ArticleThe Journal of biological chemistry2011
Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- The metabolic enzyme GYS1 condenses with NONO/p54Cell death and differentiation · 2025Article
- Atg45 is an autophagy receptor for glycogen, a non-preferred cargo of bulk autophagy in yeast.iScience · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Structure of the Mycobacterium smegmatis α-maltose-1-phosphate synthase GlgM.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Brain Glycogen Structure and Its Associated Proteins: Past, Present and Future.Advances in neurobiology · 2019Review
- Crystal Structures of theFrontiers in plant science · 2018Article
- Mechanistic insights into the allosteric regulation of bacterial ADP-glucose pyrophosphorylases.The Journal of biological chemistry · 2017Article
- The recruitment of AMP-activated protein kinase to glycogen is regulated by autophosphorylation.The Journal of biological chemistry · 2015Article
- Neurons have an active glycogen metabolism that contributes to tolerance to hypoxia.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2014Article
- Glycogen and its metabolism: some new developments and old themes.The Biochemical journal · 2012Review
- Multiple glycogen-binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycogen synthase, a central enzyme in glucose metabolism, catalyzes the successive addition of α-1,4-linked glucose residues to the non-reducing end of a growing glycogen molecule. A non-catalytic glycogen-binding site, identified by x-ray crystallography on the surface of the glycogen synthase from the archaeon Pyrococcus abyssi, has been found to be functionally conserved in the eukaryotic enzymes. The disruption of this binding site in both the archaeal and the human muscle glycogen synthases has a large impact when glycogen is the acceptor substrate. Instead, the catalytic efficiency remains essentially unchanged when small oligosaccharides are used as substrates. Mutants of the human muscle enzyme with reduced affinity for glycogen also show an altered intracellular distribution and a marked decrease in their capacity to drive glycogen accumulation in vivo. The presence of a high affinity glycogen-binding site away from the active center explains not only the long-recognized strong binding of glycogen synthase to glycogen but also the processivity and the intracellular localization of the enzyme. These observations demonstrate that the glycogen-binding site is a critical regulatory element responsible for the in vivo catalytic efficiency of GS.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.