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• W2085675018 abstract "The mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (FBPase) and destabilizes its interaction with aldolase, regulating glycogen synthesis from non-carbohydrates in skeletal muscle is poorly understood. In the current paper, we demonstrate evidence that Ca2+ affects conformation of the catalytic loop 52–72 of muscle FBPase and inhibits its activity by competing with activatory divalent cations, e.g. Mg2+ and Zn2+. We also propose the molecular mechanism of Ca2+-induced destabilization of the aldolase–FBPase interaction, showing that aldolase associates with FBPase in its active form, i.e. with loop 52–72 in the engaged conformation, while Ca2+ stabilizes the disengaged-like form of the loop." @default.
• W2085675018 created "2016-06-24" @default.
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• W2085675018 date "2013-10-11" @default.
• W2085675018 modified "2023-10-18" @default.
• W2085675018 title "The Mechanism of Calcium-Induced Inhibition of Muscle Fructose 1,6-bisphosphatase and Destabilization of Glyconeogenic Complex" @default.
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• W2085675018 doi "https://doi.org/10.1371/journal.pone.0076669" @default.
• W2085675018 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3795747" @default.
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