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

Robert J. Bonney | Zendy; Herbert Weinfeld | Zendy

Open Access

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

Author(s) -

Robert J. Bonney,

Herbert Weinfeld

Publication year - 1971

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.105.3.940-946.1971

Subject(s) - thymidine phosphorylase , biology , biochemistry , thymidine , purine nucleoside phosphorylase , aldolase a , nucleotide salvage , escherichia coli , deoxyribose , operon , enzyme , microbiology and biotechnology , purine , nucleic acid , nucleotide , gene , dna

InEscherichia 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.

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