Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Triton X-100 | FMO3 enzymes show a 2fold activation of kcat/Km in the presence of Triton X-100. MBP-FMO3 also shows disassociation from a high-order oligomeric form to a monomeric status in the presence of Triton X-100 | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression of FMO3 and FMO5 as N-terminal maltose-binding protein fusion proteins, MBP-FMOs, in Escherichia coli strain DH5alpha | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetic analysis of commercial recombinant enzymes and recombinant MBP-FMOs expressed in Escherichia coli, overview | Homo sapiens | |
15 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is Triton X-100, recombinant MBP-FMO3 | Homo sapiens | |
25 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is Triton X-100, commercial recombinant FMO3 | Homo sapiens | |
32 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is a minimal detergent, recombinant MBP-FMO3 | Homo sapiens | |
35 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is a minimal detergent, commercial recombinant FMO3 | Homo sapiens | |
38 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is CHAPS, recombinant MBP-FMO3 | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
microsome | membrane-bound | Homo sapiens | - |
- |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
100000 | - |
x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation | Homo sapiens |
102000 | - |
x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation | Homo sapiens |
104000 | - |
x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant MBP-fusion FMO3 and FMO5 from Escherichia coli strain DH5alpha to about 90% purity by amylose affinity chromatography, and for FMO3 also further by anion exchange chromatography | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | recombinant enzymes expressed in insect cells | Homo sapiens | - |
liver | FMO3 and FMO5 are the predominant FMO forms in adult liver | Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine + NADPH + H+ + O2 | - |
Homo sapiens | 10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine N-oxide + NADP+ + H2O | - |
? | |
L-methionine + NADPH + H+ + O2 | - |
Homo sapiens | L-methionine S-oxide + NADP+ + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 100000, recombinant MBP-FMO3 and MBP-FMO5, SDS-PAGE, x * 102000, about, MBP-FMO3, sequence calculation, x * 104000, about, MBP-FMO5, sequence calculation | Homo sapiens |
More | MBP-FMO3 shows disassociation from a high-order oligomeric form to a monomeric status in the presence of Triton X-100. MBP-FMO3 solubilized in 0.5% CHAPS and MBP-FMO5 solubilized in 0.01% DDM or minimal detergent conditions contain hexameric and larger aggregates of protein | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
flavin-containing monooxygenase 3 | - |
Homo sapiens |
FMO3 | - |
Homo sapiens |
FMO5 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.18 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is a minimal detergent, recombinant MBP-FMO3 | Homo sapiens | |
0.19 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is CHAPS, recombinant MBP-FMO3 | Homo sapiens | |
0.22 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is Triton X-100, recombinant MBP-FMO3 | Homo sapiens | |
0.55 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is a minimal detergent, commercial recombinant FMO3 | Homo sapiens | |
0.67 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is CHAPS, commercial recombinant FMO3 | Homo sapiens | |
0.72 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is Triton X-100, commercial recombinant FMO3 | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | content determination, overview. Molar ratio of FAD to MBP-FMO3 varies from 0.5 to 0.9, and the FAD content of MBP-FMO5 has molar ratios of 0.6 and 0.7 | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | although maltose-binding-protein-FMO enzymes afford lower rates of turnover than the corresponding commercial recombinant FMOs, both types of FMO show identical substrate dependencies and similar responses to changes in assay conditions. Comparison of commercial recombinant enzymes with recombinant MBP-FMOs expressed in Escherichia coli, overview | Homo sapiens |
physiological function | the flavin-containing monooxygenase family of enzymes oxygenates nucleophilic xenobiotics and endogenous substances | Homo sapiens |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.005 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is CHAPS, recombinant MBP-FMO3 | Homo sapiens | |
0.0057 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is a minimal detergent, recombinant MBP-FMO3 | Homo sapiens | |
0.0143 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is Triton X-100, recombinant MBP-FMO3 | Homo sapiens | |
0.0152 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is a minimal detergent, commercial recombinant FMO3 | Homo sapiens | |
0.027 | - |
10-[(N,N-dimethylaminooctyl)-2-(trifluoromethyl)]phenothiazine | pH 8.5, 37°C, detergent is Triton X-100, commercial recombinant FMO3 | Homo sapiens |