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Literature summary for 1.14.13.8 extracted from

  • Eswaramoorthy, S.; Bonanno, J.B.; Burley, S.K.; Swaminathan, S.
    Mechanism of action of a flavin-containing monooxygenase (2006), Proc. Natl. Acad. Sci. USA, 103, 9832-9837.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Schizosaccharomyces pombe

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Schizosaccharomyces pombe

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methimazole + NADPH + O2 Schizosaccharomyces pombe
-
?
-
?

Organism

Organism UniProt Comment Textmining
Schizosaccharomyces pombe Q9HFE4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3) Schizosaccharomyces pombe

Reaction

Reaction Comment Organism Reaction ID
N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O catalytic reaction mechanism via 4alpha-hydroperoxyflavin transient intermediate Schizosaccharomyces pombe

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Schizosaccharomyces pombe

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methimazole + NADPH + O2
-
Schizosaccharomyces pombe ?
-
?

Subunits

Subunits Comment Organism
More the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor Schizosaccharomyces pombe

Synonyms

Synonyms Comment Organism
FMO
-
Schizosaccharomyces pombe

Cofactor

Cofactor Comment Organism Structure
FAD the prosthetic group FAD is an integral part of the protein, the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, binding structure, overview Schizosaccharomyces pombe
NADPH dependent on, the active FMO exists in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, binding structure, overview Schizosaccharomyces pombe