Information on EC 5.3.1.15 - D-lyxose ketol-isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.3.1.15
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RECOMMENDED NAME
GeneOntology No.
D-lyxose ketol-isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-Lyxose = D-xylulose
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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isomerization
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pentose and glucuronate interconversions
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SYSTEMATIC NAME
IUBMB Comments
D-lyxose aldose-ketose-isomerase
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CAS REGISTRY NUMBER
COMMENTARY hide
37318-42-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
strain RI-39
SWISSPROT
Manually annotated by BRENDA team
strain RI-39
SWISSPROT
Manually annotated by BRENDA team
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-fructose
D-mannose
show the reaction diagram
D-Lyxose
D-Xylulose
show the reaction diagram
D-Mannose
?
show the reaction diagram
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-
-
?
D-Mannose
D-Fructose
show the reaction diagram
D-Ribose
D-Ribulose
show the reaction diagram
D-ribulose
D-ribose
show the reaction diagram
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-
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r
D-tagatose
D-talose
show the reaction diagram
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-
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r
D-talose
D-tagatose
show the reaction diagram
D-xylulose
D-lyxose
show the reaction diagram
L-allose
L-psicose
show the reaction diagram
L-gulose
L-sorbose
show the reaction diagram
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-
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r
L-Lyxose
L-Xylulose
show the reaction diagram
L-Mannose
L-Fructose
show the reaction diagram
L-ribose
L-ribulose
show the reaction diagram
L-ribulose
L-ribose
show the reaction diagram
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-
-
r
L-talose
L-tagatose
show the reaction diagram
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r
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-Lyxose
D-Xylulose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
metal ion required, Fe2+ activates
Fe3+
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metal ion required, Fe3+ activates
Ni2+
activating at 1 mM, D-xylose as substrate
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co2+
-
about 15% residual activity at 1 mM
additional information
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not affected by Ca2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.4 - 54
D-fructose
3.6 - 47
D-Lyxose
1 - 34
D-mannose
3.83 - 38
D-xylulose
65
L-ribulose
at pH 7.5 and 75C
10
mannose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2010 - 4297
D-fructose
59.5 - 31340
D-Lyxose
2.97 - 16170
D-mannose
69.3 - 34960
D-xylulose
1.7
L-ribulose
Dictyoglomus turgidum
B8DZQ9
at pH 7.5 and 75C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
37 - 222
D-fructose
117
1.52 - 2333
D-Lyxose
1589
0.23 - 502
D-mannose
216
15.3 - 9560
D-xylulose
715
0.03
L-ribulose
Dictyoglomus turgidum
B8DZQ9
at pH 7.5 and 75C
1621
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
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using L-tagatose as substrate, at pH 7.5 and 45C
0.003
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using L-mannose as substrate, at pH 7.5 and 45C
0.005
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using D-psicose as substrate, at pH 7.5 and 45C
0.007
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using L-lyxose as substrate, at pH 7.5 and 45C
0.008
after 38fold purification, using L-allose as substrate, at pH 7.5 and 75C
0.01
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using L-psicose as substrate, at pH 7.5 and 45C
0.011
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using L-talose as substrate, at pH 7.5 and 45C
0.013
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using D-allose as substrate, at pH 7.5 and 45C
0.014
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using D-ribose as substrate, at pH 7.5 and 45C
0.015
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using D-tagatose as substrate, at pH 7.5 and 45C
0.017
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using L-fructose as substrate, at pH 7.5 and 45C
0.02
using L-sorbose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
0.045
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using D-tagatose as substrate, at pH 7.5 and 45C
0.077
after 38fold purification, using D-ribulose as substrate, at pH 7.5 and 75C
0.094
after 38fold purification, using D-fructose as substrate, at pH 7.5 and 75C
0.096
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using D-ribulose as substrate, at pH 7.5 and 45C
0.106
after 38fold purification, using D-talose as substrate, at pH 7.5 and 75C
0.119
after 38fold purification, using L-ribose as substrate, at pH 7.5 and 75C
0.14
using L-ribose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
0.18
