Occurrence of a catabolic L-serine (L-threonine) deaminase in Saccharomyces cerevisiae.
Saccharomyces cerevisiae mutants lacking the anabolic L-threonine deaminase, the ilv1- mutants, have been found to exhibit a normal ability to grow, without auxotrophy towards isoleucine, on L-threonine of L-serine as only nitrogen nutrient. Starting from a strain carrying a ilv1- mutation, a new mutation affecting the ability to utilize L-threonine as nitrogen source was selected. This mutation, which also impairs the ability to utilize L-serine, has been denominated cha-, for 'catabolism of hydroxyamino acids' and was found to result in the lack of a catabolic L-serine (L-threonine) deaminase. This enzyme which, unlike the anabolic threonine deaminase, is more active towards serine than towards threonine, differs from the latter enzyme by a number of biochemical and regulatory properties. Whereas the anabolic enzyme is an allosteric enzyme sensitive to feedback inhibition by isoleucine, the catabolic enzyme exhibits Michaelian kinetics: no control of its activity has been detected. Its synthesis is induced by L-serine and L-threonine. These two enzymes, which thus can be easily differentiated by means of their regulations, display a limited ability to compensate for one another's absence and appear to play clearly distinct roles under normal physiological conditions.
D012695:L-Serine Dehydratase / Q000302:isolation & purification*; D009154:Mutation; D009584:Nitrogen / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013913:Threonine Dehydratase / Q000302:isolation & purification*
D012695:L-Serine Dehydratase; D013913:Threonine Dehydratase; D009584:Nitrogen