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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

Reaction

alpha-D-xylopyranose
=
alpha-D-xylufuranose

Synonyms

D-XI, D-xylose aldose-ketose-isomerase, D-xylose isomerase, D-Xylose ketoisomerase, D-xylose ketol isomerase, D-xylose ketol-isomerase, D-xylose: ketol-isomerase, D-xylulose keto-isomerase, glucose isomerase, glucose/xylose isomerase, GXI, Isomerase, xylose, Maxazyme, Optisweet, SDXyI, Spezyme, Sweetase, Sweetzyme, Sweetzyme Q, Swetase, T80 xylose isomerase, TcaXI, TNXI, TthXI, XI, XYLA, XylC, xylose (glucose) isomerase, xylose isomerase

ECTree

     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.1 Interconverting aldoses and ketoses, and related compounds
                5.3.1.5 xylose isomerase

Engineering

Engineering on EC 5.3.1.5 - xylose isomerase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
F26W
-
catalytic efficiency with L-arabinose is increased 2fold
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
-
deficient in xylose reductase
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
-
deficient in xylose reductase
-
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
-
E407K
-
2% of strain IO-1 wild-type activity
K407E
-
92% of wild-type activity
R202M
-
9% of strain IO-1 wild-type activity
R202M/V275A
-
26% of strain IO-1 wild-type activity
R202M/Y218D
-
9% of strain IO-1 wild-type activity
R202M/Y218D/V275A
-
62% of strain IO-1 wild-type activity and soluble
S247A
-
97% of wild-type activity
S247A/K407E
-
79% of wild-type activity
S247A/S388T
-
27% of wild-type activity
S388T
-
insoluble and 8% of wild-type activity
S388T/K407E
-
soluble and 50% of wild-type activity
T388S
-
11% of strain IO-1 wild-type activity
Y218D
-
14% of strain IO-1 wild-type activity
Y218D/V275A
-
24% of strain IO-1 wild-type activity
Y275A
-
24% of strain IO-1 wild-type activity
E407K
-
2% of strain IO-1 wild-type activity
-
R202M
-
9% of strain IO-1 wild-type activity
-
T388S
-
11% of strain IO-1 wild-type activity
-
Y218D
-
14% of strain IO-1 wild-type activity
-
Y275A
-
24% of strain IO-1 wild-type activity
-
E407K
-
2% of strain IO-1 wild-type activity
-
R202M
-
9% of strain IO-1 wild-type activity
-
T388S
-
11% of strain IO-1 wild-type activity
-
Y218D
-
14% of strain IO-1 wild-type activity
-
Y275A
-
24% of strain IO-1 wild-type activity
-
E129D/V433I
-
the mutation shows an increase in enzymatic activity
E129D/V433I/E15D/E114G
-
the mutation shows an increase in enzymatic activity
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
D287N
-
inactive
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
E186Q
crystallization data
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+
V185T
mutation increases catalytic efficiency on glucose
D254R/D256R
complete loss of activity
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/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
D254R/D256R
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
complete loss of activity
-
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