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1.1.98.2: glucose-6-phosphate dehydrogenase (coenzyme-F420)

This is an abbreviated version!
For detailed information about glucose-6-phosphate dehydrogenase (coenzyme-F420), go to the full flat file.

Word Map on EC 1.1.98.2

Reaction

D-glucose 6-phosphate
+
oxidized coenzyme F420
=
6-phospho-D-glucono-1,5-lactone
+
reduced coenzyme F420

Synonyms

Rv0407, coenzyme F420-dependent glucose-6-phosphate dehydrogenase, EC 1.1.99.34, F420-dependent glucose-6-phosphate dehydrogenase, FGD, FGD1, glucose-6-phosphate dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.98 With other, known, physiological acceptors
                1.1.98.2 glucose-6-phosphate dehydrogenase (coenzyme-F420)

Crystallization

Crystallization on EC 1.1.98.2 - glucose-6-phosphate dehydrogenase (coenzyme-F420)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and selenomethionine-labeled FGD1, sitting drop vapour diffusion, mixing of protein solution in a 1:1 ratio with precipitant solution containing 1.6 M tri-sodium citrate, pH 6.5, microseeding, X-ray diffraction structure determination and analysis at 2.1 A resolution, multiwavelength anomalous diffraction
-
sitting drop vapour diffusion method, native and selenomethionine-labeled FGD1 are successfully crystallized by vapor diffusion, with the crystals diffracting to 2.1 A resolution
-
structure of the enzyme is determined by X-ray crystallography both in its apo state and in complex with F420 and citrate at resolutions of 1.90 and 1.95 A, respectively. The structure reveals a highly specific F420 binding mode, which is shared with several other F420-dependent enzymes. The competitive inhibitor citrate occupies the substrate binding pocket adjacent to F420. Modeling of the binding of the glucose 6-phosphate substrate identifies a positively charged phosphate binding pocket and shows that glucose 6-phosphate, like citrate, packs against the isoalloxazine moiety of F420 and helps promote a butterfly bend conformation that facilitates F420 reduction and catalysis