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
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1.1.99.28
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zymomonas
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mobilis
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sorbitol
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gluconic
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lactobionic
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nadp-containing
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gluconolactonase
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d-xylose
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1,5-anhydro-d-fructose
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synthesis
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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
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Engineering
Engineering on EC 1.1.99.28 - glucose-fructose oxidoreductase
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DELTA1-22/S64D
S64D mutation converts the strict NADP+ spoecificity of wild-type GFOR to a dual NADP+/NAD+ specificity
DELTA32-46
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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
K123A
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mutant enzyme shows processing behavior comparable to wild-type enzyme
S116D
S116D/K121A/K123Q/I124K
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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
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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
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
S116D
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significantly retarded processing kinetics with residual unprocessed form being detectable even after 60 min
S116D
dual NADP+/NAD+ specificity with loss of tight cofactor binding, wild type: strict NADP+ specificity