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1.5.1.36: flavin reductase (NADH)

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

Word Map on EC 1.5.1.36

Reaction

reduced flavin
+
NAD+
=
flavin
+
NADH
+
H+

Synonyms

AbeF, BaiH, BorF, C1-HpaH, DszD, FAD reductase, FerA, flavin mononucleotide reductase, flavin reductase, flavin:NADH oxidoreductase, FMN reductase, Frd188, frd2, fre, HpaC, LJ0548, LJ0549, LJ_0548, LJ_0549, LuxG, More, NAD(P)H-dependent H2O2-forming flavin reductase, NAD(P)H-flavin oxidoreductase, NAD(P)H:flavin oxidoreductase, NAD(P)H:flavin-oxidoreductase, NADH-dependent flavin reductase, NADH-flavin oxidoreductase, NADH: flavin oxidoreductase, NADH: flavinoxidore ductase/NADH oxidase, NADH:flavin oxidoreductase, NADH:FMN oxidoreductase, nfr1, nfr2, NOX, Pden2689, SMOB-ADP1

ECTree

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

Crystallization

Crystallization on EC 1.5.1.36 - flavin reductase (NADH)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
P3121 space group, to 2.9 A resolution. Each protomer of C1 contains one molecule of FMN in the nucleotide binding pocket. C1-HpaH undergoes a substantial conformational change in the presence of 4-hydroxyphenylacetic acid, concomitant with the increase in the rate of flavin reduction
purified recombinant enzyme in apoform or in complex with FMN, sitting drop vapour diffusion method, crystallization from 0.1 M HEPES, pH 7.4, 10% v/v 2-propanol, and 20% w/v PEG 4000, a few days at 20°C, method optimization, X-ray diffraction structure determination and analysis at 1.53-1.85 A resolution, small angle X-ray scattering, molecular replacement method using structure PDB ID 1RZ0 as search model
complexed with FMN, FAD or riboflavin, sitting drop vapor diffusion method, using 1.6 M ammonium sulfate and 4-5% (v/v) isopropanol
-