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Literature summary extracted from
- Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism (2005), Pharmacol. Ther., 106, 357-387.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.8 | additional information | FMO is not induced by xenobiotics | Homo sapiens |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.13.8 | genes FMO1-FMO6, FMO6 is a pseudogene, the genes are organized in two clusters chromosome 1, one of which resides on the long arm of chromosome 1 at q23 25, the second cluster is composed of 3 genes, that are not pseudogenes | Mus musculus |
| 1.14.13.8 | genes FMO1-FMO6, FMO6 is a pseudogene, the genes are organized in two clusters chromosome 1, one of which resides on the long arm of chromosome 1 at q23 25, the second cluster is composed of 5 pseudogenes | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.13.8 | D132H | natural genetic variant of isozyme FMO2, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | E132H | natural genetic variant of isozyme FMO2, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | E132H/E158K | natural genetic variant of isozyme FMO2, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | E158K | natural genetic variant of isozymes FMO2 and FMO3, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | E158K/E308G | natural genetic variant of isozyme FMO2, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | E308G | natural genetic variant of isozyme FMO2, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | F510X | natural genetic variant of isozyme FMO2, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | H97Q | natural genetic variant of isozyme FMO1, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | I303T | natural genetic variant of isozyme FMO1, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | I303V | natural genetic variant of isozyme FMO1, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | L360P | natural genetic variant of isozyme FMO2, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | additional information | three of the five expressed human FMO genes, FMO1, FMO2 and FMO3, exhibit genetic polymorphisms, overview | Homo sapiens |
| 1.14.13.8 | R502X | natural genetic variant of isozyme FMO1, substrate specificity, overview | Homo sapiens |
| 1.14.13.8 | V257M | natural genetic variant of isozyme FMO3, substrate specificity, overview | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.8 | additional information | the lung isozyme is resistant to detergent inhibition | Oryctolagus cuniculus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.13.8 | additional information | - |
additional information | - |
Homo sapiens | |
| 1.14.13.8 | additional information | - |
additional information | - |
Sus scrofa | |
| 1.14.13.8 | additional information | - |
additional information | - |
Oryctolagus cuniculus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.13.8 | microsome | - |
Homo sapiens | - |
- |
| 1.14.13.8 | microsome | - |
Sus scrofa | - |
- |
| 1.14.13.8 | microsome | - |
Oryctolagus cuniculus | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.8 | 10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2 | Homo sapiens | - |
10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O | - |
? |  |
| 1.14.13.8 | amphetamine + NADPH + O2 | Homo sapiens | - |
amphetamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | cysteamine + NADPH + O2 | Mus musculus | - |
cysteamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | cysteamine + NADPH + O2 | Homo sapiens | - |
cysteamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | cysteamine + NADPH + O2 | Sus scrofa | - |
cysteamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | cysteamine + NADPH + O2 | Oryctolagus cuniculus | - |
cysteamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | dihydrolipoic acid + NADPH + O2 | Sus scrofa | - |
? | - |
? | |
| 1.14.13.8 | fenthion + NADPH + O2 | Homo sapiens | - |
fenthion sulfoxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | imipramine + NADPH + O2 | Homo sapiens | - |
? | - |
? | |
| 1.14.13.8 | L-methionine + NADPH + O2 | Homo sapiens | - |
L-methionine S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | L-methionine + NADPH + O2 | Sus scrofa | - |
L-methionine S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | L-methionine + NADPH + O2 | Oryctolagus cuniculus | - |
L-methionine S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | lipoic acid + NADPH + O2 | Homo sapiens | - |
? | - |
? | |
| 1.14.13.8 | lipoic acid + NADPH + O2 | Sus scrofa | - |
? | - |
? | |
| 1.14.13.8 | methimazole + NADPH + O2 | Homo sapiens | - |
? | - |
? | |
| 1.14.13.8 | methyl 4-tolyl sulfide + NADPH + O2 | Homo sapiens | - |
