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  • Title: Biochemical characterization of sulfur assimilation by Salmonella pullorum.
    Author: Kline BC, Schoenhard DE.
    Journal: J Bacteriol; 1970 Apr; 102(1):142-8. PubMed ID: 4908669.
    Abstract:
    The biochemical basis for a cysteine requirement in Salmonella pullorum strain MS35 is presented. Before determining the missing biochemical functions, it was established that the assimilatory sulfate-reducing pathway for this species is an inorganic one in which 3'-phosphoadenylylsulfate (PAPS), sulfite, and sulfide are intermediates. A requirement for 2'- and 3'-adenosine monophosphate was found for in vitro synthesis of PAPS, possibly because 2'- and 3'-adenosine monophosphate inhibits endogenous nucleases that destroy PAPS. The cysteine requirement of strain MS35 was attributed to a defect at 37 C in sulfate permeation and temperature sensitivity in sulfite reduction. At 25 C, sulfite was metabolized to sulfide. A novel property of sulfate-utilizing revertants was their unselected ability to assimilate thiosulfate sulfur at 25 C but not at 37 C.
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