Open AccessMetabolism of 2‐oxoaldehydes in yeasts
Author(s) -
MURATA Kousaku,
SAIKUSA Toshihiko,
FUKUDA Yasuki,
WATANABE Kunihiko,
INOUE Yoshiharu,
SHIMOSAKA Makoto,
KIMURA Akira
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09668.x
Subject(s) - biochemistry , methylglyoxal , catabolism , threonine , saccharomyces cerevisiae , chemistry , metabolism , glycolysis , acetaldehyde , enzyme , serine , biology , yeast , ethanol
l ‐Threonine catabolism by Saccharomyces cerevisiae was studied to determine the role of glycolytic bypath as a detoxyfication system of 2‐oxoaldehyde (methylglyoxal) formed from l ‐threonine catabolism. During the growth on l ‐threonine as a sole source of nitrogen, a large amount of aminoacetone was accumulated in the culture. The enzymatic analyses indicated that l ‐threonine was converted into either acetaldehyde and glycine by threonine aldolase or 2‐aminoacetoacetate by NAD‐dependent threonine dehydrogenase. Glycine formed was condensed with acetyl‐CoA by aminoacetone synthase to form 2‐aminoacetoacetate, a labile compound spontaneously decarboxylated into aminoacetone. The enzyme activities of the glycolytic bypath of the cells grown on l ‐threonine were considerably higher than those of the cells grown on ammonium sulfate as a nitrogen source. The result indicated the possible role of glycolytic bypath as a detoxification system of methylglyoxal formed from l ‐threonine catabolism.