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using L-xylulose as substrate, at pH 7.5 and 45C
0.19
using D-talose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
0.219
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using L-ribose as substrate, at pH 7.5 and 45C
0.28
using D-tagatose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
0.292
after 38fold purification, using L-ribulose as substrate, at pH 7.5 and 75C
0.4
using L-ribulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
0.403
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using D-fructose as substrate, at pH 7.5 and 45C
0.5
crude extract, using D-lyxose as substrate, at pH 7.5 and 75C
0.523
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using D-mannose as substrate, at pH 7.5 and 45C
0.872
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using L-ribulose as substrate, at pH 7.5 and 45C
1.05
using L-gulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
1.41
using D-fructose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
1.668
after 38fold purification, using D-mannose as substrate, at pH 7.5 and 75C
4.2
crude extract, in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40C
5.42
using D-mannose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
8.4
of the native enzyme after purification, at 70C, with L-ribose as substrate
10
using D-lyxose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
18.8
after 38fold purification, using D-lyxose as substrate, at pH 7.5 and 75C
22.33
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using D-lyxose as substrate, at pH 7.5 and 45C
24
after 10fold purification, in 50 mM Tris-HCl, 1 mM Mn2+, pH 8.0, at 40C
24.04
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using D-xylulose as substrate, at pH 7.5 and 45C
26.2
using D-xylulose as substrate, at pH 7.5 and 40C, in the presence of 1 mM Mn2+
33.1
after 38fold purification, using D-xylulose as substrate, at pH 7.5 and 75C
50.2
of the recombinant enzyme after purification, at 70C, with L-ribose as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
wild-type and recombinant enzymes at 1 mM Mn2+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9 - 7
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pH 4.0: about 50% of maximal activity, pH 7.0: maximal activity
7 - 8.5
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at pH 7.0 and 8.5, the activities are approximately 60% of the maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
wild-type and recombinant enzymes at 1 mM Mn2+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 65
the enzyme activity increases as the temperature increases, showing higher activity at 40C to 45C, and is completely lost at temperatures greater than 65C
40 - 50
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at 40C and 50C, the activities are approximately 60% of the maximum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
wild-type and recombinant enzymes
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19500
x * 19500, estimated from SDS-PAGE
22160
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2 * 22160, calculated from amino acid sequence
26756
2 * 26756, calculated from amino acid sequence
27000
2 * 27000, SDS-PAGE
40000
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gel filtration, density gradient centrifugation
42000
gel filtration
54000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 19500, estimated from SDS-PAGE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M sodium cacodylate pH 6.5, 0.2 M NaCl, 2.0 M ammonium sulfate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
60 - 85
at pH 7.5 and 75C and in the presence of 0.5 mM Co2+ the enzyme has a half-life of 108 min. After incubation at 75C for 5 min, more than 97% of the enzyme activity remains. The half-lives of the enzyme at 60, 65, 70, 75, 80 and 85C are 547, 247, 171, 108, 49, and 16 min, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
approximately 10% of the total activity is lost during theimmobilization process on Duolite A568 beads. The
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conversion yields using Duolite A568 and Chitopearl BCW2510 beads are 25 and 16%, respectively. Those using Amberlite IRA-120 S and IRA-400 ZLB beads are 7 and 9%, respectively. Immobilization on XAD7, XAD8, and Sephadex LH-60-120 results in no conversion
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
at -20C for several months
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-Trap column chromatography
His-Trap column chromatography, gel filtration
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HiTrap column chromatography, Superdex S200 gel filtration
metal ion affinity column chromatography
Ni-NTA agarose bead column chromatography and ultrafiltration
of the native protein to homogeneity by DEAE-Sephacel ion-exchange chromatography, followed by RESOURCE PHE hydrophobic chromatography, of the recombinant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli B834 (DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli ER2566 cells
overexpression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry