SGD Paper 
Holzer H and Purwin C (1986) How does glucose initiate proteolysis of yeast fructose-1,6-bisphosphatase? Biomed Biochim Acta 45(11-12):1657-63
Abstract: Glucose-induced proteolysis of fructose-1,6-bisphosphatase (FBPase) in yeast (Funayama, S. et al. (1980) Eur. J. Biochem. 109, 61-66) is preceded by rapid phosphorylation of the enzyme (Muller, D., and Holzer, H. (1981) Biochem. Biophys. Res. Commun. 103. 926-933; Mazon, M. J. et al. (1982) J. Biol. Chem. 257, 1128-1130). The postulated sequence of events is as follows. Glucose causes a decrease of the cytosolic pH from 7.0 to about 6.5 (Purwin, C. et al. (1986) J. Biol. Chem. 261, in press). The change in pH activates adenylate cyclase which is at pH 6.5 2-3 times more active than at pH 7.0 The concentration of cAMP increases 2-5 times (Purwin, C. et al. (1982) Biochem. Biophys. Res. Commun. 107, 1482-1489) and thereby activates a protein kinase which phosphorylates FBPase (Pohlig, G., and Holzer, H. (1985) J. Biol. Chem. 260, 13818 to 13823). The phosphorylated enzyme is either proteolyzed in the cytosol or taken up into the vacuoles, the compartment where unspecific proteolysis takes place.FAU - Holzer, .
| Status: Published | Type: Journal Article | PubMed ID: 3034238 |
Topics addressed in this paper
Number of different genes curated to this paper: 2
- To find other papers on a gene and topic, click on the colored ball in the appropriate box.
- displays other papers with information about that topic for that gene.
- displays other papers in SGD that are associated with that topic.
The topic is addressed in these papers but does not describe a specific gene or chromosomal feature.
- To go to the Locus page for a gene, click on the gene name.
