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Rat liver fructose-1,6-bisphosphatase: Identification of serine- 338 as a third major phosphorylation site for cyclic AMP-dependent protein kinase. Activity changes associated with multisite phosphorylation in vitro
Department of Medical and Physiological Chemistry, Biomedical Center, University of Uppsala.ORCID iD: 0000-0001-7888-1571
1987 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 262, p. 16699-16703Article in journal (Refereed) Published
Abstract [en]

Rat liver fructose-1,6-bisphosphatase was phosphorylated with [32P]ATP and the catalytic subunit of cyclic AMP-dependent protein kinase. After digestion with trypsin, two peptides were isolated containing 68 and 32% of the total radioactivity, respectively. The former was found to contain the sequence Ala-Lys-Ser(P)-Arg-Pro-Ser(P)-Leu-Pro. In this fragment, Ser-341, but not Ser-338, had earlier been reported to be a phosphorylation site. The other peptide contained phosphorylated Ser-356. It was demonstrated that all the protein-bound [32P]phosphate was distributed evenly between these three serines in the native enzyme regardless of the degree of phosphorylation. Preservation of the three-dimensional structure, however, was needed to obtain phosphorylation of Ser-356. Peptides containing each phosphorylatable serine residue were sequentially removed by digesting the enzyme with chymotrypsin which cleaved off Ser-356, denaturing it with urea, digesting it further with chymotrypsin, thus removing Ser-341, and finally treating it with trypsin which eliminated the rest of the radioactivity which was bound to Ser-338. Kinetic studies of fructose-1,6-bisphosphatase digested in this manner revealed that phosphorylation of Ser-338 decreased the apparent Km for fructose 1,6-bisphosphatase, whereas phosphorylation of Ser-341 decreased the inhibitory effect of AMP and fructose 2,6-bisphosphatase, Phosphorylation of Ser-356 did not affect these parameters. 

Place, publisher, year, edition, pages
1987. Vol. 262, p. 16699-16703
National Category
Immunology in the medical area
Research subject
Biomedical Sciences, Immunology
Identifiers
URN: urn:nbn:se:lnu:diva-1104OAI: oai:DiVA.org:lnu-1104DiVA, id: diva2:307893
Available from: 2010-04-01 Created: 2010-04-01 Last updated: 2018-01-12Bibliographically approved

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Nilsson Ekdahl, Kristina

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CiteExportLink to record
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