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Literature summary for 1.14.13.8 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

Activating Compound Comment Organism Structure
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
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
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
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
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
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)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
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

Inhibitors Comment Organism Structure
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
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
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
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
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P17635 isozyme FMO2
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
FMO
-
Oryctolagus cuniculus