pH 8.0, 25C
15
D-Allose 6-phosphate
in 50 mM Tris-HCl (pH 7.6), 150 mM NaCl and 5 mM MESNA, at 30C
0.89
D-arabinose 5-phosphate
-
50C, pH 7.5
0.34
N-(5-phospho-D-ribonoyl)-glycine
pH 7.5, 37C, RpiB, substrate is D-ribose 5-phosphate
1.9
N-(5-phospho-D-ribonoyl)-hydrazine
-
pH 7.5, 37C, RpiB, substrate is D-allose 5-phosphate
0.11 - 0.18
N-(5-phospho-D-ribonoyl)-methylamine
7.9 - 130
phosphate
4
Xylulose 5-phosphate
-
pH 8.0, 25C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
4-phospho-D-erythronate
Trypanosoma cruzi
Q4CQE2
pH 8.4, 25C
0.7
4-phospho-D-erythronohydroxamic acid
Trypanosoma cruzi
Q4CQE2
pH 8.4, 25C
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 37C
6.3
D-allulose 6-phosphate
Mycobacterium tuberculosis
-
in 50 mM Tris-HCl, pH 7.5, at 37C
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, 37C, 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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0005
-
using D-sorbose as substrate, at 35C and pH 7.5
0.0011
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using L-fructose as substrate, at 35C and pH 7.5
0.0013
-
using L-tagatose as substrate, at 35C and pH 7.5
0.0019
-
using D-allose as substrate, at 35C and pH 7.5
0.0021
-
using D-psicose as substrate, at 35C and pH 7.5
0.0025
-
using D-ribose as substrate, at 35C and pH 7.5
0.0053
-
using D-gulose as substrate, at 35C and pH 7.5
0.0096
-
using L-lyxose as substrate, at 35C and pH 7.5
0.019
-
using L-talose as substrate, at 35C and pH 7.5
0.027
-
using L-lyxose as substrate, at 35C and pH 7.5
0.048
-
using D-ribulose as substrate, at 35C and pH 7.5
0.058
-
using D-glucose 6-phosphate as substrate, at 35C and pH 7.5
0.121
-
using L-xylulose as substrate, at 35C and pH 7.5
0.2
-
after 9.1fold purification, at pH 8.0 and 75C
0.21
-
purified enzyme, using D-tagatose as substrate, at 65C and pH 7.5
0.259
-
mutant enzyme H98A, using D-psicose as substrate, pH 7.5, 80C
0.299
-
mutant enzyme H133A, using D-psicose as substrate, pH 7.5, 80C; mutant enzyme R136A, using D-psicose as substrate, pH 7.5, 80C
0.388
-
using D-ribose 5-phosphate as substrate, at 35C and pH 7.5
0.53
-
purified enzyme, using L-allose as substrate, at 65C and pH 7.5
0.698
-
mutant enzyme N99A, using D-psicose as substrate, pH 7.5, 80C
0.917
-
mutant enzyme T67A, using D-psicose as substrate, pH 7.5, 80C
1
Peptoclostridium difficile
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substrate D-sorbose, pH 7.5, 40C
1.256
-
mutant enzyme H9A, using D-psicose as substrate, pH 7.5, 80C
1.815
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mutant enzyme T135A, using D-psicose as substrate, pH 7.5, 80C
1.994
-
wild type enzyme, using D-psicose as substrate, pH 7.5, 80C
2.313
-
mutant enzyme R132A, using D-psicose as substrate, pH 7.5, 80C
3
Peptoclostridium difficile
-
substrate D-psicose, pH 7.5, 40C
7
Peptoclostridium difficile
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substrate L-lyxose, pH 7.5, 40C
9
Peptoclostridium difficile
-
substrate L-fructose, pH 7.5, 40C
12
-
purified enzyme, using L-psicose as substrate, at 65C and pH 7.5
14
Peptoclostridium difficile
-
substrate D-ribulose, pH 7.5, 40C
15
Peptoclostridium difficile
-
substrate D-allose, pH 7.5, 40C
28
Peptoclostridium difficile
-
substrate L-talose, pH 7.5, 40C
45
Peptoclostridium difficile
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substrate L-talose, pH 7.5, 40C
50
-
purified enzyme, using D-talose as substrate, at 65C and pH 7.5
53
Peptoclostridium difficile
-
substrate D-ribose, pH 7.5, 40C
57
Peptoclostridium difficile
-
substrate L-xylulose, pH 7.5, 40C
120
Peptoclostridium difficile
-
substrate D-gulose, pH 7.5, 40C
187
-
cell lysate, at 50C and pH 7.0
272
-
purified enzyme, using L-ribose as substrate, at 65C and pH 7.5
290
-
after purification, at 50C and pH 7.0
600
-
purified enzyme, using L-allose as substrate, at 65C and pH 7.5
720
-
purified enzyme, using L-ribulose as substrate, at 65C and pH 7.5
1037
-
purified enzyme, using D-psicose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-psicose
