Date of Award:
5-1971
Document Type:
Thesis
Degree Name:
Master of Science (MS)
Department:
Biology
Department name when degree awarded
Bacteriology and Public Health
Committee Chair(s)
Carl A. Westby
Committee
Carl A. Westby
Committee
Bruce F. Burnham
Committee
Rex S. Spendlove
Abstract
Ribose-5 '-phosphate aminotransferase, an alternate first enzyme in the purine de novo pathway, has been purified about 800-fold from Salmonella typhimurium (pur D-55 ). The enzyme is distinct from ribosylpyrophosphate-5'-phosphate amidotransferase (E C 2.4.2.14), has an approximate molecular weight of 229,000, and requires ribose-5'-phosphate, ATP and either ammonium ion, carbamyl phosphate or L-glutamine, to synthesize 5'-phosphoribosylamine (PRA). A coupled assay system, employing a S. typhimurium (pur G-310) extract as the coupling-agent source, was used to measure the enzyme. PRA production in this system was inhibited by higher ribose-5' -phosphate concentrations and longer (over 10 minutes) incubation periods. It is proposed that an alternate pathway for the initial step of purine biosynthesis exists in S. typhimurium, namely, the direct conversion of ribose-5 '-phosphate and ammonium ion to PRA.
Checksum
6e417806cc216d989a7e707141c027bd
Recommended Citation
Vahora, Gulamnabi Y., "Ribose 5'-Phosphate Aminotransferase of Salmonella typhimurium" (1971). All Graduate Theses and Dissertations, Spring 1920 to Summer 2023. 8279.
https://digitalcommons.usu.edu/etd/8279
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