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

Key Role of the Carboxyl Terminus of Hyaluronan Synthase in Processive Synthesis and Size Control of Hyaluronic Acid Polymers.

Biomacromolecules - 10 Apr 2017

Yang Ji, Cheng Fangyu, Yu Huimin, Wang Junting, Guo Zhigang, Stephanopoulos Gregory

Abstract excerpt

The essential pathophysiological roles of hyaluronic acid (HA) strongly depend on HA binding and HA size. Here we deployed the atomic vision of molecular dynamics (MD) simulation to experimentally investigate the influence of C-terminal mutations of Streptococcus equisimilis hyaluronan synthase (SeHAS) on HA product synthesis in Escherichia coli. R413 was vital for HA production, as the removal or mutation of...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Glucuronosyltransferase

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hyaluronic Acid

Share to Lysine

Share to Molecular Dynamics Simulation

Share to Molecular Weight

Share to Polymers

Share to Streptococcus

Source

Identifiers

PMID: 28192668
DOI: 10.1021/acs.biomac.6b01239

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Key Role of the Carboxyl Terminus of Hyaluronan Synthase in Processive Synthesis and Size Control of Hyaluronic Acid Polymers.PMID 28192668Read ↗

Hyaluronan synthase control of synthesis rate and hyaluronan product size are independent functions differentially affected by mutations in a conserved tandem B-X7-B motif.Semantic proximity Read ↗

Mutation of two intramembrane polar residues conserved within the hyaluronan synthase family alters hyaluronan product size.Semantic proximity Read ↗

The streptococcal hyaluronan synthases are inhibited by sulfhydryl-modifying reagents, but conserved cysteine residues are not essential for enzyme function.Semantic proximity Read ↗

The prophage-encoded hyaluronate lyase has broad substrate specificity and is regulated by the N-terminal domain.Semantic proximity Read ↗

Improving enzyme activity of glucosamine-6-phosphate synthase by semi-rational design strategy and computer analysis.Semantic proximity Read ↗

Hyaluronan Breakdown Contributes to Immune Defense against Group A StreptococcusSemantic proximity Read ↗

Kinetic properties of Streptococcus pneumoniae hyaluronate lyase.Semantic proximity Read ↗

Designed human serum hyaluronidase 1 variant, HYAL1DeltaL, exhibits activity up to pH 5.9.Semantic proximity Read ↗

Genetic variation reveals the enhanced microbial hyaluronan biosynthesis via atmospheric and room temperature plasma.Semantic proximity Read ↗

Hyaluronidase activity of human Hyal1 requires active site acidic and tyrosine residues.Semantic proximity Read ↗

Substitution of acidic residues near the catalytic Glu131 leads to human HYAL1 activity at neutral pH via charge-charge interactions.Semantic proximity Read ↗

The effect of double (S238F/W159H) mutations on the structure and dynamics of PET degrading enzyme.Semantic proximity Read ↗

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