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
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high-fructose
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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
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Engineering
Engineering on EC 5.3.1.5 - xylose isomerase
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E186D
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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
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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
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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
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substitution of His101 by Phe abolishes the enzyme activity, whereas substitution of other His residues has no effect
H41L
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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
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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
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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
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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
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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
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deficient in xylose reductase and xylitol dehydrogenase xyl2-A
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 1
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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
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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
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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
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deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA HpXYL3)
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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
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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
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deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli, strain 2
H101X
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selective substitution of His101 or His271 shows that they are essential components of the active site
H271X
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selective substitution of His101 or His271 shows that they are essential components of the active site
Hansenula polymorpha
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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
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deficient in xylose reductase and xylitol dehydrogenase xyl2-A
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DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
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deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B
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Hansenula polymorpha
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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
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E129D/V433I/E15D/E114G/T142S/A177T
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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
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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
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40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
D56N
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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
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40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
D81A
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40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
E221A
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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
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decreased affinity for Mg2+ and decraesed activity in contrast to wild-type
N185K
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decreased affinity for Mg2+ and decraesed activity in contrast to wild-type
H101F
W139A
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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
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double mutants, W139F/V186T and W139F/V186S have 5fold and 2fold higher catalytic efficiency, respectively, than does the wild-type
W139F/V186T
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double mutants, W139F/V186T and W139F/V186S have 5fold and 2fold higher catalytic efficiency, respectively, than does the wild-type
W139M
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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
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no activity, Tm of 95.5°C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E232K
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no activity, Tm of 100.7°C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E232K/D309K
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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
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broader pH range and nine times higher turnover for D-xylose at 60°C than wild-type
E372G/F163L
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broader pH range and nine times higher turnover for D-xylose at 60°C than wild-type
E372G/V379A
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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
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the mutant shows an increase in the specificity on D-lyxose, L-arabinose and D-mannose
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N91D
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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the mutant shows increased substrate specificity for D-xylose compared to the wild type enzyme
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additional information
H101F
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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
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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
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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
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the mutant shows increased substrate specificity for D-xylose compared to the wild type enzyme
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metabolic engineering of Corynebacterium glutamicum to broaden substrate utilization range
additional information
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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
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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
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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
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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
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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
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additional information
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Saccharomyces cerevisiae: five enzymes of non-oxidative pentose-phosphate-pathway are induced, a unspecific aldose reductase is deleted
additional information
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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
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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
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Saccharomyces cerevisiae: five enzymes of non-oxidative pentose-phosphate-pathway are induced, a non-specific aldose reductase is deleted