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1.14.13.8: flavin-containing monooxygenase

This is an abbreviated version!
For detailed information about flavin-containing monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.8

Reaction

Hypotaurine
+
H2O
 +
NAD+
=
taurine
 +
NADH
 +
H+

Synonyms

class 3 flavin-containing mono-oxygenase, class 3 FMO, dechlorinating flavin-dependent monooxygenase, dimethylaniline monooxygenase (N-oxide-forming), dimethylaniline monooxygenase [N-oxide-forming] 1, dimethylaniline N-oxidase, dimethylaniline oxidase, dimethylsulfone monooxygenase, DMA oxidase, EC 1.13.12.11, EC 1.8.1.3, EtaA, FAD-containing monooxygenase, FAD-containing monooxygenase 3, flavin containing monooxygenase 3, flavin mono-oxygenase, flavin monooxygenase, flavin-containing mono-oxygenase, flavin-containing monooxygenase, flavin-containing monooxygenase 1, flavin-containing monooxygenase 3, flavin-containing monooxygenase 5, flavin-containing monooxygenase-3, flavin-containing-monooxygenase, flavin-dependent monooxygenase, flavoprotein monooxygenase, FMO, FMO 1A1, FMO 1B1, FMO 1C1, FMO 1D1, FMO 1E1, FMO-E, FMO-I, FMO-II, FMO1, FMO2, FMO2.1, FMO3, FMO4, FMO5, FMOGS-OX6, FMOGS-OX7, HadA, hFMO1, hFMO3, hFMO5, Met S-oxidase, mFMO, mixed-function amine oxidase, monooxygenase FMO1, More, MymA, N,N-dimethylaniline monooxygenase, oxygenase, dimethylaniline mono- (N-oxide-forming), oxygenase, methylphenyltetrahydropyridine N-mono-, PtFMO, sfnG, TetX, type II flavin-containing monooxygenase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.8 flavin-containing monooxygenase

Crystallization

Crystallization on EC 1.14.13.8 - flavin-containing monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of enzyme and enzyme in complex with NADP+, and a mutant Y207S, which lacks indole oxygenation activity, with and without indole. The crystal structures reveal overlapping binding sites for NADP+ and indole, suggestive of a double-displacement reaction mechanism. NADPH induces conformational changes in two active site motifs. One of the motifs contains Arg229, which participates in interactions with the phosphate group of NADPH and appears be a determinant of the preferential binding to NADPH rather than NADH. The second motif contains Tyr207
mutant E158A/E159A, ligand-free or in complex with NADP+, microbatch technique at 4°C by mixing equal volumes of 8 mg of protein/ml in 25 mM Tris-HCl, pH 8.0, 250 mM NaCl, 1 mM NADP+, and of crystallization solution containing PEG 4000 20% w/v in 0.1 M Na/HEPES, pH 7.5, X-ray diffraction structure determination and analysis at 2.6-2.8 A resolution, molecular replacement
-
the crystal structure of mFMO that contains both cofactors, FAD and NADP+, is analyzed
-
purified recombinant enzyme in complex with FAD, and NADPH or methimazole, sitting drop vapor diffusion method, purified protein in 10 mM HEPES, pH 7.0, and 150 mM NaCl, versus reservoir solution containing 20% PEG 4000, 0.1 M sodium citrate buffer, pH 5.8, and 1,6-diaminohexane, cryoprotection by 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.1-2.4 A resolution