A possible mechanism for the in vitro activation of L-serine deaminase activity in Escherichia coli K12.
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 radical 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.
Newman
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EB
Biology Department, Concordia University, Montréal, Que., Canada.
Walker
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C
Ziegler-Skylakakis
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K
D000975:Antioxidants / Q000494:pharmacology; D001426:Bacterial Proteins / Q000378:metabolism*; D002412:Cations / Q000494:pharmacology; D004229:Dithiothreitol / Q000494:pharmacology; D004789:Enzyme Activation / Q000187:drug effects; D004926:Escherichia coli / Q000201:enzymology*; D005609:Free Radicals; D006639:Histidine / Q000494:pharmacology; D007501:Iron / Q000378:metabolism; D012695:L-Serine Dehydratase / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D011499:Protein Processing, Post-Translational
D000975:Antioxidants; D001426:Bacterial Proteins; D002412:Cations; D005609:Free Radicals; D006639:Histidine; D007501:Iron; D012695:L-Serine Dehydratase; D010100:Oxygen; D004229:Dithiothreitol