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Information on EC 5.3.1.5 - xylose isomerase
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5.3.1.5 xylose isomeraseIUBMB Comments
Contains two divalent metal ions, preferably magnesium, located at different metal-binding sites within the active site. The enzyme catalyses the interconversion of aldose and ketose sugars with broad substrate specificity. The enzyme binds the closed form of its sugar substrate (in the case of xylose and glucose, only the alpha anomer ) and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism.
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Word Map
- 5.3.1.5
-
isomerization
- biomass
- d-glucose
- xylitol
- xylulokinase
- pentose
-
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
-
xylose-utilizing
-
diauxic
- food industry
- nutrition
- biotechnology
- degradation
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
xylose isomerase, glucose isomerase, d-xylose isomerase, spezyme, xylose (glucose) isomerase, glucose/xylose isomerase, tcaxi, sdxyi, tthxi, sweetzyme, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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/xylose isomerase
GXI
Isomerase, xylose
-
-
-
-
Maxazyme
Optisweet
SDXyI
Sweetzyme
Swetase
-
-
-
-
XI
XYLA
XylC
xylose (glucose) isomerase
xylose isomerase
D-xylose isomerase
-
-
-
-
D-Xylose ketoisomerase
-
-
-
-
SDXyI
Streptomyces diastaticus No. 7 M1033
-
-
-
XI
-
-
-
-
xylose isomerase
no activity in Hansenula polymorpha CBS4732s leu2-2
-
-
-
xylose isomerase
-
xylose isomerase exhibits two temperature stable isoforms having optimal activity at temperatures 70°C (T70) and 90°C (T90), respectively
xylose isomerase
Opuntia vulgaris
-
xylose isomerase exhibits two temperature stable isoforms having optimal activity at temperatures 70°C (T70) and 90°C (T90), respectively
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-xylopyranose = alpha-D-xylufuranose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-xylopyranose aldose-ketose-isomerase
Contains two divalent metal ions, preferably magnesium, located at different metal-binding sites within the active site. The enzyme catalyses the interconversion of aldose and ketose sugars with broad substrate specificity. The enzyme binds the closed form of its sugar substrate (in the case of xylose and glucose, only the alpha anomer [4]) and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism.
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CAS REGISTRY NUMBER
COMMENTARY
9023-82-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-ribose
?
-
no increased reaction rate observed for mutant F26W
-
-
?
D-Fructose
?
-
compulsory order of binding: 1. Co2+ binds first to site 2 and then to site 1, then the D-fructose binds at site 1. At normal concentrations Mg2+ binds at site 1, then D-fructose, and then Mg2+ at site 2. At very high Mg2+ concentrations, above 10 mM, the order is Mg2+ at site1, Mg2+ at site 2, then D-fructose
-
-
?
D-Glucose
D-Fructose
-
-
maximum conversion rate of 48% at 60°C
-
r
D-Glucose
D-Fructose
Limosilactobacillus reuteri DSM Z 17509
-
-
maximum conversion rate of 48% at 60°C
-
r
D-Glucose
D-Fructose
V185T mutation increases catalytic efficiency on glucose
-
-
?
D-Xylose
D-Xylulose
-
-
D-xylulose is an important intermediate in pentose metabolism
-
?
additional information
?
-
-
the recombinant enzyme catalyzes also the isomerization of D-glucose to D-fructose
-
-
?
additional information
?
-
-
important enzyme in degradation of xylans and metabolizing D-xylose via the pentose phosphate pathway
-
-
?
additional information
?
-
-
important enzyme in degradation of xylans and metabolizing D-xylose via the pentose phosphate pathway
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-Xylose
D-Xylulose
-
-
D-xylulose is an important intermediate in pentose metabolism
-
?
additional information
?
-
-
important enzyme in degradation of xylans and metabolizing D-xylose via the pentose phosphate pathway
-
-
?
additional information
?
