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
-
bioethanol
- piromyces
- arthrobacter
- l-arabinose
- synthesis
- actinoplanes
-
high-fructose
-
xylose-fermenting
- transaldolase
-
saccharification
- thermoanaerobacter
-
co-fermentation
-
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
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Metals Ions
Metals Ions on EC 5.3.1.5 - xylose isomerase
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Co2+
Fe2+
Mg2+
Mn2+
Zn2+
additional information
Co2+
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XI is substantially structurally stabilized in the presence of CO2+
Co2+
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when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Co2+
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with D-xylose as substrate, the activity is increased by the addition of 1 mM Co2+ (1.9fold). A mixture of 0.5 mM Co2+ and 0.5 mM Mn2+ increases the enzyme activity 3.2fold. Glucose isomerase activity is maximally enhanced by the addition of 5 mM Co2+
Co2+
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two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization. Co2+ is the most efficient cofactor for D-glucose isomerization
Co2+
D-xylose and D-glucose isomerase activities of XylA are enhanced by Co2+. When 1 mM Co2+ and 10 mM Mg2+ are added together, the activity of XylA is increased by about 10% compared to 1 mM Co2+ only
Co2+
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XI is substantially structurally stabilized in the presence of CO2+
Co2+
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most effectively activates D-glucose isomerization and D-ribose isomerization
Mg2+
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XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
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when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Mg2+
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XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
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glucose isomerase activity is maximally enhanced by the addition of 5 mM Mg2+
Mg2+
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two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization
Mg2+
D-xylose and D-glucose isomerase activities of XylA are enhanced by Mg2+
Mg2+
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XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
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activates D-glucose isomerization, D-xylose isomerization and D-ribose isomerization
Mg2+
recombinant XylA requires the addition of Mg2+ for optimum activity (100%)
Mg2+
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activates D-glucose isomerization, D-xylose isomerization and D-ribose isomerization
Mn2+
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XI is substantially structurally stabilized in the presence of Mn2+
Mn2+
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when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Mn2+
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with D-xylose as substrate, the activity is increased by the addition of 1 mM Mn2+ (2.9fold). A mixture of 0.5 mM Co2+ and 0.5 mM Mn2+ increases the enzyme activity 3.2fold. Glucose isomerase activity is maximally enhanced by the addition of 5 mM Mn2+
Mn2+
essential for activity, there are two manganese atoms visible in the atomic resolution study
Mn2+
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two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization
Mn2+
D-xylose isomerase activity of XylA is enhanced by Mn2+
Mn2+
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XI is substantially structurally stabilized in the presence of Mn2+
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two metal sites: metal site 1 is four-coordinated and tetrahedral in the absence of substrate and is six-coordinated and octahedral in its presence, the O2 and O4 atoms of the linear inhibitors and substrate bind to the metal 1. Metal site 2 is octahedral in all cases, its position changes by 0.7 A when it binds O1 of the substrate and by more than 1 A when it also binds O2
additional information
no activity with Fe2+, Fe3+, Ni2+, and Cu2+
additional information
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no activity with Fe2+, Fe3+, Ni2+, and Cu2+
additional information
addition of Ca2+, Zn2+, Fe2+, or Cu2+ is not effective