Corynebacterial sarcosine oxidase, a heterotetrameric () enzyme containing covalent and noncovalent FAD, catalyzes the oxidative demethylation of sarcosine to yield glycine, HO, and 5,10-CH-tetrahydrofolate (H folate) in a reaction requiring Hfolate and O. The sarcosine oxidase operon contains at least five closely packed genes encoding sarcosine oxidase subunits and serine hydroxymethyltransferase (glyA), arranged in the order glyAsoxBDAG. The operon status of a putative purU gene, found 340 nucleotides downstream from soxG, is not known. No homology with other proteins is observed for the smallest sarcosine oxidase subunits and . The subunit (405 residues) contains an ADP-binding motif near its NH terminus, the covalent FAD attachment site (H175), and exhibits homology with the NH-terminal half of dimethylglycine dehydrogenase (857 residues) and monomeric, bacterial sarcosine oxidases (388 residues), enzymes that contain a single covalent FAD. The subunit (967 residues) contains a second ADP-binding motif within an 280 residue region near the NH terminus that exhibits homology with subunit A from octopine and nopaline oxidases, heterodimeric enzymes that catalyze analogous oxidative cleavage reactions with N-substituted arginine derivatives. An 380 residue region near the COOH terminus of exhibits homology with T-protein and the COOH-terminal half of dimethylglycine dehydrogenase. These enzymes catalyze the formation of 5,10-CH-Hfolate, using different one-carbon donors. The results suggest that the subunit and dimethylglycine dehydrogenase contain an NH-terminal domain that binds noncovalent or covalent FAD, respectively, and a carboxyl-terminal Hfolate-binding domain.

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