Use of thiocarbamides as selective substrate probes for isoforms of flavin-containing monooxygenases
References (21)
Flavin-containing monooxygenases: Enzymes adapted for multisubstrate specificity
Trends Pharmacol Sci
(1990)- et al.
Identification of distinct hepatic and pulmonary forms of microsomal flavin-containing monooxygenase in the mouse and rabbit
Biochem Biophys Res Commun
(1985) Liver microsomes contain two distinct NADPH-monooxygenases with NH2-terminal segments homologous to the flavin containing NADPH monoxygenase of Pseudomonas fluorescens
Biochem Biophys Res Commun
(1989)- et al.
The flavin-containing monooxygenase enzymes expressed in rabbit liver and lung are products of related but distinctly different genes
J Biol Chem
(1990) - et al.
Multiplicity of liver microsomal flavin-containing monooxygenase in the guinea pig: Its purification and characterization
Arch Biochem Biophys
(1990) - et al.
The liver microsomal FAD-containing monooxygenase
J Biol Chem
(1979) - et al.
The reductive half-reaction of liver microsomal FAD-containing monooxygenase
J Biol Chem
(1981) - et al.
The oxidative half-reaction of liver microsomal FAD-containing monooxygenase
J Biol Chem
(1981) - et al.
Studies on substrate specificity of the hog liver flavin-containing mono-oxygenase: Anionic organic sulfur compounds
Biochem Pharmacol
(1987) - et al.
Hepatic microsomal mixed-function amine oxidase
Methods Enzymol
(1978)
Cited by (37)
Characterization of mouse flavin-containing monooxygenase transcript levels in lung and liver, and activity of expressed isoforms
2008, Biochemical PharmacologyCitation Excerpt :Although oxygenation usually represents a detoxication reaction, some FMO-oxygenated sulfur substrates, such as thioureas, produce reactive sulfenic or sulfinic acids as major metabolites. Sulfenic acid metabolites can react with GSH inducing oxidative stress through a futile redox cycle [2–5]. Humans have five FMO genes (FMO1-5) and six pseudogenes (FMO6P-11P) [6–8], while mice have nine FMO genes (Fmo1-6, 9, 12 and 13) [7].
C-terminal truncation of rabbit flavin-containing monooxygenase isoform 2 enhances solubility
2006, Archives of Biochemistry and BiophysicsMammalian flavin-containing monooxygenases: Structure/function, genetic polymorphisms and role in drug metabolism
2005, Pharmacology and TherapeuticsCitation Excerpt :The lack of activity of rabbit FMO2 toward imipramine and chlorpromazine are consistent with this model. Thioureas of various sizes have been used to demonstrate the existence of multiple FMO enzymes in various tissues (Nagata et al., 1990; Guo et al., 1992; Shehin-Johnson et al., 1995; Kim & Ziegler, 2000). The activity of rabbit FMO2 toward alkyl 2-naphthyl sulfides of increasing chain length confirm this restricted substrate access channel in FMO2 (Fisher & Rettie, 1997).
Thiourea toxicity in mouse C3H/10T1/2 cells expressing human flavin-dependent monooxygenase 3
2002, Biochemical PharmacologyCitation Excerpt :The thiocarbamate specificity of FMO was originally delineated by the ability of a spectrum of these compounds to support NADPH oxidation in the presence of purified FMO 1 [22]. In this and subsequent studies, it was shown that the kinetic characteristics for TU (Vmax=1180 nmol/min/mg, Km=4 μM) were similar to ETU (Vmax=1060 nmol/min/mg, Km=99 μM), and PTU and ANTU [15,26]. When ETU was tested for cytotoxicity on parental and FMO 3 clone 7, it proved negative over a concentration range of 10−6 to 10−3 M.