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]

Crystallization

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Crystallization on EC 1.1.99.28 - glucose-fructose oxidoreductase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Zymomonas mobilis

-

10915

hanging drop method, crystal structure of oxidized preGFOR R30K/R31K, in complex with succinate (preGFOR(succ)) and with glycerol (PreGFOR(gll)), at 2.2 A and 2.05 A resolution, respectively, and of reduced preGFOR R30K/R31K, after incubation with glucose (preGFOR(Glu)) and with sorbitol (preGFOR(sorb)) at 2.5 A and 2.6 A resolution. In all four crystal structures, the signal peptide is disordered, implying a flexibility that may be important for its interaction with the translocation apparatus. The crystal structures show that the mature enzyme portion of preGFOR is identical to native GFOR, in structure and cofactor binding

Zymomonas mobilis

-

654586

structure at 2.7 A

Zymomonas mobilis

-

10914

vapour diffusion in hanging drops, crystal structure of the NAD+ complex of a truncated form of the enzyme, GFORDELTA1-22/S64D, in which the first 22 residues of the N-terminal arm of the mature protein have been deleted, structure refined at 2.7 A resolution shows that the truncated form of the enzyme forms a dimer and implies that the N-terminal arm is essential for tetramer formation by wild-type GFOR

Zymomonas mobilis

Q07982

656483