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Literature summary extracted from

  • Vuong, T.V.; Foumani, M.; MacCormick, B.; Kwan, R.; Master, E.R.
    Direct comparison of gluco-oligosaccharide oxidase variants and glucose oxidase substrate range and H2O2 stability (2016), Sci. Rep., 6, 37356 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
1.1.3.4 additional information despite the broad range of applications for glucose oxidase, the effectiveness of glucose oxidase is restricted by the narrow substrate range of this enzyme and susceptibility to H2O2 inactivation Aspergillus niger

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.4 recombinant expression of His-tagged enzyme in Pichia pastoris strain KM71H Aspergillus niger
1.1.99.B3 recombinant expression of His-tagged mutant enzyme in Pichia pastoris strain KM71H Sarocladium strictum

Protein Variants

EC Number Protein Variants Comment Organism
1.1.99.B3 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 Sarocladium strictum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.4 H2O2 loss of 40% activity on D-glucose at 200 mM H2O2 Aspergillus niger
1.1.99.B3 additional information mutants Y300D and CtCBM22A_Y300A GOOX variants show no H2O2 inactivation on cellobiose Sarocladium strictum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.99.B3 0.21
-
cellotriose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 0.25
-
cellobiose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 0.25
-
cellobiose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 0.25
-
cellotriose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 0.3
-
cellopentaose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 0.31
-
cellohexaose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 3
-
xylohexaose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 3.15
-
xylotriose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 4.49
-
xylopentaose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 4.57
-
xylotriose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 5.11
-
xylobiose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 5.4
-
D-glucose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 5.84
-
xylobiose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 8.1
-
D-glucose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 37
-
D-xylose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 51.8
-
D-xylose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.4 beta-D-glucose + O2 Aspergillus niger
-
D-glucono-1,5-lactone + H2O2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger Q9HFQ1
-
-
1.1.99.B3 Sarocladium strictum Q6PW77
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.4 beta-D-glucose + O2
-
Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?
1.1.3.4 beta-D-glucose + O2 the enzyme is highly specific for D-glucose Aspergillus niger D-glucono-1,5-lactone + H2O2
-
?
1.1.3.4 additional information the enzyme oxidizes the anomeric carbon of beta-D-glucose using molecular oxygen as an electron acceptor, producing H2O2 and D-glucono-delta-lactone, which in the presence of water spontaneously hydrolyzes to gluconic acid. Poor activity with xylose, maltose, cellobiose, cellotetraose, and xylo-oligosaccharides Aspergillus niger ?
-
?
1.1.99.B3 cellobiose + O2 preferred substrate Sarocladium strictum ? + H2O2
-
?
1.1.99.B3 cellohexaose + O2
-
Sarocladium strictum Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-D-glucono-1,5-lactone + H2O2
-
?
1.1.99.B3 cellopentaose + O2
-
Sarocladium strictum Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-D-glucono-1,5-lactone + H2O2
-
?
1.1.99.B3 cellotetraose + O2
-
Sarocladium strictum Glc-beta-(1->4)-Glc-beta-(1->4)-Glc-beta-(1->4)-D-glucono-1,5-lactone + H2O2
-
?
1.1.99.B3 cellotriose + O2
-
Sarocladium strictum Glc-beta-(1->4)-Glc-beta-(1->4)-D-glucono-1,5-lactone + H2O2
-
?
1.1.99.B3 D-glucose + O2
-
Sarocladium strictum D-glucono-1,5-lactone + H2O2
-
?
1.1.99.B3 D-xylose + O2
-
Sarocladium strictum D-xylono-1,5-lactone + H2O2
-
?
1.1.99.B3 maltose + O2
-
Sarocladium strictum 4-O-alpha-D-glucopyranosyl-D-glucono-1,5-lactone + H2O2
-
?
1.1.99.B3 additional information enzyme GOOX oxidizes the anomeric carbon of carbohydrate substrates through an FAD reduction mechanism. The enzyme displays a comparatively broad substrate profile, ranging from D-xylose, and galactose, to malto-, cello- and xylooligosaccharides. GOOX oxidizes oligosaccharides more effectively than monosaccharides Sarocladium strictum ?
-
?
1.1.99.B3 xylobiose + O2
-
Sarocladium strictum xyl-beta-(1->4)-D-xylono-1,5-lactone + H2O2
-
?
1.1.99.B3 xylohexaose + O2
-
Sarocladium strictum D-Xyl-beta-(1->4)-D-Xyl-beta-(1->4)-D-Xyl-beta-(1->4)-D-Xyl-beta-(1->4)-D-Xyl-beta-(1->4)-D-xylono-1,5-lactone + H2O2
-
?
1.1.99.B3 xylooligosaccharide + O2
-
Sarocladium strictum ? + H2O2
-
?
1.1.99.B3 xylopentaose + O2
-
Sarocladium strictum D-Xyl-beta-(1->4)-D-Xyl-beta-(1->4)-D-Xyl-beta-(1->4)-D-Xyl-beta-(1->4)-D-xylono-1,5-lactone + H2O2
-
?
1.1.99.B3 xylotriose + O2
-
Sarocladium strictum xyl-beta-(1->4)-xyl-beta-(1->4)-D-xylono-1,5-lactone + H2O2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.1.99.B3 gluco-oligosaccharide oxidase
-
Sarocladium strictum
1.1.99.B3 GOOX
-
Sarocladium strictum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.4 37
-
assay at Aspergillus niger
1.1.99.B3 37
-
assay at Sarocladium strictum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.99.B3 11.17
-
cellotriose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 11.33
-
D-xylose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 13.22
-
D-glucose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 13.28
-
xylobiose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 13.72
-
cellobiose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 13.87
-
xylotriose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 15.68
-
D-glucose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 16.25
-
D-xylose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 16.33
-
cellobiose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 16.5
-
cellohexaose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 17.43
-
xylohexaose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 18.33
-
cellopentaose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 18.67
-
cellotriose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 19.67
-
xylotriose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 19.72
-
xylobiose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum
1.1.99.B3 26.17
-
xylopentaose pH 8.0, 37°C, recombinant mutant CtCBM22A_Y300A Sarocladium strictum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.4 5
-
assay at Aspergillus niger
1.1.99.B3 8
-
assay at Sarocladium strictum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.4 FAD a flavoenzyme with a tightly but non-covalently bound FAD cofactor Aspergillus niger
1.1.99.B3 FAD the FAD cofactor is bi-covalently linked through cysteine and histidine residues Sarocladium strictum

