Cloned (Comment) | Organism |
---|---|
expression of wild-type enzyme and mutants M66I and R492W in Spodoptera frugiperda Sf9 cell membranes | Homo sapiens |
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Homo sapiens | 16020 | - |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
FMO3 | - |
Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Homo sapiens | |
NADPH | - |
Homo sapiens |