Information on EC 5.3.1.B3 - L-ribulose isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.1.B3
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
L-ribulose isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-ribose = L-ribulose
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
SYSTEMATIC NAME
IUBMB Comments
L-ribose aldose-ketose isomerase
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CAS REGISTRY NUMBER
COMMENTARY hide
180615-70-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose
D-mannose
show the reaction diagram
-
-
-
r
D-Lyxose
D-Xylulose
show the reaction diagram
D-Mannose
D-Fructose
show the reaction diagram
D-tagatose
D-talose
show the reaction diagram
-
-
-
r
D-talose
D-tagatose
show the reaction diagram
D-xylulose
D-lyxose
show the reaction diagram
-
-
-
r
L-allose
L-psicose
show the reaction diagram
L-gulose
L-sorbose
show the reaction diagram
2.27% activity compared to L-ribose
-
-
r
L-psicose
L-allose
show the reaction diagram
-
-
-
r
L-ribose
L-ribulose
show the reaction diagram
L-ribulose
L-ribose
show the reaction diagram
L-sorbose
L-gulose
show the reaction diagram
-
-
-
r
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
L-ribose
L-ribulose
show the reaction diagram
L-ribulose
L-ribose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme is not dependent for metallic ions for its activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
51
D-fructose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
37.1
D-Lyxose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
51.1
D-mannose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
39.2
D-tagatose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
37.6
D-talose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
32.8
D-xylulose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
40.3
L-allose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
40.1
L-gulose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
54.8
L-psicose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
30.4
L-ribose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
15.4
L-ribulose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
40
L-sorbose
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17.5
D-fructose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
17.3
D-Lyxose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
2.5
D-mannose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
40.8
D-tagatose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
15.8
D-talose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
18.2
D-xylulose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
2.8
L-allose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
2.1
L-gulose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
2.2
L-psicose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
95.2
L-ribose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
108.8
L-ribulose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
0.38
L-sorbose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034
D-fructose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
117
0.47
D-Lyxose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
1589
0.048
D-mannose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
216
0.104
D-tagatose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
2197
0.42
D-talose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
2017
0.56
D-xylulose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
715
0.07
L-allose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
10165
0.054
L-gulose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
7666
0.04
L-psicose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
72365
3.13
L-ribose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
3127
7.05
L-ribulose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
1621
0.009
L-sorbose
Cellulomonas parahominis
L0N3Y0
in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
685
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.103
activity determined from the cell extracts of Escherichia coli UP1110 3 h after the onset of IPTG induction
0.183
activity determined from the cell extracts of Lactobacillus plantarum BPT232 1h after the induction with the peptide SPPIP
1.49
crude native enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
4.9
crude recombinant enzyme, in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
39.5
native enzyme after 27fold purification, in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
214
recombinant enzyme after 43.6fold purification, in 50 mM glycine-NaOH buffer (pH 9.0), at 40C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
process of L-ribose production
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
more than 60% activity between pH 6.0 and 11.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
activity assay
39
process of L-ribose production
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27435
x * 27435, calculated from amino acid sequence
28700
x * 28700, N-terminally His-tagged enzyme, SDS-PAGE
32000
x * 32000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.2 M NaCl, 30% (w/v) PEG 400, 0.1 M HEPES pH 7.5 or 18-23% (w/v) PEG 400, 0.1 M HEPES pH 7.5, 0.16-0.2 M NaCl with or without 10-20 mM hexamminecobalt(III) chloride
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
the enzyme is stable in a pH range of pH 7.0-10.0 at 4C for 24 h in any buffer
728006
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
the enzyme is stable up to 40C for 1 h
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q Sepharose column chromatography, Resource PHE column chromatographym and Resource Q column chromatography
HisTrap affinity column chromatography, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 cells
into the pTrcHis 2B expression vector for transformation of Escherichia coli cells, and into the pSIP401 expression vector for transformation of Lactobacillus plantarum cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
industry