-
-
important enzyme in degradation of xylans and metabolizing D-xylose via the pentose phosphate pathway
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe2+
Mg2+
Mn2+
Zn2+
additional information
Co2+
-
XI is substantially structurally stabilized in the presence of CO2+
Co2+
-
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+
-
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+
-
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+
-
XI is substantially structurally stabilized in the presence of CO2+
Co2+
-
most effectively activates D-glucose isomerization and D-ribose isomerization
Mg2+
-
XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
-
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+
-
XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
-
glucose isomerase activity is maximally enhanced by the addition of 5 mM Mg2+
Mg2+
-
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+
-
XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
-
activates D-glucose isomerization, D-xylose isomerization and D-ribose isomerization
Mg2+
recombinant XylA requires the addition of Mg2+ for optimum activity (100%)
Mg2+
-
activates D-glucose isomerization, D-xylose isomerization and D-ribose isomerization
Mn2+
-
XI is substantially structurally stabilized in the presence of Mn2+
Mn2+
-
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+
-
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+
-
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+
-
XI is substantially structurally stabilized in the presence of Mn2+
additional information
-
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
-
no activity with Fe2+, Fe3+, Ni2+, and Cu2+
additional information
addition of Ca2+, Zn2+, Fe2+, or Cu2+ is not effective
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glyceraldehyde
competitive inhibition of the isomerization of D-xylose
Ca2+
less than 10% residual activity for D-xylose and D-glucose isomerase activities of XylA at 1 mM Zn2+
Cu2+
complete inhibition of D-xylose and D-glucose isomerase activities of XylA at 1 mM Cu2+
D-glucose
-
suppressed enzyme synthesis by increased content from 0.1 to 1.5%, productivity maxima at 0.1%, if D-xylose is the carbon source: D-glucose supplementation suppresses formation of xylose isomerase
D-glucose
-
suppressed enzyme synthesis by increased D-glucose content from 0.1 to 1.5%, productivity maxima at 1.0%
D-glucose
-
suppressed enzyme synthesis by increased D-glucose content from 0.1 to 1.5%, productivity maxima at 0.1% D-glucose, if D-xylose is the carbon source D-glucose supplementation suppresses formation of xylose isomerase
D-sorbitol
-
competitive against D-glucose, D-xylose, and D-ribose. Co2+ and Mg2+ prevent inhibition
D-Threonohydroxamic acid
-
slow-binding competitive inhibitor with glucose as substrate
D-Threonohydroxamic acid
competitive inhibitor, complete inhibition at 0.5 mM
EDTA
less than 10% residual activity for D-xylose and D-glucose isomerase activities of XylA at 1 mM Zn2+
EDTA
-
Mn2+, Mg2+, or Co2+ restore 60-70% of the original xylose isomerase activity
Tris(hydroxymethyl)aminomethane
-
strong inhibition of D-glucose isomerization, slight inhibition of D-xylose isomerization, competitive
xylitol
-
inhibits in vitro xylose isomerase activity severely and competitively
Zn2+
less than 10% residual activity for D-glucose isomerase activity and about 10% residual activity for D-xylose activity of XylA at 1 mM Zn2+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-glucose
-
if D-xylose is the carbon source D-glucose supplementation stimulates formation of xylose isomerase
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cysts
Down-regulation of cellulose synthase inhibits the formation of endocysts in Acanthamoeba.
Dehydration
A generic protocol for protein crystal dehydration using the HC1b humidity controller.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
180
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A and wild-type
200
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
259.6
D-glucose
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
259.6
D-glucose
Opuntia vulgaris
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
310
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutants E221A and D56N
1 - 4
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
1 - 1.2
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
3
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
3.4
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
3.8
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
4 - 5
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
4.3
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
4.9
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
5
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
5.3
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
6
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
6.5
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
7.4
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
8
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
10
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
15
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
27
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
33
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
37
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
42
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
46.4
D-xylose
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
46.4
D-xylose
Opuntia vulgaris
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
50.18
D-xylose
-
mutant enzyme E129D/V433I/E15D/E114G, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C
54.03
D-xylose
-
in 100 mM Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30°C
83
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
86.97
D-xylose
-
wild type enzyme, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C
89.98
D-xylose
-
mutant enzyme E129D/V433I, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C
168.4
D-xylose
-
mutant enzyme E129D/V433I/E15D/E114G/T142S/A177T, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C
548
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
additional information
additional information
-
Km-values for wild-type enzyme and mutants E186D and E186Q, activated by Mg2+, Mn2+ or Co2+
-
additional information
additional information
-
Km-value for D-xylose varies with the concentration Mn2+
