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Literature summary extracted from

  • Krueger, S.K.; Siddens, L.K.; Henderson, M.C.; VanDyke, J.E.; Karplus, P.A.; Pereira, C.B.; Williams, D.E.
    C-terminal truncation of rabbit flavin-containing monooxygenase isoform 2 enhances solubility (2006), Arch. Biochem. Biophys., 450, 149-156.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.8 n-decyl-beta-D-maltoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-dodecyl-beta-D-maltoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-dodecyl-N,N-dimethylamine-n-oxide 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-nonyl-beta-D-glucoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-octyl-beta-D-glucoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-octyl-beta-D-thioglucoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.8 expression of N-terminally His6-tagged truncation mutant in Escherichia coli as soluble enzyme, and expression of the mutant in Spodoptera frugiperda Sf9 insect cells Oryctolagus cuniculus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.8 additional information C-terminal truncation of 26 amino acids and and a double Ser substitutio of isozyme FMO2 enhances the enzyme solubility and reduce hydrophobicity required for efficient enzyme crystallization, overview Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.8 n-decyl-beta-D-maltoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-dodecyl-beta-D-maltoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-dodecyl-N,N-dimethylamine-n-oxide 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-nonyl-beta-D-glucoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-octyl-beta-D-glucoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus
1.14.13.8 n-octyl-beta-D-thioglucoside 1%, activates at pH 7.5-8.5, inhibits at pH 9.5, mutant and wild-type enzymes Oryctolagus cuniculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.8 membrane associated Oryctolagus cuniculus 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.8 additional information Oryctolagus cuniculus the enzyme is involved in oxidative metabolism of drugs and other chemicals ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.8 Oryctolagus cuniculus P17635 isozyme FMO2
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.8 additional information the enzyme is involved in oxidative metabolism of drugs and other chemicals Oryctolagus cuniculus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.8 FMO
-
 Oryctolagus cuniculus