1.1.99.B3: glucooligosaccharide oxidase
This is an abbreviated version!
For detailed information about glucooligosaccharide oxidase, go to the full flat file.
Word Map on EC 1.1.99.B3
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1.1.99.B3
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strictum
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acremonium
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fad
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sarocladium
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xylo-oligosaccharides
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maltose
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cellobiose
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maltooligosaccharides
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cello
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carbohydrate-binding
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isoalloxazine
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flavinylation
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flavoenzyme
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xylos
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cello-oligosaccharide
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maltotriose
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6-s-cysteinyl
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maltopentaose
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lactobionic
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xylobiose
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hardwood
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bran
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maltohexaose
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thermocellum
- 1.1.99.B3
- strictum
-
acremonium
- fad
-
sarocladium
- xylo-oligosaccharides
- maltose
- cellobiose
- maltooligosaccharides
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cello
-
carbohydrate-binding
- isoalloxazine
-
flavinylation
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flavoenzyme
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xylos
- cello-oligosaccharide
- maltotriose
-
6-s-cysteinyl
- maltopentaose
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lactobionic
- xylobiose
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hardwood
- bran
- maltohexaose
- thermocellum
Reaction
Synonyms
gluco-oligosaccharide oxidase, glucooligosaccharide oxidase, GOOX, GOOX-VN
ECTree
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Engineering
Engineering on EC 1.1.99.B3 - glucooligosaccharide oxidase
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A38V
the mutation significantly increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
A38V/S388N
the mutation increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
E247A
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q353A
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q353N
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q384A
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Q384N
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
W351A
W351F
the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates
Y300A
Y300N
the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
Y72A
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
Y72F
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
A38V
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the mutation significantly increases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
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E247A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
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Q384A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
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W351F
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the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates
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Y300A
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the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
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Y300N
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the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
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Y72A
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
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Y72F
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the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
-
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
W351A
the mutation increases Km values by up to 2 orders of magnitude while also increasing kcat up to 3fold on cello- and xylo-oligosaccharides and showing no substrate inhibition compared to the wild type enzyme
the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
Y300A
the variant shows broader substrate range and higher H2O2 stability and specifically exhibits up to 40times higher activity on all tested sugars except D-glucose compared to the wild type enzyme
Y300A
the mutant variant of gluco-oligosaccharide oxidase (GOOX) from Sarocladium strictum shows a broader substrate range and higher H2O2 stability compared to the wild-type enzyme. The mutant Y300A exhibits up to 40times higher activity on all tested sugars except glucose, compared to wild-type. Fusion of the Y300A variant to a family 22 carbohydrate binding module from Clostridium thermocellum (CtCBM22A) nearly doubles its catalytic efficiency on glucose, while retaining significant activity on oligosaccharides. In the presence of 200 mM of H2O2, the recombinant CtCBM22A_Y300A retains 80% of activity on glucose and 100% of activity on cellobiose, the preferred substrate for this enzyme, while the wild-type enzyme retains 60% activity on D-glucose under the same conditions. GOOX variants appear to undergo a different mechanism of inactivation, as a loss of histidine instead of methionine is observed after H2O2 incubation. The addition of CtCBM22A also promotes functional binding of the fusion enzyme to xylan, facilitating its simultaneous purification and immobilization using edible oat spelt xylan, which might benefit the usage of this enzyme preparation in food and baking applications. The presence of CtCBM22A also permits enzyme binding to oat spelt xylans, facilitating simultaneous purification and immobilization of the enzyme, and ancillary fibre enrichment in potential food applications