J. Biol. Chem., Vol. 259, Issue 10, 6085-6089, 05, 1984

Glycine synthase of the purinolytic bacterium, Clostridium acidiurici. Purification of the glycine-CO2 exchange system

RT Gariboldi and HL Drake

When the growth medium of Clostridium acidiurici was supplemented with trace metals, glycine synthase and glycine-CO2 exchange activities in cell-free extracts were found to increase significantly. The glycine- CO2 exchange system was purified and shown to consist of a heat-labile component and a heat-stable component. By gel filtration, heat-labile component had an estimated native Mr = 230,000 and contained two subunits of Mr = 65,000 and 58,000 on sodium dodecyl sulfate- polyacrylamide gels, indicating an alpha 2 beta 2 tetramer. Heat-stable component had an estimated Mr = 20,000 and could not be replaced by lipoic acid in reaction mixtures. Pyridoxal phosphate was not bound to either of the purified components but was essential for glycine-CO2 exchange. By spectral analysis, heat-labile component was shown to interact with pyridoxal phosphate and that reductant influenced this interaction.
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