Sexual response in Saccharomyces cerevisiae: alteration of enzyme activity in the glyoxalase system by mating factor.
Glyoxalase I activity in alpha-type budding yeast of the Saccharomyces cerevisiae strain was increased by exposure of alpha-type cells to supernatant of a culture of a-type yeast cells, although glyoxalase II activity was decreased by the same treatment. The alteration of enzyme activity in the glyoxalase system occurred during the 30-60 min period after exposure of alpha-type cells to a-type culture supernatant. No change of glyoxalase I and II activities was found in the case of the alpha-type strain, S. cerevisiae VQ3 (alpha ste3-1), which is deficient in a-factor receptors.
Inoue
Y
Y
Research Institute for Food Science, Kyoto University, Japan.
Bong-Young
C
C
Murata
K
K
Kimura
A
A
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D007791:Lactoylglutathione Lyase / Q000378:metabolism*; D008190:Lyases / Q000378:metabolism*; D000072235:Mating Factor; D009154:Mutation; D010455:Peptides / Q000235:genetics / Q000494:pharmacology / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D013869:Thiolester Hydrolases / Q000378:metabolism*; D000099301:Hydroxyacylglutathione Hydrolase
D000429:Alcohol Oxidoreductases; D007791:Lactoylglutathione Lyase; D008190:Lyases; D000072235:Mating Factor; D010455:Peptides; D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase; C031416:D-lactaldehyde dehydrogenase