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0001
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
additional information
additional information
-
turnover numbers for wild-type enzyme and mutant enzymes E186D and E186Q, activated by Mg2+, Mn2+ or Co2+
-
0.03 - 0.55
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant E221A
0.031 - 0.51
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D56N
3 - 6
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
3.02
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
0.007
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.056
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.064
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.07
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.074
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.11
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.14
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.15
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.18
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.19
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.31
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.33
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.41
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.51
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.66
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.8
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.96
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.22
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.38
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
2.3
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
2.4
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
5.52
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000034
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
0.00013
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0018
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0019
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0024
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0037
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0049
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.007
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0094
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.01
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.018
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.019
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.023
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.024
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.059
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.064
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.181
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.211
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.24
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.321
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.49
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
0.676
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.84
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00001
0.017
0.034
-
Pseudomonas putida S12 strain xylAB containing xylose isomerase and xylulokinase gene from Escherichia coli
0.04
-
Saccharomyces cerevisiae overexpressing xylose isomerase from Thermus thermophilus, 30°C
0.46
1
-
Saccharomyces cerevisiae overexpressing xylose isomerase from Thermus thermophilus, 85°C
1.1
1.39
132
wild type enzyme, with L-arabinose as substrate, at pH 7.0 and 85°C
266.4
273
wild type enzyme, with D-mannose as substrate, at pH 7.0 and 85°C
330
mutant enzyme D256R, with L-arabinose as substrate, at pH 7.0 and 85°C
380
wild type enzyme, with D-lyxose as substrate, at pH 7.0 and 85°C
6.4
6.78
682
mutant enzyme D256R, with D-mannose as substrate, at pH 7.0 and 85°C
950
mutant enzyme D256R, with D-lyxose as substrate, at pH 7.0 and 85°C
additional information
0.017
-
Saccharomyces cerevisiae overexprssing five own enzymes of pentose phosphate pathway, deletion of an unspecific aldose reductase, overexpressing xylose isomerase from Piromyces sp., 30°C
1.1
-
Saccharomyces cerevisiae overexprssing xylose isomerase from Piromyces sp., 30°C
1.1
-
Saccharomyces cerevisiae strain CEN.PK overexprssing xylose isomerase (xylA gene) from Piromyces sp., TPI1 promoter, 30°C
266.4
-
enzyme isoform T90 after 39.2fold purification with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
266.4
Opuntia vulgaris
-
enzyme isoform T90 after 39.2fold purification with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
6.78
-
enzyme isoform T90 from homogenate with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
6.78
Opuntia vulgaris
-
enzyme isoform T90 from homogenate with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
additional information
-
measurement of the degradation of xylose and glucose
additional information
-
measurement of the degradation of xylose, glucose and a xylose-glucose-mixture
additional information
-
measurement of xylose consumption and ethanol production
additional information
-
modification of established spectrophotometrical activity assay
additional information
-
no activity in: CBS 4732s leu2-2(control strain), DELTAxyl1, DELTAxyl1 DELTAxyl2-A, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
additional information
-
strains are cultivated under aerobic and anaerobic conditions
additional information
-
measurement of the consumption of xylose, mannose and glucose
additional information
-
measurement of the production of ethanol, glycerol and xylitol
additional information
-
measurement of the production of ethanol, glycerol, organic acids, xylitol, CO2
additional information
-
strains are cultivated under aerobic and anaerobic conditions
additional information
-
measurement of the degradation of xylose and glucose
additional information
-
measurement of the production of ethanol, glycerol, organic acids, xylitol, CO2
additional information
-
strain is cultivated under aerobic and anaerobic conditions
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
6.25
-
mutant E186Q, xylose isomerization, activated by Mn2+ or Mg2+
6.8
7 - 9
7.5
7.9
8 - 8.2
-
in presence of Mg2+ and Co2+, mutants D65A and D163N/E167Q
8 - 8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8.5
5 - 9
5.5 - 9.5
-
pH 5.5: about 40% of maximal activity, pH 9.5: about 80% of maximal activity, D-fructose isomerization
6 - 10
-
pH 6: about 35% of maximal activity, pH 10: about 30% of maximal activity
