ArticleProtein science : a publication of the Protein Society2003
Glucoamylase-like domains in the alpha- and beta-subunits of phosphorylase kinase.
Article in Protein science : a publication of the Protein Society, 2003. 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, 26 citations in OpenAlex.
- Architecture and activation of human muscle phosphorylase kinase.Nature communications · 2024Article
- Article
- Structural characterization of the catalytic γ and regulatory β subunits of phosphorylase kinase in the context of the hexadecameric enzyme complex.Protein science : a publication of the Protein Society · 2018Article
- The structure of the large regulatory α subunit of phosphorylase kinase examined by modeling and hydrogen-deuterium exchange.Protein science : a publication of the Protein Society · 2018Article
- Escherichia coli type III secretion system 2: a new kind of T3SS?Veterinary research · 2014Review
- Structure and location of the regulatory β subunits in the (αβγδ)4 phosphorylase kinase complex.The Journal of biological chemistry · 2012Article
- The glucoamylase inhibitor acarbose is a direct activator of phosphorylase kinase.Biochemistry · 2010Article
- Complete genome sequence and comparative metabolic profiling of the prototypical enteroaggregative Escherichia coli strain 042.PloS one · 2010Article
- The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase.Structure (London, England : 1993) · 2009Article
- Evidence for the location of the allosteric activation switch in the multisubunit phosphorylase kinase complex from mass spectrometric identification of chemically crosslinked peptides.Journal of molecular biology · 2007Article
- Identification of enterohemorrhagic Escherichia coli O26:H- genes required for intestinal colonization in calves.Infection and immunity · 2005Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylase kinase is a four-subunit enzyme involved in the regulation of glycogen breakdown. The traditional textbook view is that only the gamma subunit has enzymatic activity, whereas the other three subunits have a regulatory role. Evidence from homology searches and sequence alignments, however, shows that the alpha- and beta-subunits possess amino-terminal glucoamylase-like domains and suggests that they might possess a previously overlooked amylase activity. If true, this would have important implications for the understanding, diagnosis, and management of glycogen storage diseases. There is thus a clear need to test this hypothesis through enzymatic assays and structural studies.
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