Rat liver fructose-1,6-bisphosphatase. Identification of serine 338 as a third major phosphorylation site for cyclic AMP-dependent protein kinase and activity changes associated with multisite phosphorylation in vitro.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference15 articles.
1. In vivo and in vitro phosphorylation of rat liver fructose-1,6-bisphosphatase.
2. Amino acid sequence at the phosphorylated site of rat liver fructose-1,6-diphosphatase and phosphorylation of a corresponding synthetic peptide
3. Phosphorylation of rat hepatic fructose-1,6-bisphosphatase and pyruvate kinase.
4. Isolation of the S-peptide formed on digestion of fructose 1,6-bisphosphatase with subtilisin and its non-covalent association with the enzyme protein
5. Fructose-bisphosphatase as a substrate of cyclic AMP-dependent protein kinase.
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