6 - 11
6 - 9
-
pH 6: about 70% of maximal activity, pH 9: about 90% of maximal activity
7 - 10
-
pH 7: about 40% of maximal activity, pH 10: about 13.5% of maximal activity
7.5 - 8
5 - 9
about 40% activity at pH 5.0, about 60% activity at pH 5.5, about 88% activity at pH 6.0 and 8.0, about 92% activity at pH 6.5 and 7.5, about 80% activity at pH 8.5, about 75% activity at pH 9.0
6 - 11
-
pH 6: about 50% of maximal activity, pH 11: about 65% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
65
70
75
78
-
D-glucose, activity increases up to 85°C and remains constant nearly to 100°C
80
80 - 85
85
90
95
85
-
D-xylose,activity increases up to 85°C and remains constant nearly to 100°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
30°C: about 45% of maximal activity, 70°C: about 10% of maximal activity
40 - 80
-
40°C: about 40% of maximal activity, 80°C, about 30% of maximal activity
40 - 90
temperature profiles of recombinant mutant enzymes, overview
50 - 60
50 - 70
-
50°C: about 55% of maximal activity, 70°C: about 65% of maximal activity
50 - 80
-
about 30% activity at 50 and 80°C and about 85% activity at 60 and 70°C
55 - 95
about 52% activity at 55°C, about 65% activity at 60°C, about 75% activity at 65°C, about 78% activity at 70°C, about 85% activity at 75°C, about 95% activity at 80°C, about 78% activity at 90°C, and about 52% activity at 95°C
60 - 80
7.5
7.5
-
the purified T90 isoform at pH 7.5 exhibits a preference to yield the forward isomerization reaction
7.5
Opuntia vulgaris
-
the purified T90 isoform at pH 7.5 exhibits a preference to yield the forward isomerization reaction
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
induced by presence of xylose and xylite. The synthesis of enzyme is controlled by catabolite repression occuring at the transcriptional level and mediated by cyclic 3',5'-AMP
-
-
brenda
recombinant enzyme from Hansenula polymorpha transformants
-
-
brenda
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
source of genes encoding xylose isomerase (xylA) and xylulokinase (xylB)
-
-
brenda
transformed strain LE392-pRK248/pTXI-1, that overproduces the enzyme by induction of the strong lambda PI promoter
-
-
brenda
source of xylose isomerase gene, a phylogenetic tree of the diversity of xylose isomerase genes is given - based on GenBank database
-
-
brenda
designed strain TMB 3045, carrying the XI gene from Thermus thermophilus
-
-
brenda
strain TMB 3050, derived from strain TMB 3045, which carries the XI gene from Thermus thermophilus
-
-
brenda
source of xylose isomerase gene, a phylogenetic tree of the diversity of xylose isomerase genes is given - based on GenBank database
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Pseudomonas strain S12 containing xylose isomerase gene and xylulokinase gene from Escherichia coli strain DH5 alpha
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
a yeast strain expressing the enzyme shows fast aerobic growth on D-xylose. Deletion of Golgi Ca2+/Mn2+ ATPase Pmr1 results in increased intracellular Mn2+ concentrations, leading to increased enzymic activity
metabolism
D-xylose isomerase is essential for xylose catabolism
metabolism
-
D-xylose isomerase is essential for xylose catabolism
-
Show AA Sequence and Transmembrane Helices (16677 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115000 - 117000
-
low speed sedimentation without reaching equilibrium, equilibrium sedimentation
160000
183000
190000
200000
43000
44000
45000
46000
49000
50000
66000
68000
71000
50000
-
2 * 50000, the recombinant enzyme exists as homodimer and homotetramer, with the dimer being the more abundant form. The native enzyme exclusively exists as tetramer
50000
-
4 * 50000, the recombinant enzyme exists as homodimer and homotetramer, with the dimer being the more abundant form. The native enzyme exclusively exists as tetramer
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
monomer
tetramer
trimer
dimer
Bacillus sp. (in: Bacteria) No. KX-6
-
2 * 58000, SDS-PAGE
-
dimer
-
2 * 50000, the recombinant enzyme exists as homodimer and homotetramer, with the dimer being the more abundant form. The native enzyme exclusively exists as tetramer
homotetramer
Limosilactobacillus reuteri DSM Z 17509
-
4 * 51040, calculated from amino acid sequence
-
homotetramer
Streptomyces diastaticus No. 7 M1033
-
alpha4, crystallization studies
-
tetramer
-
4 * 50000, the recombinant enzyme exists as homodimer and homotetramer, with the dimer being the more abundant form. The native enzyme exclusively exists as tetramer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of a number of binary and ternary complexes involving wild-type and mutant enzymes, the divalent cations Mg2+, Co2+, or Mn2+ and either the substrate xylose or substrate analogs
-
structures of the enzyme containing the inhibitors xylitol and D-sorbitol at 2.5 A and 2.3 A resolution respectively
-
sitting drop vapor diffusion method, using 100 mM sodium chloride, 100 mM bicine pH 9.0, 20% (v/v) PEG MME 550
sitting drop vapor diffusion method, using 0.2 M CaCl2, 20% (w/v) polyethylene glycol 3350
sitting drop vapour diffusion method at room temperature, space group 21212 with a: 87.976 A, b: 98.836 and c: 93.927 A
-
D-threonohydroxamic acid soaked into the crystal, crystallographic structure at 1.6 A resolution
-
X-ray crystallographic structure of the metal-activated enzyme with the substrates D-glucose, 3-O-methyl-D-glucose and in the absence of substrate at 1.96 A, 2.19 A, and 1.81 A
-
analysis of the location of hydrogen atoms by time-of-flight neutron Laue technique. The neutron structure of crystalline XI with bound product, D-xylulose, shows, that O5 of D-xylulose is not protonated but is hydrogen-bonded to doubly protonated His54. Also, Lys289, which is neutral in native XI, is protonated, while the catalytic water in native XI has become activated to a hydroxyl anion which is in the proximity of C1 and C2, the molecular site of isomerization of xylose
in complex with D-glyceraldehyde, hanging drop vapor diffusion method, using 0.2-0.3 M Mg-formate at pH 7.0 and 22°C
neutron diffraction, largest crystals at 18°C, 95 mg/ml xylose isomerase, 16.9% ammonium sulfate, mathematical analysis to determine optimal conditions for crystallization
-
neutron quasi-Laue diffraction, resolution: 2.2 A - clear visibility of deuterium atoms, clarification of critical residues at the active site and their protonation states
-
