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. 1970 Apr;102(1):142–148. doi: 10.1128/jb.102.1.142-148.1970

Biochemical Characterization of Sulfur Assimilation by Salmonella pullorum1

Bruce C Kline a,2, Delbert E Schoenhard a
PMCID: PMC284980  PMID: 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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Selected References

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

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