Cysteine and homocysteine synthesis in Saccharomycopsis lipolytica; identification and characterization of two cysteine synthases.

In Saccharomycopsis (Candida) lipolytica direct cysteine synthesis is mediated by two different, simultaneously acting cysteine synthases: a low molecular mass (74,000 daltons) monofunctional enzyme (Km for O-acetyl-l-serine 23.5 mm) and a high molecular mass (220,000 daltons) bifunctional cysteine-homocysteine synthase (Km for O-acetyl-l-serine 55.0 mm). The latter enzyme is also involved in direct homocysteine synthesis from O-acetyl-l-homoserine (Km 11.9 mm). Evidence is presented that a fraction of homocysteine can be synthesized from cysteine via cystathionine. Our previous results (Morzycka & Paszewski, FEBS Lett., 1979, 101, 97-100; Mol. Gen. Genet., 1979, 174, 33-38) together with the data presented here strongly suggest that both S., lipolytica synthases are under control of the same regulatory system, together with the other enzymes of sulphur metabolism: ATP-sulphurylase and aryl-sulphatase. gamma-Cystathionase, an enzyme involved in cysteine synthesis from homocysteine, is controlled exclusively by cysteine.