structure of E186Q mutant with cyclic glucose bound at the active site, to 2.2 A resolution. Residue His54 is doubly protonated and is poised to protonate the glucose O5 position, while Lys289, which is neutral, promotes deprotonation of the glucose O1H hydroxyl group via an activated water molecule. An extended hydrogen-bonding network connects the conserved residues Lys289 and Lys183 through three structurally conserved water molecules and residue 186
study on the dynamics of solute transport in orthorhombic D-xylose isomerase crystals by means of Brownian dynamics and molecular dynamics simulations and investigation of the diffusion of S-phenylglycine molecules inside XI crystals. The S-phenylglycine molecules mostly interact with residues His54, Asp287, and Lys183. In general, the diffusivities of solute species are found to be 1 to 2 orders of magnitude lower than those of the corresponding free molecules in water
the mechanism of ring-opening for L-arabinose is the same as for the reaction with D-xylose. In the reactive Michaelis complex L-arabinose is distorted to the high-energy 5S1 conformation. Amino acid substitutions in a hydrophobic pocket near C5 of L-arabinose can enhance sugar binding. L-ribulose and L-ribose are found in furanose forms when bound to the enzyme
time-of-flight neutron diffraction at 1.8 A resolution, metal-free enzyme - emphasis on the active site of xylose isomerase, especially of protonation states of His, Lys and H2O
ammonium sulfate as precipitant, orthorhombic space group P212121 with a: 84.35 A, b: 123.6 A, c: 140.24 A
-
ortjorhombic space group P212121 with a: 84.35 A, b: 123.60 A and c: 140.24 A
-
at room temperature with polyethylene glycol 4000 as precipitant, orthorhombic space group P212121 with a: 73.34 A, b: 144.05 A and c 155.07 A
-
ortjorhombic space group P212121 with a: 73.34 A, b: 144.05 A and c: 155.07 A
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E186D
-
mutant enzymes E186D and E186Q are active, and their metal specificity is different from that of the wild type. The E186 enzyme is most active with Mn2+ and has a drastically shifted pH optimum
E186Q
-
mutant enzymes E186D and E186Q are active, and their metal specificity is different from that of the wild type. The E186 enzyme is most active with Mn2+ and has a drastically shifted pH optimum
E253K
-
substitution of Arg for Lys at position 253 at the dimer-dimer interface increases the half-life of the enzyme by 30%. The largest stability gain is achieved in a triple mutant G70S/A73S/G74T
H101F
-
substitution of His101 by Phe abolishes the enzyme activity, whereas substitution of other His residues has no effect
H41L
-
substitution of Lys for His41 results in a mutant with near wild-type properties. This mutation completely abolishes adsorption to iminodiacetic acid-Cu(II)
Q256D
-
catalytic efficiency with L-arabinose is increased 3fold, reaction rate with L-ribose is increased 6fold
V135N
no effect on the reaction with D-xylose and L-arabinose, reaction efficiency with L-ribose is increased 2-4fold, reaction with D-glucose is impaired
D189L
-
the Glu140Lys and Asp189Lys mutant proteins are synthesized in the Escherichia coli host, but are incapable of folding correctly. Mutant Trp136Glu does not show any enzyme activity
E140L
-
the Glu140Lys and Asp189Lys mutant proteins are synthesized in the Escherichia coli host, but are incapable of folding correctly. Mutant Trp136Glu does not show any enzyme activity
Y253C
-
a Tyr253 mutant in which a disulfide bridge is introduced at the A-B subunit interface shows reduced thermostability, that is identical in both oxidized and reduced forms and also reduced stability in urea. X-ray-crystallographic analysis of the Mn2+-xylitol form of oxidized Y253C shows a changed conformation of Glu185 and also alternative conformations for Asp254, which is a ligand to the site 2 metal ion. With fructose, Mg2+-Y253C has a similar Km to that of the wild-type, and its maximal velocity is also similar below pH 6.4, but declines thereafter. In presence of Co2+, Y253C has lower activity than wild-type at all pH values, but its activity also declines at alkaline pH
DELTAxyl1 DELTAxyl2-A
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 1
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 1
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 2
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 2
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 4L/3
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 4L/3
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA HpXYL3)
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli and overexpressing endogenous xylulukinase xyl3
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 1
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli, strain 1
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 2
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli, strain 2
H101X
-
selective substitution of His101 or His271 shows that they are essential components of the active site
H271X
-
selective substitution of His101 or His271 shows that they are essential components of the active site
Hansenula polymorpha
-
yeast, strain CBS4732s leu2-2, deficient in beta-isopropyl malate dehydrogenase, deletions of genes encoding xylose reductase (xyl1) and xylitol dehydrogenases (xyl2-A and xyl2-B) - overexpression of xylA gene (Escherichia coli) and endogenous xyl3 gene
DELTAxyl1 DELTAxyl2-A
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A
-
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B
-
Hansenula polymorpha
-
yeast, strain CBS4732s leu2-2, deficient in beta-isopropyl malate dehydrogenase, deletions of genes encoding xylose reductase (xyl1) and xylitol dehydrogenases (xyl2-A and xyl2-B) - overexpression of xylA gene (Escherichia coli) and endogenous xyl3 gene
-
E129D/V433I/E15D/E114G/T142S/A177T
-
the mutant exhibits a 77% increase in enzymatic activity. A yeast strain expressing this mutant enzyme improves its aerobic growth rate by 61fold and both ethanol production and xylose consumption rates by nearly 8fold
Z180L
-
one of the metal-binding sites, M-1, is removed by substitution of Glu-180 by Lys. Glu-180 is essential for isomerization but not for ring opening
D163N/E167Q
-
40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
D56N
-
turnover number increased by 30-40% over that ofwild-type at pH 7.3, lower pH optimum than wild-type, nearly same thermostability as wild-type
