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Literature summary for 1.14.13.8 extracted from

  • Yeung, C.K.; Adman, E.T.; Rettie, A.E.
    Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria (2007), Arch. Biochem. Biophys., 464, 251-259.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.8

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type enzyme and mutants M66I and R492W in Spodoptera frugiperda Sf9 cell membranes Homo sapiens

Protein Variants

Protein Variants Comment Organism
E158K naturally occuring mutation not involved in primary trimethylaminuria Homo sapiens
E158K/E308G naturally occuring mutation not involved in primary trimethylaminuria Homo sapiens
E308G naturally occuring mutation not involved in primary trimethylaminuria Homo sapiens
M66I naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor Homo sapiens
N61S naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme Homo sapiens
P153L naturally occuring mutation involved in trimethylaminuria, the mutant shows over 90% reduced activity with trimethylamine compared to the wild-type enzyme Homo sapiens
R492W naturally occuring mutation involved in trimethylaminuria, the mutant fails to incorporate/retain the FAD cofactor Homo sapiens
V257M naturally occuring mutation not involved in primary trimethylaminuria Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Homo sapiens 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
trimethylamine + NADPH + H+ + O2 Homo sapiens mutations of FMO3 are involved in trimethylaminuria, primary trimethylaminuria is multifactorial in origin in that enzyme dysfunction can result from kinetic incompetencies as well as impaired assembly of holoprotein, overview trimethylamine N-oxide + NADP+ + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
trimethylamine + NADPH + H+ + O2
-
 Homo sapiens trimethylamine N-oxide + NADP+ + H2O
-
 ?
trimethylamine + NADPH + H+ + O2 mutations of FMO3 are involved in trimethylaminuria, primary trimethylaminuria is multifactorial in origin in that enzyme dysfunction can result from kinetic incompetencies as well as impaired assembly of holoprotein, overview Homo sapiens trimethylamine N-oxide + NADP+ + H2O
-
 ?

Subunits

Subunits Comment Organism
More structure homology model for FMO3 based on the crystal structure for yeast FMO with N61 in close proximity to the FAD catalytic center, in contrast to residues M66, P153, R492, E158, V257, and E308, overview Homo sapiens

Synonyms

Synonyms Comment Organism
FMO3
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Homo sapiens
NADPH
-
 Homo sapiens