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

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
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
W351F
the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates
Y300A
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
0
E247A
-
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
0
Q384A
-
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
0
W351F
-
the mutant shows reduced kcat values for monosaccharide and oligosaccharide substrates
0
Y300A
-
the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
0
Y300N
-
the mutation doubles kcat values for monosaccharide and oligosaccharide substrates
0
Y72A
-
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
0
Y72F
-
the mutation decreases the kcat and catalytic efficiency of the enzyme on oligosaccharides compared to the wild type enzyme
0