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. 1969 Mar;97(3):1386–1396. doi: 10.1128/jb.97.3.1386-1396.1969

2-Deoxyribose Gene-Enzyme Complex in Salmonella typhimurium: Regulation of Phosphodeoxyribomutase

Patricia A Hoffee 1, B C Robertson 1
PMCID: PMC249859  PMID: 4887516

Abstract

Phosphodeoxyribomutase, the enzyme which catalyzes the interconversion of 2-deoxyribose-1-phosphate to 2-deoxyribose-5-phosphate, has been partially purified from Salmonella typhimurium. The enzyme had an absolute requirement for manganese ion and was stimulated by glucose-1, 6-diphosphate. Phosphodeoxyribomutase was induced by deoxyribose-5-phosphate and was coordinately regulated with the enzymes thymidine phosphorylase and deoxyribose-5-phosphate aldolase, type II. Mutants deficient in these three enzymes were isolated and mapped close to the threonine locus in S. typhimurium. The three enzymes thymidine phosphorylase, deoxyribose-5-phosphate aldolase, type II, and phosphodeoxyribomutase are controlled by a series of linked genes and appear to constitute an operon.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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