Multiplicity of liver microsomal flavin-containing monooxygenase in the guinea pig: Its purification and characterization

Yamada, Hideyuki; Yuno, Koichiro; Oguri, Kazuta; Yoshimura, Hidetoshi

doi:10.1016/0003-9861(90)90334-u

Cited by 35 publications

(16 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, form I FMO activity is stimulated by primary aliphatic alkylamines, and form I FMO catalyzes the N-oxygenation of secondary and tertiary amines (1). In contrast, form II FMO N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines (10). Some aliphatic tertiary amines, such as chlorpromazine, are preferentially N-oxygenated by form II FMO (10).…”

mentioning

confidence: 99%

“…In contrast, form II FMO N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines (10). Some aliphatic tertiary amines, such as chlorpromazine, are preferentially N-oxygenated by form II FMO (10).…”

mentioning

confidence: 99%

“…In animals, FMO is present as at least one pulmonary form (8,9) and as two or more hepatic forms (e.g., forms I and II) (10,11). In rabbit liver, form I and form II are 54% identical to one another, but the amino acid sequence similarity between hog liver FMO and rabbit liver FMO form I is -90% .…”

mentioning

confidence: 99%

See 2 more Smart Citations

Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.

Lomri

Cashman

1992

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.

Lomri

Cashman

1992

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…From the dimensions of the substrates examined (Table 11) it would appear that the active site hydroperoxyflavin of HLFMO-D is about [5][6][7] A below the surface of a narrow channel. The postulated dimensions of the substrate binding channel provide a structural basis as to why detectable amounts of imipramine N-oxide was not observed to be formed in the presence of human liver microsomes (16).…”

Section: Discussionmentioning

confidence: 99%

Expression in Escherichia coli of the flavin-containing monooxygenase D (form II) from adult human liver: Determination of a distinct tertiary amine substrate specificity

Lomri

Yang²,

Cashman³

1993

Chem. Res. Toxicol.

View full text Add to dashboard Cite

The cDNA for a major component of the family of flavin-containing monooxygenases (FMOs) present in adult human liver (i.e., HLFMO-D) has been cloned and expressed in a prokaryotic system. Escherichia coli strain NM522 was transformed with pTrcHLFMO-D, and the HLFMO-D cDNA was expressed under the control of the Trc promoter. A variety of tertiary amine substrates [i.e., chlorpromazine and 10-[(N,N-dimethylamino)alkyl]- 2-(trifluoromethyl)phenothiazines] were efficiently oxygenated by HLFMO-D cDNA expressed in E. coli or by adult human liver microsomes. Approximate dimensions of the substrate binding channel for both adult human liver microsomal FMO and cDNA-expressed HLFMO-D were apparent from an examination of the N-oxygenation of a series of 10-[(N,N-dimethylamino)alkyl]-2-(trifluoromethyl)phenothiazines. The substrate regioselectivity studies suggest that adult human liver FMO form D possesses a distinct substrate specificity compared with form A FMO from animal hepatic sources. It is likely that the substrate specificity observed for cDNA-expressed adult human liver FMO-D may have consequences for the metabolism and distribution of tertiary amines and phosphorus- and sulfur-containing drugs in humans and may provide insight into the physiologic substrate(s) for adult human liver FMO.

show abstract

“…1,2) The proteins and cDNAs of FMO have been isolated from several mammalian species including humans. [3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21] Based on the sequence similarity, mammalian FMOs are classied intoˆve isoforms (FMO1-FMO5). 22) Human FMO3 is considered as a major form in adult livers, while human FMO1 is detectable in the kidney and fetal livers, but not in adult livers.…”

Section: Introductionmentioning

confidence: 99%

A Mutation in the Flavin-containing Monooxygenase 3 Gene and its Effects on Catalytic Activity for N-oxidation of Trimethylamine In Vitro

Kubota

Nakamoto

Nakayama

et al. 2002

Drug Metabolism and Pharmacokinetics

View full text Add to dashboard Cite

To clarify the mutation of the flavin-containing monooxygenase (FMO) 3 gene causing fish-odor syndrome, we analyzed the FMO3 gene of a Thai subject who possibly suffered from fish-odor syndrome. A novel mutation, a single-base substitution from G to A at the position of 265 (G265A), was identified in exon 3. The mutation caused an amino acid substitution from valine to isoleucine at residue 58 (V58I). The mutated FMO3 protein with V58I exhibited the reduced trimethylamine N-oxidase activity when it was expressed in E. coli. The V(max)/K(m) value for the activity of the mutant-type FMO3 was about 5 times lower than that for the wild-type FMO3.

show abstract

Multiplicity of liver microsomal flavin-containing monooxygenase in the guinea pig: Its purification and characterization

Cited by 35 publications

References 32 publications

Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.

Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver.

Expression in Escherichia coli of the flavin-containing monooxygenase D (form II) from adult human liver: Determination of a distinct tertiary amine substrate specificity

A Mutation in the Flavin-containing Monooxygenase 3 Gene and its Effects on Catalytic Activity for N-oxidation of Trimethylamine In Vitro

Contact Info

Product

Resources

About