Hoffee P A, Robertson B C
J Bacteriol. 1969 Mar;97(3):1386-96. doi: 10.1128/jb.97.3.1386-1396.1969.
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.
磷酸脱氧核糖变位酶,即催化2-脱氧核糖-1-磷酸与2-脱氧核糖-5-磷酸相互转化的酶,已从鼠伤寒沙门氏菌中部分纯化出来。该酶对锰离子有绝对需求,并受到葡萄糖-1,6-二磷酸的刺激。磷酸脱氧核糖变位酶由5-磷酸脱氧核糖诱导产生,并与胸苷磷酸化酶和II型5-磷酸脱氧核糖醛缩酶协同调节。分离出了这三种酶缺陷的突变体,并将其定位在鼠伤寒沙门氏菌中靠近苏氨酸基因座的位置。胸苷磷酸化酶、II型5-磷酸脱氧核糖醛缩酶和磷酸脱氧核糖变位酶这三种酶由一系列连锁基因控制,似乎构成一个操纵子。