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Role of O‐acetylhomoserine sulfhydrylase in sulfur amino acid synthesis in various yeasts
Author(s) -
Brzywczy Jerzy,
Paszewski Andrzej
Publication year - 1993
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.320091207
Subject(s) - kluyveromyces lactis , yarrowia , yeast , biology , mutant , biochemistry , saccharomyces cerevisiae , auxotrophy , schizosaccharomyces pombe , enzyme , microbiology and biotechnology , kluyveromyces , gene
Mutants defective in O‐acetylhomoserine sulfhydrylase (OAH‐SHLase) were obtained in five yeast strains representative of different yeast genera: Saccharomyces cerevisiae, Kluyveromyces lactis, Yarrowia lipolytica, Schizosaccharomyces pombe and Trichosporon cutaneum. In vitro , in all five strains, the enzyme also had O‐acetylserine (OAS) sulfhydrylase activity so it is a ‘bifunctional’ OAH/OAS‐SHLase (Yamagata, 1989). The enzyme was only found to be essential in S. cerevisiae (OAH SHLase‐negative mutants are auxotrophs). Its impairment in K. lactis caused a slower growth rate and a decrease of the sulfur amino acid pool. In T. cutaneum only the pool was affected whereas in Y. lipolytica and S. pombe the lesion caused no change in the growth rate nor in the pool. In all strains where OAH SHLase‐negative mutants were prototrophs, a monofunctional OAS sulfhydrylase was detected. The results indicate that OAH SHLase may play different physiological roles in various yeasts.