ArticleJournal of bacteriology2006
A novel branching enzyme of the GH-57 family in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 97 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
- Crystal Structure and Mutational Studies of Cyanobacterial Branching Enzymes Reveal the Structural Determinants of Reaction Product Specificity.Journal of applied glycoscience · 2025Article
- Orthologs of Branching Enzymes from Cyanobacteria Accumulating Distinct Types of α-Glucans Share Common Reaction Product Specificity.Journal of applied glycoscience · 2025Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Characterization of a novel thermostable phospholipase C from T. kodakarensis suitable for oil degumming.Applied microbiology and biotechnology · 2022Article
- Comparison of Catalyzing Properties of Bacterial 4-α-Glucanotransferases Focusing on Their Cyclizing Activity.Journal of microbiology and biotechnology · 2021Article
- Deciphering the functional role of hypothetical proteins fromMolecular biology research communications · 2020Article
- Article
- An overview of 25 years of research on Thermococcus kodakarensis, a genetically versatile model organism for archaeal research.Folia microbiologica · 2020Review
- 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
- Bioinformatics Analysis of Metabolism Pathways of Archaeal Energy Reserves.Scientific reports · 2019Article
- Article
- Biotechnological applications of archaeal enzymes from extreme environments.Biological research · 2018Review
- In silico analysis of the α-amylase family GH57: eventual subfamilies reflecting enzyme specificities.3 Biotech · 2018Article
- Draft Genome Sequences of 12 Dry-Heat-Resistant Bacillus Strains Isolated from the Cleanrooms Where the Viking Spacecraft Were Assembled.Genome announcements · 2018Article
- Structure and Evolution of Glycogen Branching Enzyme N-Termini From Bacteria.Frontiers in microbiology · 2018Article
- Bound Substrate in the Structure of Cyanobacterial Branching Enzyme Supports a New Mechanistic Model.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Branching enzyme (BE) catalyzes formation of the branch points in glycogen and amylopectin by cleavage of the alpha-1,4 linkage and its subsequent transfer to the alpha-1,6 position. We have identified a novel BE encoded by an uncharacterized open reading frame (TK1436) of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. TK1436 encodes a conserved protein showing similarity to members of glycoside hydrolase family 57 (GH-57 family). At the C terminus of the TK1436 protein, two copies of a helix-hairpin-helix (HhH) motif were found. TK1436 orthologs are distributed in archaea of the order Thermococcales, cyanobacteria, some actinobacteria, and a few other bacterial species. When recombinant TK1436 protein was incubated with amylose used as the substrate, a product peak was detected by high-performance anion-exchange chromatography, eluting more slowly than the substrate. Isoamylase treatment of the reaction mixture significantly increased the level of short-chain alpha-glucans, indicating that the reaction product contained many alpha-1,6 branching points. The TK1436 protein showed an optimal pH of 7.0, an optimal temperature of 70 degrees C, and thermostability up to 90 degrees C, as determined by the iodine-staining assay. These properties were the same when a protein devoid of HhH motifs (the TK1436DeltaH protein) was used. The average molecular weight of branched glucan after reaction with the TK1436DeltaH protein was over 100 times larger than that of the starting substrate. These results clearly indicate that TK1436 encodes a structurally novel BE belonging to the GH-57 family. Identification of an overlooked BE species provides new insights into glycogen biosynthesis in microorganisms.
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