methyl 4-tolyl sulfoxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | additional information | Homo sapiens | nitrogen- and sulfur-containing endogenous substrates and physiologic functions, FMO is not induced by xenobiotics, isozyme FMO3 mutant alleles contribute to the disease known as trimethylaminuria, the enzyme is involved in detoxification and drug metabolism, overview, expression of FMO5 is markedly down-regulated in the liver of humans with type II diabetes, patients diagnosed with atrial fibrillation document a significant increase in the expression of FMO1, FMO may be associated with sideroblastic anemia, FMO3 mutations lead to trimethylaminuria, detailed overview | ? | - |
? | |
| 1.14.13.8 | additional information | Sus scrofa | nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview | ? | - |
? | |
| 1.14.13.8 | additional information | Oryctolagus cuniculus | nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview | ? | - |
? | |
| 1.14.13.8 | additional information | Mus musculus | nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview, hepatic total FMO activity is enhanced in mouse models of type I and type II diabetes | ? | - |
? | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + O2 | Mus musculus | - |
N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + O2 | Homo sapiens | - |
N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + O2 | Sus scrofa | - |
N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + O2 | Oryctolagus cuniculus | - |
N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | phenethylamine + NADPH + O2 | Homo sapiens | isozyme FMO3 | phenethylamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | ranitidine + NADPH + O2 | Homo sapiens | - |
? | - |
? | |
| 1.14.13.8 | S-farnesylcysteine + NADPH + O2 | Sus scrofa | - |
S-farnesylcysteine S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | S-farnesylcysteine methyl ester + NADPH + O2 | Sus scrofa | - |
? | - |
? | |
| 1.14.13.8 | trimethylamine + NADPH + O2 | Mus musculus | - |
trimethylamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | trimethylamine + NADPH + O2 | Homo sapiens | - |
trimethylamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | trimethylamine + NADPH + O2 | Sus scrofa | - |
trimethylamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | tyramine + NADPH + O2 | Homo sapiens | - |
tyramine N-oxide + NADP+ + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.13.8 | Homo sapiens | - |
genes FMO1-FMO6, FMO6 is a pseudogene | - |
| 1.14.13.8 | Mus musculus | - |
- |
- |
| 1.14.13.8 | Oryctolagus cuniculus | - |
tissue-specific isozymes | - |
| 1.14.13.8 | Sus scrofa | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.13.8 | from liver microsomes | Sus scrofa |
| 1.14.13.8 | isozyme from lung microsomes | Oryctolagus cuniculus |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.13.8 | N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O | catalytic cycle and catalytic reaction mechanism, structure-function relationship, FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, substrate binding has no effect on velocity, formation of a peroxyflavin intermediate | Mus musculus | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O | catalytic cycle and catalytic reaction mechanism, structure-function relationship, FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, substrate binding has no effect on velocity, formation of a peroxyflavin intermediate | Homo sapiens | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O | catalytic cycle and catalytic reaction mechanism, structure-function relationship, FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, substrate binding has no effect on velocity, formation of a peroxyflavin intermediate | Sus scrofa | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O | catalytic cycle and catalytic reaction mechanism, structure-function relationship, FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, substrate binding has no effect on velocity, formation of a peroxyflavin intermediate | Oryctolagus cuniculus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.13.8 | brain | - |
Homo sapiens | - |
| 1.14.13.8 | liver | - |
Mus musculus | - |
| 1.14.13.8 | liver | - |
Oryctolagus cuniculus | - |
| 1.14.13.8 | liver | isozyme FMO1 | Sus scrofa | - |
| 1.14.13.8 | liver | isozyme FMO3 | Homo sapiens | - |
| 1.14.13.8 | lung | isozyme FMO2 | Homo sapiens | - |
| 1.14.13.8 | lung | lung isozyme FMO2 | Oryctolagus cuniculus | - |
| 1.14.13.8 | additional information | the lung isozyme FMO2 is distinct from the liver isozyme in having high activity toward primary alkyl amines, restricted substrate specificity related to steric properties, resistance to detergent inhibition and enhanced thermal stability | Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.13.8 | 10-(N,N-dimethylaminoalkyl)-2-(trifluoromethyl) phenothiazines + NADPH + O2 | with the alkyl side chain varying in length from 2 to 7 carbons, liver isozyme FMO1 | Sus scrofa | ? | - |
