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
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1.1.98.2
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mycobacteria
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tuberculosis
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smegmatis
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archaea
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bovis
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6-phosphogluconolactone
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hydride
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pretomanid
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leprae
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prodrug
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citrate
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nadp-dependent
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methanogenic
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5-deazaflavin
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medicine
- 1.1.98.2
- mycobacteria
- tuberculosis
- smegmatis
- archaea
- bovis
- 6-phosphogluconolactone
-
hydride
-
pretomanid
- leprae
-
prodrug
- citrate
-
nadp-dependent
-
methanogenic
- 5-deazaflavin
- medicine
Reaction
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
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Crystallization
Crystallization on EC 1.1.98.2 - glucose-6-phosphate dehydrogenase (coenzyme-F420)
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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
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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
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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