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. 1971 May;122(4):415–420. doi: 10.1042/bj1220415

The substrate specificity of purine phosphoribosyltransferases in Schizosaccharomyces pombe

A De Groodt 1, E P Whitehead 1, H Heslot 1, L Poirier 1
PMCID: PMC1176796  PMID: 5123876

Abstract

1. The activities of the purine phosphoribosyltransferases (EC 2.4.2.7 and 2.4.2.8) in purine-analogue-resistant mutants of Schizosaccharomyces pombe were checked. An 8-azathioxanthine-resistant mutant lacked hypoxanthine phosphoribosyltransferase, xanthine phosphoribosyltransferase and guanine phosphoribosyltransferase activities (EC 2.4.2.8) and appeared to carry a single mutation. Two 2,6-diaminopurine-resistant mutants retained these activities but lacked adenine phosphoribosyltransferase activity (EC 2.4.2.7). This evidence, together with data on purification and heat-inactivation patterns of phosphoribosyltransferase activities towards the various purines, strongly suggests that there are two phosphoribosyltransferase enzymes for purine bases in Schiz. pombe, one active with adenine, the other with hypoxanthine, xanthine and guanine. 2. Neither growth-medium supplements of purines nor mutations on genes involved in the pathway for new biosynthesis of purine have any influence on the amount of hypoxanthine–xanthine–guanine phosphoribosyltransferase produced by this organism.

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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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