? | |
| 1.14.13.8 | 10-(N,N-dimethylaminoalkyl)-2-(trifluoromethyl) phenothiazines + NADPH + O2 | with the alkyl side chain varying in length from 5 to 7 carbons, no activity with shorter side chains by isozyme FMO2 | Oryctolagus cuniculus | ? | - |
? | |
| 1.14.13.8 | 10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2 | - |
Homo sapiens | 10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | 10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine + NADPH + O2 | formation of the cis-oxime | Homo sapiens | 10-N-(n-octylamino)-2-(trifluoromethyl) phenothiazine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | amphetamine + NADPH + O2 | - |
Homo sapiens | amphetamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | chlorpromazine + NADPH + O2 | liver isozyme FMO1 | Sus scrofa | ? | - |
? | |
| 1.14.13.8 | cysteamine + NADPH + O2 | - |
Mus musculus | cysteamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | cysteamine + NADPH + O2 | - |
Homo sapiens | cysteamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | cysteamine + NADPH + O2 | - |
Sus scrofa | cysteamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | cysteamine + NADPH + O2 | - |
Oryctolagus cuniculus | cysteamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | dihydrolipoic acid + NADPH + O2 | - |
Sus scrofa | ? | - |
? | |
| 1.14.13.8 | fenthion + NADPH + O2 | - |
Homo sapiens | fenthion sulfoxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | fenthion + NADPH + O2 | i.e. O,O-dimethyl O-4-methylthio-m-tolyl phosphorothioate, isozymes FMO1 and FMO3, stereospecifc product formation, overview | Homo sapiens | fenthion sulfoxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | imipramine + NADPH + O2 | - |
Homo sapiens | ? | - |
? | |
| 1.14.13.8 | imipramine + NADPH + O2 | liver isozyme FMO1 | Sus scrofa | ? | - |
? | |
| 1.14.13.8 | L-methionine + NADPH + O2 | - |
Homo sapiens | L-methionine S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | L-methionine + NADPH + O2 | - |
Sus scrofa | L-methionine S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | L-methionine + NADPH + O2 | - |
Oryctolagus cuniculus | L-methionine S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | lipoic acid + NADPH + O2 | - |
Homo sapiens | ? | - |
? | |
| 1.14.13.8 | lipoic acid + NADPH + O2 | - |
Sus scrofa | ? | - |
? | |
| 1.14.13.8 | methimazole + NADPH + O2 | - |
Homo sapiens | ? | - |
? | |
| 1.14.13.8 | methyl 4-tolyl sulfide + NADPH + O2 | - |
Homo sapiens | methyl 4-tolyl sulfoxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | additional information | nitrogen- and sulfur-containing endogenous substrates and physiologic functions, FMO is not induced by xenobiotics, isozyme FMO3 mutant alleles contribute to the disease known as trimethylaminuria, the enzyme is involved in detoxification and drug metabolism, overview, expression of FMO5 is markedly down-regulated in the liver of humans with type II diabetes, patients diagnosed with atrial fibrillation document a significant increase in the expression of FMO1, FMO may be associated with sideroblastic anemia, FMO3 mutations lead to trimethylaminuria, detailed overview | Homo sapiens | ? | - |
? | |
| 1.14.13.8 | additional information | nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview | Sus scrofa | ? | - |
? | |
| 1.14.13.8 | additional information | nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview | Oryctolagus cuniculus | ? | - |
? | |
| 1.14.13.8 | additional information | nitrogen- and sulfur-containing endogenous substrates and physiologic functions, the enzyme is involved in detoxification and drug metabolism, overview, hepatic total FMO activity is enhanced in mouse models of type I and type II diabetes | Mus musculus | ? | - |
? | |
| 1.14.13.8 | additional information | FMO oxygenates drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, isozyme substrate specificity, detailed overview, no activity with 1,3-diphenylthiourea | Homo sapiens | ? | - |
? | |
| 1.14.13.8 | additional information | FMO oxygenates oxygenates a wide range of sulfur- and nitrogen-containing xenobiotics and, in some cases, also oxygenates selenium, iodine, boron, phosphorus and even carbon, it oxidizes drugs and xenobiotics containing a soft nucleophile, usually nitrogen or sulfur, utilizing the reducing equivalents of NADPH to reduce 1 atom of molecular oxygen to water, while the other atom is used to oxidize the substrate, FMO does not require a reductase to transfer electrons from NADPH, liver isozyme FMO1 shows a very promiscuous substrate specificity, isozyme substrate specificity, detailed overview | Sus scrofa | ? | - |
