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J Bacteriol. 1971 March; 105(3): 940-946
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Regulation of Thymidine Metabolism in Escherichia coli K-12: Evidence That at Least Two Operons Control the Degradation of Thymidine

^a Department of Biochemistry, Roswell Park Graduate Division, State University of New York, Buffalo, New York 14203
Department of Medicine C, Roswell Park Memorial Institute, Buffalo, New York 14203

ABSTRACT

In Escherichia coli K-12, the rise in activity of thymidine phosphorylase, phosphodeoxyribomutase, and deoxyribose-5-phosphate aldolase caused by exogenous thymidine is dependent on the synthesis of new enzyme protein. Phosphodeoxyribomutase is induced by the purine ribonucleosides adenosine and guanosine, whereas the other two enzymes are not. The mutase activity induced by thymidine and by the purine ribonucleosides has been shown to be the same enzyme by four different criteria. This independent induction of phosphodeoxyribomutase suggests that the gene for this enzyme is in an operon different from the one that may contain the genes for thymidine phosphorylase and deoxyribose-5-phosphate aldolase.

¹ New York State Predoctoral Fellow.