ArticleApplied microbiology and biotechnology2019
Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.
Article in Applied microbiology and biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 19 citations in OpenAlex.
- Beyond Branching: Unlocking the Catalytic Versatility of Branching Enzymes for the Design of Diverse α-Glucan Structures.Molecules (Basel, Switzerland) · 2026Review
- Ultrasound-Assisted Optimization of the Activation and Inactivation of Thermostable α-Amylase.International journal of molecular sciences · 2026Article
- Transformation of Starch into an Equilibrium Pool of Glucose and Small Maltosaccharides by a Hyperthermophilic Enzyme Exhibiting Coupled (Exo)Amylase-Glucanotransferase Functions.Applied biochemistry and biotechnology · 2026Article
- The crystal structure of GH57 family amylopullulanase reveals its dual binding pockets sharing the same catalytic dyad.Communications biology · 2025Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- The Synergistic Effect of GH13 and GH57 GBEs ofPolymers · 2023Article
- Article
- Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes.Proteins · 2022Article
- Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
AmyC, a glycoside hydrolase family 57 (GH57) enzyme of Thermotoga maritima MSB8, has previously been identified as an intracellular α-amylase playing a role in either maltodextrin utilization or storage polysaccharide metabolism. However, the α-amylase specificity of AmyC is questionable as extensive phylogenetic analysis of GH57 and tertiary structural comparison suggest that AmyC could actually be a glycogen-branching enzyme (GBE), a key enzyme in the biosynthesis of glycogen. This communication presents phylogenetic and biochemical evidence that AmyC is a GBE with a relatively high hydrolytic (α-amylase) activity (up to 30% of the total activity), creating a branched α-glucan with 8.5% α-1,6-glycosidic bonds. The high hydrolytic activity is explained by the fact that AmyC has a considerably shorter catalytic loop (residues 213-220) not reaching the acceptor side. Secondly, in AmyC, the tryptophan residue (W 246) near the active site has its side chain buried in the protein interior, while the side chain is at the surface in Tk1436 and Tt1467 GBEs. The putative GBEs from three other Thermotogaceae, with very high sequence similarities to AmyC, were found to have the same structural elements as AmyC, suggesting that GH57 GBEs with relatively high hydrolytic activity may be widespread in nature.
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