? | |
| 1.14.13.8 | additional information | the lung isozyme is distinct from the liver isozyme in having high activity toward primary alkyl amines, restricted substrate specificity related to steric properties, resistance to detergent inhibition and enhanced thermal stability, and restricted substrate access, no activity of the lung isozyme with 1,3-diphenylthiourea, chlorpromazine and imipramine by isozyme FMO2, isozyme substrate specificity, detailed overview | Oryctolagus cuniculus | ? | - |
? | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + O2 | - |
Mus musculus | N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + O2 | - |
Homo sapiens | N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + O2 | - |
Sus scrofa | N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | N,N-dimethylaniline + NADPH + O2 | - |
Oryctolagus cuniculus | N,N-dimethylaniline N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | naphthylthiourea + NADPH + O2 | isozyme FMO2 | Homo sapiens | naphthylthiourea S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | naphthylthiourea + NADPH + O2 | isozyme FMO2 | Oryctolagus cuniculus | naphthylthiourea S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | phenethylamine + NADPH + O2 | isozyme FMO3 | Homo sapiens | phenethylamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | phenylthiourea + NADPH + O2 | isozyme FMO2 | Homo sapiens | phenylthiourea S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | phenylthiourea + NADPH + O2 | isozyme FMO2 | Oryctolagus cuniculus | phenylthiourea S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | ranitidine + NADPH + O2 | - |
Homo sapiens | ? | - |
? | |
| 1.14.13.8 | S-farnesylcysteine + NADPH + O2 | - |
Sus scrofa | S-farnesylcysteine S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | S-farnesylcysteine methyl ester + NADPH + O2 | - |
Sus scrofa | ? | - |
? | |
| 1.14.13.8 | S-farnesylcysteine methyl ester + NADPH + O2 | - |
Sus scrofa | S-farnesylcysteine S-oxide methyl ester + NADP+ + H2O | - |
? | |
| 1.14.13.8 | sulindac sulfide + NADPH + O2 | - |
Sus scrofa | sulindac + NADP+ + H2O | - |
? | |
| 1.14.13.8 | thiourea + NADPH + O2 | - |
Sus scrofa | thiourea S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | thiourea + NADPH + O2 | isozyme FMO2 | Homo sapiens | thiourea S-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | trifluoroperazine + NADPH + O2 | - |
Sus scrofa | ? | - |
? | |
| 1.14.13.8 | trimethylamine + NADPH + O2 | - |
Mus musculus | trimethylamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | trimethylamine + NADPH + O2 | - |
Homo sapiens | trimethylamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | trimethylamine + NADPH + O2 | - |
Sus scrofa | trimethylamine N-oxide + NADP+ + H2O | - |
? | |
| 1.14.13.8 | tyramine + NADPH + O2 | - |
Homo sapiens | tyramine N-oxide + NADP+ + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.13.8 | More | structure motifs, overview, structural modeling | Mus musculus |
| 1.14.13.8 | More | structure motifs, overview, structural modeling | Homo sapiens |
| 1.14.13.8 | More | structure motifs, overview, structural modeling | Sus scrofa |
| 1.14.13.8 | More | structure motifs, overview, structural modeling | Oryctolagus cuniculus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.13.8 | FMO | - |
Mus musculus |
| 1.14.13.8 | FMO | - |
Homo sapiens |
| 1.14.13.8 | FMO | - |
Sus scrofa |
| 1.14.13.8 | FMO | - |
Oryctolagus cuniculus |
| 1.14.13.8 | More | the enzyme belongs to the human FMO functional gene family | Homo sapiens |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.14.13.8 | additional information | - |
the lung isozyme shows high thermal stability as the liver isozyme | Oryctolagus cuniculus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.13.8 | FAD | one molecule per enzyme molecule, binding motif | Mus musculus | |
| 1.14.13.8 | FAD | one molecule per enzyme molecule, binding motif | Homo sapiens | |
| 1.14.13.8 | FAD | one molecule per enzyme molecule, binding motif | Sus scrofa | |
| 1.14.13.8 | FAD | one molecule per enzyme molecule, binding motif | Oryctolagus cuniculus | |
| 1.14.13.8 | additional information | the enzyme contains no heme | Mus musculus | |
| 1.14.13.8 | additional information | the enzyme contains no heme | Homo sapiens | |
| 1.14.13.8 | additional information | the enzyme contains no heme | Sus scrofa | |
| 1.14.13.8 | additional information | the enzyme contains no heme | Oryctolagus cuniculus | |
| 1.14.13.8 | NADPH | binding structure | Mus musculus | |
| 1.14.13.8 | NADPH | binding structure | Homo sapiens | |
| 1.14.13.8 | NADPH | binding structure | Sus scrofa | |
| 1.14.13.8 | NADPH | binding structure | Oryctolagus cuniculus | |
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