|
type |
Journal Article |
authors |
Zinecker, H.; Andreesen, J. R.; Pich, A. |
title |
Partial purification of an iron-dependent L-serine dehydratase from Clostridium sticklandii |
journal |
J Basic Microbiol |
Activity |
4.3.1.17 |
ui |
98300644 |
year |
(1998) |
volume |
38 |
number |
2 |
pages |
147-55 |
| |
keywords |
Aerobiosis |
abstract |
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. |
last changed |
2002/11/18 17:04 |
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