1.1.99.B3: glucooligosaccharide oxidase

This is an abbreviated version, for detailed information about glucooligosaccharide oxidase, go to the full flat file.

Reaction

[beta-D-hexosyl-(1->4)]n-beta-D-hexose
+
acceptor
=
[beta-D-hexosyl-(1->4)]n-D-hexono-1,5-lactone
+
reduced acceptor

Synonyms

gluco-oligosaccharide oxidase, glucooligosaccharide oxidase, GOOX, GOOX-VN

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.99 With unknown physiological acceptors
                1.1.99.B3 glucooligosaccharide oxidase

Engineering

Engineering on EC 1.1.99.B3 - glucooligosaccharide oxidase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
C130A
-
FAD binding site, FAD covalently attached
E247A
-
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
H70A
-
FAD binding site, FAD covalently attached
H70A/C130A
-
no activity, lack of essential FAD cofactor
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
-
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme; 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
W351F
-
the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates
Y300N
-
the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
Y310A
-
larger amount of carbohydrates
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
-
the mutation significantly 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
-
Q384A
-
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
-
W351F
-
the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates
-
Y300A
-
the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
-
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
-