Cyclic AMP-dependent phosphorylation of fructose-1,6-bisphosphatase and other proteins in the yeast Candida maltosa.
In crude extracts of Candida maltosa, about 12 proteins are phosphorylated in the presence of cAMP or of a catalytic subunit of cAMP-dependent protein kinase. A strongly labelled protein spot occurred in the position of fructose-1,6-bisphosphatase both after electrophoresis of crude extracts incubated with cAMP and of a partially purified fructose-1,6-bisphosphatase incubated with a catalytic subunit of cAMP-dependent protein kinase. No phosphorylation of the cytoplasmic malate dehydrogenase could be detected. From these results it was concluded that cAMP-dependent phosphorylation plays an important role in the catabolite inactivation of fructose-1,6-bisphosphatase in Candida maltosa, as described for Saccharomyces cerevisiae.
Hofmann
K H
KH
Sektion Biologie, WB Technische Mikrobiologie, Ernst-Moritz-Arndt-Universität Greifswald.
Polnisch
E
E
D002175:Candida / Q000201:enzymology / Q000378:metabolism*; D000242:Cyclic AMP / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006597:Fructose-Bisphosphatase / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation
D005656:Fungal Proteins; D010750:Phosphoproteins; D000242:Cyclic AMP; D008291:Malate Dehydrogenase; D006597:Fructose-Bisphosphatase