Evidence that alpha-isopropylmalate synthase of Saccharomyces cerevisiae is under the "general" control of amino acid biosynthesis.
The specific activity and the immunoreactive amount of alpha-isopropylmalate synthase were more than three times above wild-type values in a Saccharomyces cerevisiae mutant (cdr1) with constitutively derepressed levels of enzymes known to be under the "general" control of amino acid biosynthesis. The specific activity was also higher in lysine- and arginine-leaky strains when these were grown under limiting conditions, and in wild-type cells grown in the presence of 5-methyltryptophan. A low specific activity was found in a mutant (ndr1) unable to derepress enzymes of the general control system. Neither isopropylmalate isomerase nor beta-isopropylmalate dehydrogenase responded to general control signals.
D015079:2-Isopropylmalate Synthase / Q000378:metabolism*; D050539:3-Isopropylmalate Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000596:Amino Acids / Q000096:biosynthesis*; D006836:Hydro-Lyases / Q000378:metabolism; D009154:Mutation; D007652:Oxo-Acid-Lyases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics
D000596:Amino Acids; D000429:Alcohol Oxidoreductases; D050539:3-Isopropylmalate Dehydrogenase; D015079:2-Isopropylmalate Synthase; D007652:Oxo-Acid-Lyases; D006836:Hydro-Lyases; C021455:3-isopropylmalate dehydratase