5.3.1.5: xylose isomerase
This is an abbreviated version!
For detailed information about xylose isomerase, go to the full flat file.
Word Map on EC 5.3.1.5
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5.3.1.5
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isomerization
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biomass
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d-glucose
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xylitol
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xylulokinase
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pentose
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lignocellulosic
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isomerases
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syrup
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corn
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gi
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d-fructose
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rubiginosus
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bioethanol
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piromyces
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arthrobacter
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l-arabinose
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synthesis
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actinoplanes
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high-fructose
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xylose-fermenting
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transaldolase
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saccharification
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thermoanaerobacter
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co-fermentation
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hemicellulosic
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thermoanaerobacterium
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neapolitana
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stipitis
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energy production
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orpinomyces
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thermosulfurogenes
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xylose-utilizing
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diauxic
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food industry
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nutrition
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biotechnology
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degradation
- 5.3.1.5
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isomerization
- biomass
- d-glucose
- xylitol
- xylulokinase
- pentose
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lignocellulosic
- isomerases
- syrup
- corn
- gi
- d-fructose
- rubiginosus
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bioethanol
- piromyces
- arthrobacter
- l-arabinose
- synthesis
- actinoplanes
-
high-fructose
-
xylose-fermenting
- transaldolase
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saccharification
- thermoanaerobacter
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co-fermentation
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hemicellulosic
- thermoanaerobacterium
- neapolitana
- stipitis
- energy production
- orpinomyces
- thermosulfurogenes
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xylose-utilizing
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diauxic
- food industry
- nutrition
- biotechnology
- degradation
Reaction
Synonyms
D-XI, D-xylose aldose-ketose-isomerase, D-xylose isomerase, D-Xylose ketoisomerase, D-xylose ketol isomerase, D-xylose ketol-isomerase, D-xylose: ketol-isomerase, D-xylulose keto-isomerase, glucose isomerase, glucose/xylose isomerase, GXI, Isomerase, xylose, Maxazyme, Optisweet, SDXyI, Spezyme, Sweetase, Sweetzyme, Sweetzyme Q, Swetase, T80 xylose isomerase, TcaXI, TNXI, TthXI, XI, XYLA, XylC, xylose (glucose) isomerase, xylose isomerase
ECTree
5.3.1.5 xylose isomeraseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 5.3.1.5 - xylose isomerase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
109
in the presence of Mg2+ plus Co2+, the enzyme shows a biphasic inactivation time course and two melting transitions at 99°C and 109°C
50
50 - 70
the enzyme is stable up to 50°C for 20 min. However, only 34% of the maximal activity is observed after preincubation at 60°C for 20 min, and no activity is observed after preincubation at 70°C for 20 min
53
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half life in presence of Co2+: 7 days, half-life in presence of Mg2+: 9 days, in presence of Mn2+ the enzyme activity remains constant for at least 10 days
60
65
70
70 - 80
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pH 7.8, 2 h, after following 2 h incubation at 80°C 37.6% loss of activity, 70-75% loss of activity at 80°C
75
80
85
90
97 - 112
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chitin-binding domain-D-xylose isomerase fusion protein (CBD-TNXI) bound to chitin has a half-life approximately 3times longer than the soluble wild type xylose isomerase (19.9 h vs. 6.8 h, respectively). The unbound soluble CBD-TNXI has a significantly longer half-life (56.5 h) than the immobilized enzyme. TNXI-apo enzyme melts at 97.5°C, while transitions at 100°C and 112°C are observed in the presence of Co2+ (0.5 mM) and Mn2+ (5.0 mM). The apo version of the immobilized enzyme melts at 104°C, with transitions at 87°C and 110°C for the halo enzyme
99
in the presence of Mg2+ plus Co2+, the enzyme shows a biphasic inactivation time course and two melting transitions at 99°C and 109°C
additional information
65
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mutant Q256D remains fully active for 60 min at 65°C, whereas the activity is rapidly lost at 80°C
70
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in the presence of CO2+, cell-free xylose isomerase retains 100% activity without loss of activity for 7 days
70
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half-life in absence of divalent cations: 4 d. In presence of Mn2+ or Co2+ stable for at least 1 month
80
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10 min, 80% loss of activity in absence of metal ions, 50% loss of activity in presence of 1 mM Mg2+, no loss of activity in presence of 1 mM Co2+
85
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in the presence of CO2+, cell-free xylose isomerase retains 50% residual activity for 13.5 h
90
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the melting temperature of the native enzyme isoform T90 is at 90°C
90
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after 1 h incubation the recombinant and the wild-type enzymes retain 25 and 34% of their activity, respectively
90
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in the presence of CO2+, cell-free xylose isomerase retains 50% residual activity for 126 min
additional information
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Tm: 50.3°C (apoenzyme), 53.3°C (in the presence of 5 microM Mg2+), 73.4°C (in the presence of 5 microM Co2+), 73.6°C (in the presence of 5 microM Mn2+)
additional information
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Tm: 50.8°C (apoenzyme), 56.2°C (in the presence of 5 microM Mg2+), 56.2°C (in the presence of 5 microM Co2+), 57.3°C (in the presence of 5 microM Mn2+)
additional information
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Co2+ is superior as protector against thermal inactivation at 80°C
additional information
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Mn2+ and Co2+ increase thermal stability
additional information
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Tm: 64.1°C (apoenzyme), 83.0°C (in the presence of 5 microM Mg2+), 86.0°C (in the presence of 5 microM Co2+), 86.1°C (in the presence of 5 microM Mn2+)
additional information
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Tm: 96.4°C (apoenzyme), 97.6°C (in the presence of 5 microM Mg2+), 97.5°C (in the presence of 5 microM Co2+), 96.9°C (in the presence of 5 microM Mn2+), 100.4°C (in the presence of 5 mM Mg2+), 100.0°C (in the presence of 5 mM Co2+), 100.5°C (in the presence of 5 mM Mn2+), 100.9°C (in the presence of 5 mM Ni2+), 100.5°C (in the presence of 5 mM Ca2+), half-lives: 83.2 min in the presence of 2 mM Mn2+ at 99°C, 6.9 min in the presence of 2 mM Mn2+ at 102°C, 4.2 min in the presence of 2 mM Mn2+ at 104°C, 2.3 min in the presence of 2 mM Mn2+ at 106°C, 59.5 min in the presence of 2 mM Co2+ at 96°C, 14 min in the presence of 2 mM Co2+ at 99°C, 5.8 min in the presence of 2 mM Co2+ at 102°C, 2.9 min in the presence of 2 mM Co2+ at 104°C, 12 min in the presence of 2 mM Mg2+ at 92°C, 2.3 min in the presence of 2 mM Mg2+ at 96°C, 1.9 min in the presence of 2 mM Mg2+ at 99°C, 1.3 min in the presence of 2 mM Mg2+ at 102°C, 30 min in the absence of metal ions at 87°C, 11.3 min in the absence of metal ions at 90°C, 7.5 min in the presence of 5 mM Mg2+ and 0.5 mM Co2+ at 100°C, 3.0 min in the presence of 0.5 mM Co2+ at 100°C
additional information
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stability is also strongly influenced by the addition of divalent cations. The addition of Mn2+ gives the highest thermostability, Mg2+ has a smaller stabilizing effect, while other metals have no effect
additional information
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Mn2+, Co2+ and Ni2+ strongly protect the enzyme from heat denaturation
