Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria.

Structure (London, England : 1993) - 7 Feb 2017

Bai Yuxiang, Gangoiti Joana, Dijkstra Bauke W, Dijkhuizen Lubbert, Pijning Tjaard

Abstract excerpt

Food processing and refining has dramatically changed the human diet, but little is known about whether this affected the evolution of enzymes in human microbiota. We present evidence that glycoside hydrolase family 70 (GH70) glucansucrases from lactobacilli, synthesizing α-glucan-type extracellular polysaccharides from sucrose, likely evolved from GH13 starch-acting α-amylases, via GH70...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to alpha-Amylases
Share to Carbohydrate Sequence

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Dietary Carbohydrates

Share to Glycogen Debranching Enzyme System

Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Starch

Share to Sucrose

Source

Identifiers

PMID: 28065507
DOI: 10.1016/j.str.2016.11.023

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal Structure of 4,6-α-Glucanotransferase Supports Diet-Driven Evolution of GH70 Enzymes from α-Amylases in Oral Bacteria.PMID 28065507Read ↗

An 1,4-α-glucosyltransferase defines a new maltodextrin catabolism scheme in <i>Lactobacillus acidophilus</i>Semantic proximity Read ↗

Discovery of α-l-arabinopyranosidases from human gut microbiome expands the diversity within glycoside hydrolase family 42.Semantic proximity Read ↗

Draft Genome Sequences of 18 Oral Streptococcus Strains That Encode Amylase-Binding ProteinsSemantic proximity Read ↗

Bacteroides thetaiotaomicron generates diverse α-mannosidase activities through subtle evolution of a distal substrate-binding motif.Semantic proximity Read ↗

Molecular details of a starch utilization pathway in the human gut symbiont E ubacterium rectaleSemantic proximity Read ↗

Mannose foraging by Bacteroides thetaiotaomicron: structure and specificity of the beta-mannosidase, BtMan2A.Semantic proximity Read ↗

Discovery and Development of Promiscuous O-Glycan Hydrolases for Removal of Intact Sialyl T-Antigen.Semantic proximity Read ↗

Directed Mutation of Two Key Amino Acid Residues Alters the Product Structure of the New 4,6-α-Glucanotransferase from Bacillus sporothermodurans.Semantic proximity Read ↗

Novel carbohydrate binding modules in the surface anchored α-amylase of Eubacterium rectale provide a molecular rationale for the range of starches used by this organism in the human gut.Semantic proximity Read ↗

Residue Leu940 has a crucial role in the linkage and reaction specificity of the glucansucrase GTF180 of the probiotic bacterium Lactobacillus reuteri 180.Semantic proximity Read ↗

Global Profiling of Carbohydrate Active Enzymes in Human Gut MicrobiomeSemantic proximity Read ↗

Acceptor Subsite Mutants of Limosilactobacillus fermentum NCC 2970 GtfB 4,3-α-Glucanotransferase Regulate the Ratio of (α1 → 3)/(α1 → 6) Linkages in Biosynthesized α-Glucans.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.