1352
-
purified enzyme, using D-allose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-allose
5374
-
purified enzyme, using D-ribulose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribulose
5800
-
purified enzyme, using D-ribose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribose
7363
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purified enzyme, using L-talose as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate L-talose
19680
-
purified enzyme, using D-ribulose 5-phosphate as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribulose 5-phosphate
25690
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purified enzyme, using D-ribose 5-phosphate as substrate, at 65C and pH 7.5; purified recombinant enzyme, substrate D-ribose 5-phosphate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
-
-
7.7 - 7.8
-
D-ribulose 5-phosphate, D-ribose 5-phosphate
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9.9
-
pH 6: about 40% of maximal activity, pH 9.9: about 65% of maximal activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
-
30C: about 50% of maximal activity, 80C: about 45% of maximal activity
40 - 99
-
enzyme activity increases significantly when the temperature increases until 80C. The optimum temperature is 80C. The activity at 30C is 25% of that at 80C. The enzyme activity decreases after 80C. It is still highly active when the temperature reaches 99C, 90% activity of that of 80C. This enzyme shows relatively high activity (above 50% of its maximum activity) over a large temperature range of 40-99C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.77
isoelectric focusing
5.1
-
isoelectric focusing
6.4
Peptoclostridium difficile
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
one electrophorectic form
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
highest expression
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
-
one electrophorectic form
Manually annotated by BRENDA team
-
one electrophorectic form
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
metacyclic and in cell-culture
Manually annotated by BRENDA team
-
two electrophorectic forms
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Anaplasma phagocytophilum (strain HZ)
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
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)
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Francisella tularensis subsp. tularensis (strain WY96-3418)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Lactobacillus salivarius (strain UCC118)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Toxoplasma gondii (strain ATCC 50611 / Me49)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Trypanosoma cruzi (strain CL Brener)
Vibrio vulnificus (strain YJ016)
Vibrio vulnificus (strain YJ016)
Vibrio vulnificus (strain YJ016)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000 - 35000
-
gel filtration
32000 - 34000
-
ribosephosphate isomerase B, gel filtration
32000
-
dynamic light scattering
35000
-
about, native PAGE, recombinant enzyme
35200
-
gel filtration
39600
gel filtration
49000
-
gel filtration
50000
-
dynamic light scattering
53000
-
high-speed equilibrium centrifugation
54000
Chromatium sp.
-
-
96000
-
gel filtration
98000
gel filtration
105000
-
gel filtration
183000
-
gel filtration
228000
-
analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
homotetramer
-
4 * 23724, calculated from amino acid sequence; 4 * 24000, SDS-PAGE
tetramer
trimer
-
1 * 75000, alpha, + 2 * 54000, beta, SDS-PAGE
additional information
-
homology modeling of RpiB, substrate binding structure, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
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, 18C. The mixture is covered with 0.015 ml silicone and paraffin oil, X-ray diffraction structure determination and analysis at 1.78 A resolution, molecular replacement and 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
-
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 co