General Information

EC Number General Information Comment Organism
1.1.3.4 evolution glucose oxidase (GO) belongs to the auxiliary activity family AA3_2 Aspergillus niger
1.1.3.4 malfunction comparison of the substrate profile and H2O2 inactivation of the wild-type glucose oxidase, EC 1.1.3.4, and the Y300A mutant variant of GOOX, the mutant shows a comparatively broad substrate range along with reduced substrate inhibition compared to glucose oxidase, overview Aspergillus niger
1.1.3.4 additional information narrow binding pocket of glucose oxidase Aspergillus niger
1.1.99.B3 malfunction comparison of the substrate profile and H2O2 inactivation of the wild-type glucose oxidase, EC 1.1.3.4, and the Y300A mutant variant of GOOX, the mutant shows a comparatively broad substrate range along with reduced substrate inhibition compared to glucose oxidase, overview Sarocladium strictum
1.1.99.B3 additional information open active site of GOOX compared to glucose oxidase Sarocladium strictum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.99.B3 0.25
-
cellobiose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 0.25
-
cellotriose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 0.45
-
D-xylose pH 8.0, 37°C, recombinant enzyme mutant Sarocladium strictum
1.1.99.B3 2.883
-
D-glucose pH 8.0, 37°C, recombinant enzyme mutant Sarocladium strictum
1.1.99.B3 3.15
-
xylotriose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 5.11
-
xylobiose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 8.1
-
D-glucose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum
1.1.99.B3 51.8
-
D-xylose pH 8.0, 37°C, recombinant mutant Y300A Sarocladium strictum