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sarcosine dehydrogenase
In enzymology, sarcosine dehydrogenase () is a mitochondrial enzyme that catalyzes the chemical reaction N-demethylation of sarcosine to give glycine. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donor with other acceptors. The systematic name of this enzyme class is sarcosine:acceptor oxidoreductase (demethylating). Other names in common use include sarcosine N-demethylase, monomethylglycine dehydrogenase, and sarcosine:(acceptor) oxidoreductase (demethylating). Sarcosine dehydrogenase is closely related to dimethylglycine dehydrogenase, which catalyzes the demethylation reaction of dimethylglycine to sarcosine. Both sarcosine dehydrogenase and dimethylglycine dehydrogenase use FAD as a cofactor. Sarcosine dehydrogenase is linked by electron-transferring flavoprotein (ETF) to the respiratory redox chain.
The general chemical reaction catalyzed by sarcosine dehydrogenase is:
:sarcosine + acceptor + H2O glycine + formaldehyde + reduced acceptor
== Structure ==
There is no crystal structure available for sarcosine dehydrogenase. Sarcosine dehydrogenase contains a covalently bound FAD group " linked via the 8 alpha position of the isoalloxazine ring to an imidazole N(3) of a histidine residue". The enzyme, according to Freisell Wr. et al., also contains non-heme iron in a ratio of 1 or 2 iron per 300000g of enzyme, and 0.5 mol of acid soluble sulfur suggesting that the electron transfer during the first step in the reaction might proceed through a different pathway than that of Fe-S clusters.〔
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