EC Number | Cloned (Comment) | Organism |
---|---|---|
1.5.3.1 | genes TK0116 and TK0117, separate cloning and expression in Eschericia coli strain BL21(DE3) of His-tagged alpha and beta subunits of SOX | Thermococcus kodakarensis |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.5.3.1 | 43000 | - |
4 * 54000, recombinant alpha-subunnit, + 4 * 43000, recombinant beta-subunit, SDS-PAGE, (alphabeta)4 , the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the heterooctameric (alphabeta)4 form and shows NADH dehydrogenase activity, transmission electron microscopy and gel filtration | Thermococcus kodakarensis |
1.5.3.1 | 54000 | - |
4 * 54000, recombinant alpha-subunnit, + 4 * 43000, recombinant beta-subunit, SDS-PAGE, (alphabeta)4 , the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the heterooctameric (alphabeta)4 form and shows NADH dehydrogenase activity, transmission electron microscopy and gel filtration | Thermococcus kodakarensis |
1.5.3.1 | 160000 | - |
isolated recombinant beta-subunit, native PAGE | Thermococcus kodakarensis |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.3.1 | sarcosine + H2O + O2 | Thermococcus kodakarensis | - |
glycine + formaldehyde + H2O2 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.3.1 | Thermococcus kodakarensis | - |
genes TK0116 and TK0117 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.5.3.1 | recombinant His-tagged alpha and beta subunits from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity | Thermococcus kodakarensis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.3.1 | additional information | the alpha subunit shows sarcosine oxidase and L-proline dehydrogenase activity, while the beta subunit displays both sarcosine oxidase and L-proline dehydrogenase activity, but not NADH dehydrogenase activity, measurement of L-proline dehydrogenase activity with 2,6-dichloroindophenol as cofactor. Dye-linked NADH dehydrogenase activity is assayed with NADH, FAD and 2,6-dichloroindophenol | Thermococcus kodakarensis | ? | - |
? | |
1.5.3.1 | sarcosine + H2O + O2 | - |
Thermococcus kodakarensis | glycine + formaldehyde + H2O2 | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.5.3.1 | heterooctamer | 4 * 54000, recombinant alpha-subunnit, + 4 * 43000, recombinant beta-subunit, SDS-PAGE, (alphabeta)4 , the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the heterooctameric (alphabeta)4 form and shows NADH dehydrogenase activity, transmission electron microscopy and gel filtration | Thermococcus kodakarensis |
1.5.3.1 | More | structure of isolated subunit tetramers, overview | Thermococcus kodakarensis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.3.1 | SOX | - |
Thermococcus kodakarensis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.5.3.1 | 80 | - |
assay at | Thermococcus kodakarensis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.5.3.1 | 8 | - |
assay at | Thermococcus kodakarensis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.3.1 | additional information | the recombinant alpha subunit forms a dimeric structure and behaves as an NADH dehydrogenase, while the beta subunit is a tetramer that has sarcosine oxidase and L-proline dehydrogenase activity.. The SOX complex assembles into the hetero-octameric (alphabeta)4 form and shows NADH dehydrogenase activity, structure of isolated subunit tetramers, overview | Thermococcus kodakarensis |
1.5.3.1 | physiological function | sarcosine oxidase catalyzes the oxidation of the methyl group in sarcosine and transfer of the oxidized methyl group into the one-carbon metabolic pool, yielding equimolar glycine, hydrogen peroxide, and formaldehyde or 5,10-methylenetetrahydrofolate | Thermococcus kodakarensis |