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Literature summary extracted from

  • Lee, S.; Jia, B.; Pham, B.P.; Shao, Y.; Kwak, J.M.; Cheong, G.W.
    Architecture and characterization of sarcosine oxidase from Thermococcus kodakarensis KOD1 (2012), Extremophiles, 16, 87-93.
    View publication on PubMed

Cloned(Commentary)

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.3.1 Thermococcus kodakarensis
-
genes TK0116 and TK0117
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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
-
?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.5.3.1 SOX
-
Thermococcus kodakarensis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.3.1 80
-
assay at Thermococcus kodakarensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.3.1 8
-
assay at Thermococcus kodakarensis

General Information

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