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1.5.3.1: sarcosine oxidase (formaldehyde-forming)

This is an abbreviated version!
For detailed information about sarcosine oxidase (formaldehyde-forming), go to the full flat file.

Word Map on EC 1.5.3.1

Reaction

sarcosine
+
H2O
+
O2
=
glycine
+
formaldehyde
+
H2O2

Synonyms

heterotetrameric sarcosine oxidase, L-pipecolate oxidase, L-pipecolic acid oxidase, monomeric sarcosine oxidase, MSOX, PSO, sarcosine : oxygen oxidoreductase (demethylating), sarcosine oxidase, sarcosine: O2 oxidoreductase, sarcosine:oxygen oxidoreductase (demethylating), SO, SO-U96, SOX, SoxA, trd_1773, TSOX

ECTree

     1 Oxidoreductases
         1.5 Acting on the CH-NH group of donors
             1.5.3 With oxygen as acceptor
                1.5.3.1 sarcosine oxidase (formaldehyde-forming)

General Information

General Information on EC 1.5.3.1 - sarcosine oxidase (formaldehyde-forming)

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
hydride-transfer is the most energetically favorable mechanism. Hydrogen is not transferred in the hydride state (H-) but in a hydrogen atom state. A single electron is simultaneously transferred from sarcosine to flavin through their overlapping orbitals, the reaction mechanism can be labeled the hydrogen-atom coupled electron-transfer (HACET) mechanism. Sarcosine is moved close to the flavin ring because of a small charge transfer and the positively charged residues (Arg49, Arg52, and Lys348) near the active site play a prominent role in stabilizing the sarcosine-flavin complex
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
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