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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

Reaction

D-glucose
+
D-fructose
=
D-gluconolactone
+
D-glucitol

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

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.99 With unknown physiological acceptors
                1.1.99.28 glucose-fructose oxidoreductase

Engineering

Engineering on EC 1.1.99.28 - glucose-fructose oxidoreductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTA1-22/S64D
S64D mutation converts the strict NADP+ spoecificity of wild-type GFOR to a dual NADP+/NAD+ specificity
DELTA32-46
-
the mutant enzyme DELTA32-46 is a protein that is no longer processed but shows full enzymatic activity and has the cofactor firmly bound. The mutant enzyme DELTA2-20 or a mutant enzyme with an exchange of the entire signal sequence with the signal sequence of gluconolactonase of Zymomonas mobilis leads to an active and processed protein
K121A
-
mutant enzyme is not processed within 60 min
K123A
-
mutant enzyme shows processing behavior comparable to wild-type enzyme
S116D
S116D/K121A/K123Q/I124K
-
significantly retarded processing kinetics with residual unprocessed form being detectable even after 60 min
Y269F
essential acid-base catalyst, involved in substrate binding, activity completely abolished
additional information
-
mutant enzymes with deletions in the signal peptide are enzymatically active and contain tightly bound NADP(H). Mutant enzymes with a complete deletion of the signal peptide are produced as cytosolic enzymes