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The detection of cGMP in yeast (Eckstein 1988), but lacking hints at guanylate cyclase from sequencing of the yeast genome, raised questions about existence, isoform, and regula­tion of guanylate cyclase from this organism. We found a particulate guanylate cyclase activity in yeast extracts, exhibiting properties of an integral membrane protein. Characteristics are: pH-optimum at pH 6.8, temperature-optimum around 60 °C, only slight stimulation by Mn 2+ . Sigmoidal enzyme kinetics indicate allosteric regulation, ATP and Ca 2+  act as negative allosteric effectors. The enzyme activity is increased by yeast alpha-1 mating factor, and by sodium nitrite, thus showing properties of particulate as well as of soluble isoforms from other eukaryotes. The activation by alpha-1 mating factor suggests receptor functions, and a role in ascospore conjugation.

A Particulate Guanylate Cyclase (EC 4.6.1.2) from Growing Yeast Cells {Saccharomyces cerevisiae)