Cyclic AMP-dependent phosphorylation of fructose-1,6-bisphosphatase and other proteins in the yeast Candida maltosa
✍ Scribed by Dr. K. H. Hofmann; E. Polnisch
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 280 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0233-111X
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✦ Synopsis
In crude extracts of Cundidu maltom, 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-l,6-bisphosphatase both after electrophoresis of crude extracts incubated with cAMP and of a partially purified fructose-I .6-bisphosphatase incubated with a catalytic subunit of CAMP-dependent protein kinase. N o 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-I ,6-bisphosphatase in Candid0 maltma, as described for Sacclzaroniyces cereaisiae.