Sulphate activation and its control in Escherichia coli and Bacillus subtilis

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Abstract
The enzymes (adenosine triphosphate-sulphate adenylyltransferase (EC 2.7.7.4) and adenosine triphosphate-adenylylsulphate 3[image]-phospho-transferase (EC 2.7.1.25) catalyzing the synthesis of adenosine 3[image]-phosphate 5[image] -sulphatophosphate have been shown to be present in ultrasonic extracts of Escherichia coli and Bacillus subtilis. The enzyme system catalyzing synthesis of adenosine 3[image]-phosphate 5[image]-sulphato-phosphate is repressed by cystine in E. coli and by cyst(e)ine and glutathione in B. subtilis. Growth of E. coli on sulphate as the sole source of Su is abolished by 2 mM-sodium selenate; growth on glutathione is inhibited 60%, but growth on cystine is unaffected.