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Key Documents

F5053

Sigma-Aldrich

Flavin-Containing Monooxygenase-3, Microsomes human

recombinant, expressed in baculovirus infected insect cells, buffered aqueous solution

Synonym(s):

FMO-3

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About This Item

Enzyme Commission number:
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in baculovirus infected insect cells

Quality Level

form

buffered aqueous solution

mol wt

55-60 kDa

packaging

vial of 2.5 mg

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... FMO3(2328)

General description

Flavin-Containing Monooxygenase-3 (FMO3) is a member of the flavin-containing monooxygenase (FMO) family of enzymes. It is highly expressed in the human liver.

Application

FMO3 is the major human hepatic form.

Biochem/physiol Actions

Flavin-Containing Monooxygenase-3 (FMO3) facilitates the oxidization of several drugs, chemicals, and xenobiotics. Human FMO3 is also involved in the synthesis of N-oxide of trimethylamine (TMAO) from trimethylamine (TMA). Mutations in the FMO3 gene are associated with trimethylaminuria or fish odor syndrome. Deficiency of the FMO3 gene results in lower plasma TMAO levels, which may reduce the risk of developing atherosclerosis and thrombosis.

Physical form

Solution in 100 mM potassium phosphate buffer, pH 7.4

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Robert R Reddy et al.
Drug metabolism and disposition: the biological fate of chemicals, 38(12), 2239-2245 (2010-09-03)
The flavin-containing monooxygenase (FMO) family of enzymes oxygenates nucleophilic xenobiotics and endogenous substances. Human FMO3 and FMO5 are the predominant FMO forms in adult liver. These enzymes are naturally membrane-bound, and recombinant proteins are commercially available as microsomal preparations from

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