A possible mechanism for the in vitro activation of L-serine deaminase activity in Escherichia coli K12
- 1 April 1990
- journal article
- research article
- Published by Canadian Science Publishing in Biochemistry and Cell Biology
- Vol. 68 (4) , 723-728
- https://doi.org/10.1139/o90-104
Abstract
L-Serine deaminase is inactive in crude extracts of Escherichia coli K12, but can be activated by incubation with iron and dithiothreitol. This activation requires oxygen, and is inhibited by free radial scavengers and by diethylene triamine pentaacetic acid, which prevents Fe cycling. We suggest that in vitro activation of L-serine deaminase is catalyzed by an oxidant (perhaps hydroxyl radicals). Also, activation may be accompanied by a decrease in molecular weight and involve both a cleavage of the polypeptide chain and a reversible reduction of the molecule.This publication has 15 references indexed in Scilit:
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