Glycine metabolism. III. A flavin-linked dehydrogenase associated with the glycine cleavage system in Peptococcus glycinophilus

Klein, S.M.; Sagers, R.D.

Journal of Biological Chemistry 242(2): 297-300

1967


ISSN/ISBN: 0021-9258
Accession: 024753564

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Abstract
One of the 4 proteins involved in the cleavage of glycine to 1-C units and the transfer of electrons from glycine to DPN is a flavoprotein. Precipitation of the protein with acid (NH4)2 SO4 in the presence of 1 M KBr separated the coenzyme from the apoenzyme. The latter was fully reactivated by incubation with FAD but showed no activity with FMN. The flavoprotein could be reduced by glycine or DPNH2. No protein other than the flavoprotein was required for the electron transfer when reduced by the latter, but it was necessary to add the 3 other proteins plus tetra-hydrofolate to achieve a measurable rate of reduction by glycine. Dihydrofolate was entirely inactive in the system.