Glutamine Degradation Through the -Amidase Pathway in Saccharomyces cerevisiae

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Abstract
A glutamine transaminase activity has been identified in Saccharomyces cerevisiae, and the existence of the .omega.-amidase activity previously described in this yeast has been confirmed. The glutamine transaminase utilizes different 2-oxo acids as substrates, including pyruvate and glyoxylate, and its regulated by the available nitrogen source. The glutamine transaminase activity decreases when lysine or glycine is added to the medium; the inhibition by lysine diminishes under microaerophilic culture conditions.