D65A
-
40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
D81A
-
40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
E221A
-
turnover number increased by 30-40% over that from wild-type at pH 7.3, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
H220S
-
decreased affinity for Mg2+ and decraesed activity in contrast to wild-type
N185K
-
decreased affinity for Mg2+ and decraesed activity in contrast to wild-type
H101F
W139A
-
replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid
W139F
W139F/V186S
-
double mutants, W139F/V186T and W139F/V186S have 5fold and 2fold higher catalytic efficiency, respectively, than does the wild-type
W139F/V186T
-
double mutants, W139F/V186T and W139F/V186S have 5fold and 2fold higher catalytic efficiency, respectively, than does the wild-type
W139M
-
replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid
D309K
-
no activity, Tm of 95.5°C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E232K
-
no activity, Tm of 100.7°C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E232K/D309K
-
no activity, Tm of 96.5°C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
D256R
the mutant shows an increase in the specificity on D-lyxose, L-arabinose and D-mannose
E372G
-
broader pH range and nine times higher turnover for D-xylose at 60°C than wild-type
E372G/F163L
-
broader pH range and nine times higher turnover for D-xylose at 60°C than wild-type
E372G/V379A
-
broader pH range and nine times higher turnover for D-xylose at 60°C than wild-type
N91D
N91D/D375G
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/D375G/V385A
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/K355A
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/V144A
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
D256R
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the mutant shows an increase in the specificity on D-lyxose, L-arabinose and D-mannose
-
N91D
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
the mutant shows increased substrate specificity for D-xylose compared to the wild type enzyme
-
additional information
H101F
-
substitution of His101 by Phe completely abolishes enzyme activity. When His101 is changed to Glu, Gln, Asn, or Asp, approximately 10-16% of wild-type enzyme activity is retained by the mutant enzymes. The His101Gln mutant enzyme is resistant to diethyldicarbonate inhibition which completely inactivates the wild-type enzyme
W139F
-
replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid
W139F
-
the W139F substitution reduces the Km and increases the turnover number of the mutant towards glucose, while the reverse effect towards xylose is observed
N91D
-
the mutant shows increased substrate specificity for D-xylose compared to the wild type enzyme
additional information
-
metabolic engineering of Corynebacterium glutamicum to broaden substrate utilization range
additional information
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
additional information
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
-
additional information
overexpression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate, overview. Expression in a wild-type strain does not lead to increased polyhydroxybutyrate repoduction and cell growth, overview
additional information
-
overexpression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate, overview. Expression in a wild-type strain does not lead to increased polyhydroxybutyrate repoduction and cell growth, overview
additional information
-
overexpression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate, overview. Expression in a wild-type strain does not lead to increased polyhydroxybutyrate repoduction and cell growth, overview
-
additional information
-
Saccharomyces cerevisiae: five enzymes of non-oxidative pentose-phosphate-pathway are induced, a unspecific aldose reductase is deleted
additional information
-
the overexpressing Saccharomyces cerevisiae strain RWB 218 shows sensitivity to inhibitor acetic acid, kinetics and stoichiometry, detailed overview. At pH 3.5 acetic acid had a strong and specific negative impact on xylose consumption rates, which, after glucose depletion, slowed down dramatically, leaving 50% of the xylose unused after 48 h of fermentation
additional information
-
establishing and optimization of ethanol production from hotcompressed water treatment of Japanese beech by bioconversion of D-xylose via xylose isomerase, production enhancement by process integration of saccharifi cation, isomerization, and fermentation, process schemes, overview
additional information
-
Saccharomyces cerevisiae: five enzymes of non-oxidative pentose-phosphate-pathway are induced, a non-specific aldose reductase is deleted
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10
the enzyme is stable for 1 h from pH 5.5 to 10.0 at 60°C
714586
5.5 - 8.5
7 - 8
additional information
-
stable in acidic as well as basic pH in presence of divalent kations Mn2+, Co2+, and Mg2+
691766
5.5 - 8.5
-
the enzyme exhibits a broad range (5.5-8.5) of pH stability but denatures readily at pH values below 4.0
713800
5.5 - 8.5
Opuntia vulgaris
-
the enzyme exhibits a broad range (5.5-8.5) of pH stability but denatures readily at pH values below 4.0
713800
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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
-
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
-
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
-
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
-
mutant Q256D remains fully active for 60 min at 65°C, whereas the activity is rapidly lost at 80°C
70
-
in the presence of CO2+, cell-free xylose isomerase retains 100% activity without loss of activity for 7 days
70
-
half-life in absence of divalent cations: 4 d. In presence of Mn2+ or Co2+ stable for at least 1 month
80
-
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
-
in the presence of CO2+, cell-free xylose isomerase retains 50% residual activity for 13.5 h
90
-
the melting temperature of the native enzyme isoform T90 is at 90°C
90
-
after 1 h incubation the recombinant and the wild-type enzymes retain 25 and 34% of their activity, respectively
90
-
in the presence of CO2+, cell-free xylose isomerase retains 50% residual activity for 126 min
additional information
-
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
-
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
-
