1.1.99.28: glucose-fructose oxidoreductase
This is an abbreviated version!
For detailed information about glucose-fructose oxidoreductase, go to the full flat file.
Word Map on EC 1.1.99.28
-
1.1.99.28
-
zymomonas
-
mobilis
-
sorbitol
-
gluconic
-
lactobionic
-
nadp-containing
-
gluconolactonase
-
d-xylose
-
1,5-anhydro-d-fructose
-
synthesis
-
dihydrodiol
- 1.1.99.28
- zymomonas
- mobilis
- sorbitol
-
gluconic
-
lactobionic
-
nadp-containing
- gluconolactonase
- d-xylose
- 1,5-anhydro-d-fructose
- synthesis
-
dihydrodiol
Reaction
Synonyms
EC 1.1.1.99, GFOD2, GFOR, glucose fructose oxidoreductase, glucose-fructose oxidoreductase, glucose-fructose oxidoreductase domain containing 2, Glucose-fructose transhydrogenase, NADP(H)-dependent glucose-fructose oxidoreductase, Transhydrogenase, glucose-fructose
ECTree
Advanced search results
Cofactor
Cofactor on EC 1.1.99.28 - glucose-fructose oxidoreductase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
NADH
a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type
a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type
NAD+
S64D mutation converts the strict NADP+ specificity of wild-type GFOR to a dual NADP+/NAD+ specificity
NADP+
-
tightly bound as hydrogen carrier
NADP+
a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type
NADP+
-
in recombinant strains a precursor form of the enzyme accumulates that is enzymatically active and contains the cofactor NADPH/NADP+
NADP+
S64D mutation converts the strict NADP+ specificity of wild-type GFOR to a dual NADP+/NAD+ specificity
NADPH
-
tightly bound as hydrogen carrier
NADPH
a single site mutation S116D alters the enzyme which in the wild type situation contains NAD(P)+ as nondissociable redox cofactor reacting in a ping-pong type mechanism to a dehydrogenase with dissociable NAD(P)+ as cosubstrate and a sequential reaction type
NADPH
-
in recombinant strains a precursor form of the enzyme accumulates that is enzymatically active and contains the cofactor NAD(P)H/NAD(P)+