Partial purification of an iron-dependent L-serine dehydratase from Clostridium sticklandii.

An oxygen-sensitive and highly unstable L-serine dehydratase was partially purified from the Gram-positive anaerobe Clostridium sticklandii. The final active preparation contained five proteins of 27, 30, 44.5, 46, and 58 kDa as judged by SDS-PAGE. The N-terminal sequence of the 30 kDa subunit showed some similarity to the alpha-subunits of the iron-containing L-serine dehydratases from Clostridium propionicum and Peptostreptococcus asaccharolyticus. Oxygen-inactivated L-serine dehydratase from C. sticklandii was reactivated by incubation with Fe2+ under reducing conditions. Furthermore, the enzyme was inactivated by iron-chelating substances like phenanthroline and EDTA. Pyridoxal-5-phosphate (PLP) did not stimulate the activity, and known inhibitors of PLP-containing enzymes such as NaBH4 had no effect on the activity of L-serine dehydratase from C. sticklandii.