SUMMARY: A yeast strain highly resistant to propargylglycine (an inhibitor of cystathionine γ-lyase) was isolated from air. It was partially characterized, but it has not been identified with any known yeast species. Its sulphur amino acid metabolism differed from that of other fungi by the lack of the reverse transsulphuration pathway from methionine to cysteine, as no activity of cystathionine β-synthase or cystathionine γ-lyase was found. The functional lack of this pathway was confirmed by growth tests and by experiments with [S]methionine. In contrast to neither homocysteine synthase nor the sulphate assimilation pathway were repressible by methionine in the new strain; on the contrary, a regulatory effect of cysteine was observed.


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