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.

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

     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

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Results	in table
2	Activating Compound
1851	AA Sequence
4	Application
1	CAS Registry Number
6	Cloned(Commentary)
37	Cofactor
4	Crystallization (Commentary)
2	Disease/ Diagnostics
2	General Information
12	General Stability
5	Inhibitors
5	KM Value [mM]
17	Localization
7	Molecular Weight [Da]
23	Natural Substrates/ Products (Substrates)
63	Organism
1	Pathway
30	PDB ID
6	pH Optimum
3	pH Range
2	pH Stability
2	Posttranslational Modification
10	Protein Variants
7	Purification (Commentary)
3	Reaction
2	Reaction Type
42	Reference
2	Source Tissue
7	Specific Activity [micromol/min/mg]
57	Substrates and Products (Substrate)
9	Subunits
35	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
2	Temperature Range [°C]
5	Temperature Stability [°C]
5	Turnover Number [1/s]

General Stability

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General Stability on EC 1.1.99.28 - glucose-fructose oxidoreductase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

enzyme activity loss in pineapple juice is even stronger (18%) than in 0.5 M sugar solution

Zymomonas mobilis

-

724873

glucose-fructose oxidoreductase (GFOR)/glucono-delta-lactonase (GL) enzyme complex immobilized on Ca-alginate is stable for at least 23 cycles

Zymomonas mobilis

Q07982

762807

guanidinium hydrochloride inactivates by induction of structural transitions that are comparable to that observed during substrate turnover. This leads to time-dependent formation of high-order associates and consequently inactivation

Zymomonas mobilis

-

10909

in absence of substrates or in presence of only one substrate, either fructose or glucose, the enzyme is fully stable

Zymomonas mobilis

-

10908

inactivation during substrate conversion

Zymomonas mobilis

-

10911, 10912

inactivation during substrate turnover. The process of inactivation is triggered by structural transitions that are induced by the lactone product and involves aggregation as the ultimate cause of irreversible inactivation

Zymomonas mobilis

-

10909

the interaction of the enzyme with the aldonolactone product triggers a sequential process that affects the protein structure conformationally and chemically and, ultimately, results in an irreversible loss of activity

Zymomonas mobilis

-

10903

thiol reagents stabilize. Dithiothreitol is the most efficient, 5-15 mM

Zymomonas mobilis

-

10908, 10911, 10912

urea, 1.0 M, prevents the formation of high-order associates and increases the half-life under operational conditions 10fold

Zymomonas mobilis

-

10909