Co2+ is superior as protector against thermal inactivation at 80°C
additional information
-
Mn2+ and Co2+ increase thermal stability
additional information
-
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
-
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
-
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
-
Mn2+, Co2+ and Ni2+ strongly protect the enzyme from heat denaturation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after operating at 70°C for 5 days, the remaining enzyme activities of the immobilized enzyme and the whole cells in the presence of Mg2+ and Co2+ is 75%
-
Co2+ is superior as protector against thermal inactivation at 80°C
-
glycinamidylated enzyme is less stable than the native enzyme in 8 M urea or on heating
-
immobilized enzyme remains stable for at least 45 d at 4°C or at 25°C, upon incubation at 70°C the half-life is about 4 d
-
stability is also strongly influenced by the addition of divalent cations. The addition of Mn2+ gives the highest thermostability, Mg2+ has a
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
-
70-80% of cross-linked crystalline xylose isomerase activity is left after incubation for 24 h at 50°C in buffer solutions (pH 7.2) containing 10-90% acetone. Soluble xylose isomerase is considerably less stable in acetone-containing solutions. The addition of acetone enhances the production of fructose from glucose by enhancing the reaction rate and shifting the equilibrium toward fructose. However, xylose isomerase must be in the form of cross-linked crystals for maximal activity and stability
Ethanol
-
in buffer containing 50% ethanol only 2% of the initial cross-linked crystalline xylose isomerase activity is retained after 24 h at 50°C. Soluble xylose isomerase is considerably less stable in ethanol-containing solutions
Methanol
-
cross-linked crystalline xylose isomerase is inactivated in 24 h at 50°C even more in maleate buffer containing 50% methanol
Pyridine
-
cross-linked crystalline xylose isomerase is inactivated in 24 h at 50°C even more in maleate buffer containing 10% pyridine
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, pH 7.5, 5 mM MgSO4, stable for at least 6 months, in absence of Mg2+ loss of activity within 3 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Dowex-1 anion exchange column chromatography, and Sephadex G-100 gel filtration
ammonium sulfate precipitation, Dowex-1 column chromatography, and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation, Ni-NTA column chromatography, and Superdex 200 gel filtration
from a stock solution of a food grade product, 2 counterdiffusion dialysis devices: diffusion-controlled apparatus for microgravity and counterdiffusion cell, growth of crystals approx. 3 months
gel filtration over Sephacryl S200 - dialysis against 0.05 g/l MgSO4, purity control verified with capillary electrophoresis
-
gel filtration with Sephacryl S-200 high resolution media, running buffer composed of 0.05 M sodium phosphate pH 7.7, 0.1 M sodium chloride and 0.02% azide - final purity of xylose isomerase: 96%
-
heat treatment and DEAE-Sepharose column chromatography
heat treatment, DEAE-Sepharose column chromatography and Q-Sepharose column chromatography
-
one-step purification by high-performance immobilized copper-affinity chromatography
-
PAGE and SDS-PAGE, identical electrophoretic mobility of intact and denatured enzyme compared with xylose isomerase from Arthrobacter nicotianae and Erwinia carotovora subsp. atroseptica
-
PAGE and SDS-PAGE, identical electrophoretic mobility of intact and denatured enzyme compared with xylose isomerase from Escherichia coli and Erwinia carotovora subsp. atroseptica
-
PAGE and SDS-PAGE, identical electrophoretic mobility of intact and denatured enzyme compared with xylose isomerase from from Arthrobacter nicotianae and Escherichia coli
-
recombinant enzyme from Escherichia coli strain BL21(DE3) by one-step affinity chromatography to over 90% purity
-
recombinant enzyme, by heat precipitation and cation exchange, proteins were 95% pure when estimated in SDS-PAGE
Talon metal affinity column chromatography and Superdex 75 gel filtration
ammonium sulfate precipitation, Dowex-1 anion exchange column chromatography, and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation, Dowex-1 anion exchange column chromatography, and Sephadex G-100 gel filtration
Opuntia vulgaris
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and functional expression of enzymes from Escherichia coli in Pseudomonas putida
-
co-overexpression of genes encoding xylose isomerase (EcxylA, Escherichia coli) and xylulokinase (XYL3, Hansenula polymorpha), expression of both genes is driven by Hansenula polymorpha GAP-DH promoter
-
Corynebacterium glutamicum is transformed with: xylose isomerase (xylA, Escherichia coli) and xylulokinase (xylB, Escherichia coli)-two recombinant strains of Corynebacterium glutamicum are obtained: CRX1 (xylA) and CRX2 (xylA/xylB)
-
expressed in Escherichia coli BL21 Star (DE3) cells and in Lactobacillus plantarum
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae
expression in Escherichia coli
expression in Escherichia coli (DH5-alpha) and Saccharomyces cerevisiae
-
expression in Escherichia coli HB101
expression in Escherichia coli, sequence homology with enzymes from other sources
-
expression in Saccharomyces cerevisiae
expression in the yeast Hansenula polymorpha
expression of mutant enzymes in Escherichia coli strain BL21 (DE3)
gene XYL1, subcloning in Escherichia coli strain MC1061, functional expression in Corynebacterium glutamicum, ATCC13032. Biotransformation of xylose into xylitol appears to be influenced by xylose transport, which is in turn affected by the glucose concentration in the reaction medium
-
gene xylA, expression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate and increasing cell growth, overview
phylogenetic analysis and enzyme sequence comparisons, functional expression of codon-optimized enzyme in Saccharomyces cerevisiae confers on the yeast cells the ability to metabolize D-xylose and to use it as the sole carbon and energy source. The recombinant enzyme shows reduced sensitivity to inhibition by xylitol
phylogenetic analysis, enzyme expression in Escherichia coli strain BL21(DE3)
-
Saccharomyces cerevisiae is transformed with a gene encoding xylose isomerase (Thermus thermophilus)
-
Saccharomyces cerevisiae is transformed with a gene encoding xylose isomerase originating from Piromyces sp.
