ArticleThe Journal of biological chemistry2011
Thermus thermophilus glycoside hydrolase family 57 branching enzyme: crystal structure, mechanism of action, and products formed.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 109 citations in OpenAlex.
- Beyond Branching: Unlocking the Catalytic Versatility of Branching Enzymes for the Design of Diverse α-Glucan Structures.Molecules (Basel, Switzerland) · 2026Review
- 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
- Elucidation of the noncovalent interactions driving enzyme activity guides branching enzyme engineering for α-glucan modification.Nature communications · 2024Article
- 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
- Biochemical characteristics and potential application of a thermostable starch branching enzyme from Bacillus licheniformis.AMB Express · 2023Article
- Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes.Proteins · 2022Article
- From Prokaryotes to Eukaryotes: Insights Into the Molecular Structure of Glycogen Particles.Frontiers in molecular biosciences · 2021Review
- The structure of a family 110 glycoside hydrolase provides insight into the hydrolysis of α-1,3-galactosidic linkages in λ-carrageenan and blood group antigens.The Journal of biological chemistry · 2020Article
- Deciphering the functional role of hypothetical proteins fromMolecular biology research communications · 2020Article
- Article
- Comparison of the Structural Properties and Nutritional Fraction of Corn Starch Treated with Thermophilic GH13 and GH57 α-Glucan Branching Enzymes.Foods (Basel, Switzerland) · 2019Article
- Identification of Thermotoga maritima MSB8 GH57 α-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.Applied microbiology and biotechnology · 2019Article
- Article
- In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities.3 Biotech · 2018Article
- Distribution of glucan-branching enzymes among prokaryotes.Cellular and molecular life sciences : CMLS · 2016Review
- Biochemical Characterization of the Lactobacillus reuteri Glycoside Hydrolase Family 70 GTFB Type of 4,6-α-Glucanotransferase Enzymes That Synthesize Soluble Dietary Starch Fibers.Applied and environmental microbiology · 2015Article
- Membrane-bound amylopullulanase is essential for starch metabolism of Sulfolobus acidocaldarius DSM639.Extremophiles : life under extreme conditions · 2015Article
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Branching enzyme (EC 2.4.1.18; glycogen branching enzyme; GBE) catalyzes the formation of α1,6-branching points in glycogen. Until recently it was believed that all GBEs belong to glycoside hydrolase family 13 (GH13). Here we describe the cloning and expression of the Thermus thermophilus family GH57-type GBE and report its biochemical properties and crystal structure at 1.35-Å resolution. The enzyme has a central (β/α)(7)-fold catalytic domain A with an inserted domain B between β2 and α5 and an α-helix-rich C-terminal domain, which is shown to be essential for substrate binding and catalysis. A maltotriose was modeled in the active site of the enzyme which suggests that there is insufficient space for simultaneously binding of donor and acceptor substrates, and that the donor substrate must be cleaved before acceptor substrate can bind. The biochemical assessment showed that the GH57 GBE possesses about 4% hydrolytic activity with amylose and in vitro forms a glucan product with a novel fine structure, demonstrating that the GH57 GBE is clearly different from the GH13 GBEs characterized to date.
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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.