Glutamine degradation through the omega-amidase pathway in Saccharomyces cerevisiae.
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 is 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.
Soberón
M
M
Centro de Investigación sobre Fijación de Nitrógeno, UNAM, Cuernavaca, Morelos.
González
A
A
D000581:Amidohydrolases / Q000378:metabolism*; D005973:Glutamine / Q000378:metabolism*; D009154:Mutation; D010641:Phenotype; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D000637:Transaminases / Q000378:metabolism
D005973:Glutamine; D000637:Transaminases; C020656:glutamine-pyruvate aminotransferase; D000581:Amidohydrolases; C047679:omega-amidase