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Literature summary extracted from

  • Bashiri, G.; Squire, C.J.; Moreland, N.J.; Baker, E.N.
    Crystal structures of F420-dependent glucose-6-phosphate dehydrogenase FGD1 involved in the activation of the anti-tuberculosis drug candidate PA-824 reveal the basis of coenzyme and substrate binding (2008), J. Biol. Chem., 283, 17531-17541.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.98.2
-
 Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.98.2 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 Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.98.2 citrate competitive Mycobacterium tuberculosis

Organism

EC Number Organism UniProt Comment Textmining
1.1.98.2 Mycobacterium tuberculosis P9WNE1
-
-
1.1.98.2 Mycobacterium tuberculosis H37Rv P9WNE1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.98.2
-
 Mycobacterium tuberculosis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
1.1.98.2 0.043
-
-
 Mycobacterium tuberculosis citrate