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Partial purification of an iron‐dependent L ‐serine dehydratase from Clostridium sticklandii
Author(s) -
Zinecker Heidi,
Andreesen Jan R.,
Pich Andreas
Publication year - 1998
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/(sici)1521-4028(199805)38:2<147::aid-jobm147>3.0.co;2-m
Subject(s) - dehydratase , biochemistry , serine , enzyme , pyridoxal phosphate , chemistry , clostridium , pyridoxal , bacteria , biology , cofactor , genetics
An oxygen‐sensitive and highly unstable L ‐serine dehydratase was partially purified from the Grampositive 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 α‐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 Fe 2+ 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 NaBH 4 had no effect on the activity of L ‐serine dehydratase from C. sticklandii .