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Literature summary for 1.14.13.8 extracted from

  • Lickteig, A.J.; Riley, R.; Melton, R.J.; Reitz, B.A.; Fischer, H.D.; Stevens, J.C.
    Expression and characterization of functional dog flavin-containing monooxygenase 3 (2009), Drug Metab. Dispos., 37, 1987-1990.
    View publication on PubMed
Search for more literature for 1.14.13.8

Cloned(Commentary)

Cloned (Comment) Organism
FMO3 cDNA from liver, DNA and amino acid sequence determination and analysis, expression in Spodoptera frugiperda Sf9 insect cells Canis lupus familiaris
FMO3 cDNA from liver, expression in Spodoptera frugiperda Sf9 insect cells Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information the recombinant enzyme exhibits Michaelis-Menten kinetics Canis lupus familiaris
additional information
-
 additional information the recombinant enzyme exhibuts Michaelis-Menten kinetics Homo sapiens
0.0186
-
 Benzydamine pH 7.4, 37°C Canis lupus familiaris
0.0426
-
 Benzydamine pH 7.4, 37°C Homo sapiens
0.0693
-
 sulindac pH 9.0, 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Homo sapiens
-
-
microsome
-
 Canis lupus familiaris
-
-

Organism

Organism UniProt Comment Textmining
Canis lupus familiaris
-
 female and male beagle dogs
-
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Homo sapiens
-
liver
-
 Canis lupus familiaris
-
lung
-
 Homo sapiens
-
lung
-
 Canis lupus familiaris
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0000163
-
 male dog liver microsomes, substrate benzydamine Canis lupus familiaris
0.0000367
-
 female dog liver microsomes, substrate benzydamine Canis lupus familiaris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzydamine + NADPH + H+ + O2 N-oxidation Homo sapiens benzydamine N-oxide + NADP+ + H2O
-
 ?
benzydamine + NADPH + H+ + O2 N-oxidation Canis lupus familiaris benzydamine N-oxide + NADP+ + H2O
-
 ?
clozapine + NADPH + H+ + O2 N-oxidation Homo sapiens clozapine N-oxide + NADP+ + H2O
-
 ?
clozapine + NADPH + H+ + O2 N-oxidation Canis lupus familiaris clozapine N-oxide + NADP+ + H2O
-
 ?
sulindac sulfide + NADPH + H+ + O2 S-oxidation Homo sapiens sulindac + NADP+ + H2O
-
 ?
sulindac sulfide + NADPH + H+ + O2 S-oxidation, low activity Canis lupus familiaris sulindac + NADP+ + H2O
-
 ?

Synonyms

Synonyms Comment Organism
FMO3
-
 Homo sapiens
FMO3
-
 Canis lupus familiaris

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens
37
-
 assay at Canis lupus familiaris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4 9 assay pH depends on the substrate Homo sapiens
7.4 9 assay pH depends on the substrate Canis lupus familiaris

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Homo sapiens
FAD
-
 Canis lupus familiaris
NADPH
-
 Homo sapiens
NADPH
-
 Canis lupus familiaris

General Information

General Information Comment Organism
physiological function FMO catalyzes the oxidation at nucleophilic, heteroatom centers and is important for drug, xenobiotic, and endogenous substrate metabolism Homo sapiens
physiological function FMO catalyzes the oxidation at nucleophilic, heteroatom centers and is important for drug, xenobiotic, and endogenous substrate metabolism Canis lupus familiaris