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.
Zinecker
H
H
Martin-Luther-Universität Halle-Wittenberg, Institut für Mikrobiologie.
Andreesen
J R
JR
Pich
A
A
D000332:Aerobiosis; D000595:Amino Acid Sequence; D000693:Anaerobiosis; D002845:Chromatography; D002850:Chromatography, Gel; D003013:Clostridium / Q000201:enzymology* / Q000254:growth & development; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D007501:Iron / Q000378:metabolism; D012695:L-Serine Dehydratase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data
D007501:Iron; D012695:L-Serine Dehydratase