The product of theade1 gene inSchizosaccharomyces pombe: A bifunctional enzyme catalysing two distinct steps in purine biosynthesis

Publisher Website
Google Scholar
Abstract
The assignment of the knownade genes to steps in purine biosynthesis inSchizosaccharomyces pombe has been completed with the demonstration that anade3 mutants lacks FGAR amidotransferase,ade1A mutants lack GAR synthetase andade1B mutants lack AIR synthetase. A comparison of enzyme activity with map position forade1 mutants shows that (1) complementingade1A mutants lack GAR synthetase but possess wild type amounts of AIR synthetase, (2) complementingade1B mutants lack AIR synthetase but posses variable amounts of GAR synthetase, (3) non-complementing mutants lack both activities. In wild type strains the two activities fractionate together throughout a hundred-fold purification. Hence theade1 gene appears to code for a bifunctional enzyme catalysing two distinct steps in purine biosynthesis. The two activities are catalysed by two different regions of the polypeptide chain which can be altered independendently by mutation. Gel filtration studies on partially purified enzymes from wild type and various complementing mutant strains, indicate that the bifunctional enzyme is a multimer consisting of between four and six sub-units of 40,000 daltons each. GAR synthetase activity is associated with both the monomeric and multimeric forms but AIR synthetase is only associated with the multimer. A comparison of enzyme levels between diploids and their original complementing haploid strains suggests that complementation is due to hybrid enzyme formation.