-
the production of the cloned gene in Escherichia coli and Bacillus brevis are compared expression in Escherichia coli and Bacillus brevis. Bacillus brevis is able to produce the isomerase efficiently (more than 1 g/l)
-
transformants bearing the fused lac-xylA or tac-xylA gene, cloned into various high copy-number plasmids
-
xylose isomerase gene (Piromyces sp.) is overexpressed in Saccharomyces cerevisiae strain TMB3044 resulting in strain TMB 3066
-
Zymobacter palmae is transformed with: xylose isomerase (xylA, Escherichia coli), xylulokinase (xylB, Escherichia coli), transaldolase (tal, Escherichia coli), transketolase (tktA, Escherichia coli). Different promotors from Zymomonas mobilis ATCC 29191 are used: gap-dh (Pgap), enolase (Peno)
-
phylogenetic analysis and enzyme sequence comparisons, functional expression of codon-optimized enzyme in Saccharomyces cerevisiae confers on the yeast cells the ability to metabolize D-xylose and to use it as the sole carbon and energy source. The recombinant enzyme shows reduced sensitivity to inhibition by xylitol
-
phylogenetic analysis and enzyme sequence comparisons, functional expression of codon-optimized enzyme in Saccharomyces cerevisiae confers on the yeast cells the ability to metabolize D-xylose and to use it as the sole carbon and energy source. The recombinant enzyme shows reduced sensitivity to inhibition by xylitol
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
xylulose at a concentration of 0.005% (w/v) almost completely represses the xylose isomerase synthesis in Arthrobacter nicotianae
xylulose at a concentration of 0.005% (w/v) almost completely represses the xylose isomerase synthesis in Arthrobacter nicotianae
-
xylulose at a concentration of 0.005% (w/v) almost completely represses the xylose isomerase synthesis in Arthrobacter nicotianae
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
putative use of lignocellulosic biomass as feedstock for the chemical industry
degradation
energy production
food industry
nutrition
synthesis
degradation
enzyme additionally displays xylose fermenting activity. A Saccharomyces cerevisae strain coexpressing xylose isomerase and endo-1,4-beta-xylanase Xyn11B from Saccharophagus degradans, and beta-xylosidase XlnD from Aspergillus niger is able to produce 6.0 g/l ethanol from xylan
degradation
-
enzyme additionally displays xylose fermenting activity. A Saccharomyces cerevisae strain coexpressing xylose isomerase and endo-1,4-beta-xylanase Xyn11B from Saccharophagus degradans, and beta-xylosidase XlnD from Aspergillus niger is able to produce 6.0 g/l ethanol from xylan
-
energy production
-
engineering of Saccharomyces cerevisiae for alcoholic fermentation of D-xylose
energy production
-
engineering Saccharomyces cerevisiae for alcoholic fermentation of D-xylose
energy production
-
genetic engineering of Saccharomyces cerevisiae in order to increase ethanol production by fermentation of D-xylose
energy production
-
genetic engineering of the yeast Hansenula polymorpha in order to increase ethanol production by D-xylose fermentation
energy production
-
genetic engineering of Zymobacter palmae in order to produce ethanol from xylose fermentation
energy production
-
genetic engineering of the yeast Hansenula polymorpha in order to increase ethanol production by D-xylose fermentation
-
food industry
-
thermophilic xylose isomerase from Opuntia vulgaris can serve as a good alternate source of enzyme for use in the production of high fructose corn syrup
food industry
Opuntia vulgaris
-
thermophilic xylose isomerase from Opuntia vulgaris can serve as a good alternate source of enzyme for use in the production of high fructose corn syrup
food industry
-
xylose isomerase is widely used for production of glucose fructose syrup, a natural sweetener in dietary and preventive nutrition
food industry
-
xylose isomerase isozyme T80 serves as potential alternate catalytic converter of glucose in the production of high-fructose corn syrup for the sweetener industry and for ethanol production
food industry
industrial production of high fructose corn syrup
food industry
-
xylose isomerase is widely used for production of glucose fructose syrup, a natural sweetener in dietary and preventive nutrition
-
synthesis
-
used in industry for the production of high-fructose corn syrups
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
synthesis
-
higher rates of xylose utilization by further improved strains make alcoholic fermentation of hemicellulose fractions of plant biomass a realistic enterprise
synthesis
alcohol fermentation of xylose and mixed sugars by Saccharomyces cerevisiae constitutively overexpressing of the Orpinomyces sp. xylose isomerase, the Saccharomyces cerevisiae xylulokinase, and the Pichia stipitis SUT1 sugar transporter genes. A strain adapted for enhanced growth on xylose by serial transfer in xylose-containing minimal medium under aerobic conditions can ferment 20 g per l of xylose to ethanol with a yield of 0.37 g per g and production rate of 0.026 g per l and h. Raising the fermentation temperature from 30°C to 35°C results in a substantial increase in the ethanol yield and production as well as a significant reduction in the xylitol yield. Ethanol production from xylose and a mixture of glucose and xylose is achieved in complex medium containing yeast extract, peptone, and borate with a considerably high yield of 0.48 g per g
synthesis
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
synthesis
-
expression of Escherichia coli xylose isomerase and xylulokinase in Pseudomonas putida S12 for efficient utilization of D-xylose and L-arabinose. After laboratory evolution of strains by repeated transfer to fresh minimal medium with xylose, a strain that efficiently utilizes xylose at a considerably improved growth rate can be obtained. The high yield can be attributed in part to glucose dehydrogenase inactivity, whereas the improved growth rate may be connected to alterations in the primary metabolism. The evolved D-xylose-utilizing strain metabolizes L-arabinose as efficiently as D-xylose, while its ability to utilize glucose is not affected
synthesis
the combination of TxyA, XloA, and XylA is useful tool for the D-xylulose production from beta-1,3-xylan
synthesis
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
-
synthesis
-
the combination of TxyA, XloA, and XylA is useful tool for the D-xylulose production from beta-1,3-xylan
-
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Release 2023.1 (January 2023)
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