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1.5.1.30: flavin reductase (NADPH)

This is an abbreviated version!
For detailed information about flavin reductase (NADPH), go to the full flat file.

Word Map on EC 1.5.1.30

Reaction

reduced riboflavin
+
NADP+
=
riboflavin
+
NADPH
+
H+

Synonyms

alkanesulfonate FMN reductase, ArsH, azoreductase, AZRü, biliverdin IXbeta reductase, biliverdin reductase B, biliverdin reductase-B, Biliverdin-IX beta-reductase, BLVRB, CysJ, EC 1.6.8.2, FAD-dependent NADP-reductase, flavin oxidoreductase, flavin reductase, flavin reductase 1, flavin reductase Nr1, flavin reductase P, FLR, FR1, Frb, Frd188, frd2, fre, Fre oxidoreductase, Fre-1, FRG/FRaseI, FRGvf, FRP, FRPvh, GHBP, Green heme binding protein, HpaC, ipa-43d, LuxG, More, NAD(P)H-dependent H2O2-forming flavin reductase, NAD(P)H:flavin-oxidoreductase, NADPH-dependant FMN reductase, NADPH-dependent diaphorase, NADPH-flavin oxidoreductase, NADPH-flavin reductase, NADPH-FMN oxidoreductase, NADPH-FMN reductase, NADPH-nitrofurazone reductase, NADPH-specific flavin reductase, NADPH:FAD oxidoreductase, NADPH:flavin oxidoreductase, NADPH:FMN oxidoreductase, NfrA1, nitro/flavin reductase, non-luminescent-bacterial NfsA/Frp-type enzyme, SsuE, TVAG_517010

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.1 With NAD+ or NADP+ as acceptor
                1.5.1.30 flavin reductase (NADPH)

Renatured

Renatured on EC 1.5.1.30 - flavin reductase (NADPH)

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
soluble denatured mutant enzyme E99K is mixed into 50fold volume of pre-cooled 50 mM phosphate buffer containing 0.1 M FMN and stirred on ice in the dark for 15 min for protein renaturation and the reconstitution of E99K holoenzyme
-
the recombinant FlaR is insoluble under physiological conditions and its purification can be obtained under denaturing conditions in buffer supplemented with 8 M urea. Different refolding conditions are tested for their ability to renature the protein. Dialysis of the denatured protein against buffers at different pH levels reveals that rFlaR can be solubilized at below pH 8.0. The presence of cysteine-rich sequence suggests that the protein has a transitional metal-binding ability. Thus, rFlaR is dialyzed against PBS (pH 7.3) supplemented with 2 mM salts of either transition metal or calcium and magnesium (2 mM of each). rFlaR becomes fully soluble in the presence of 2 mM FeSO4. Partial solubility can be obtained in the presence of 2 mM CoCl2 or CuSO4