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

Rational enzyme design for controlled functionalization of acetylated xylan for cell-free polymer biosynthesis.

Carbohydrate polymers - 1 Dec 2021

Wang Hsin-Tzu, Bharadwaj Vivek S, Yang Jeong-Yeh, Curry Thomas M, Moremen Kelley W, Bomble Yannick J, Urbanowicz Breeanna R

Abstract excerpt

Xylan O-acetyltransferase 1 (XOAT1) is involved in O-acetylating the backbone of hemicellulose xylan. Recent structural analysis of XOAT1 showed two unequal lobes forming a cleft that is predicted to accommodate and position xylan acceptors into proximity with the catalytic triad. Here, we used docking and molecular dynamics simulations to investigate the optimal orientation of xylan in the binding cleft of XOAT1...

Read the complete abstract on PubMed

Topics

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

Share to Acetylation
Share to Acetyltransferases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Arabidopsis Proteins

Share to Catalytic Domain

Share to Molecular Docking Simulation

Share to Molecular Dynamics Simulation

Share to Mutagenesis, Site-Directed

Share to Xylans

Source

Open in PubMed Open full text

Identifiers

PMID: 34560975
DOI: 10.1016/j.carbpol.2021.118564
PMCID: PMC8506904

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Rational enzyme design for controlled functionalization of acetylated xylan for cell-free polymer biosynthesis.PMID 34560975Read ↗

Molecular Mechanism of Polysaccharide Acetylation by the Arabidopsis Xylan O-acetyltransferase XOAT1.Semantic proximity Read ↗

The Arabidopsis DUF231 domain-containing protein ESK1 mediates 2-O- and 3-O-acetylation of xylosyl residues in xylan.Semantic proximity Read ↗

Regiospecific Acetylation of Xylan is Mediated by a Group of DUF231-Containing O-Acetyltransferases.Semantic proximity Read ↗

Biochemical characterization of rice xylan O-acetyltransferases.Semantic proximity Read ↗

Exploring the aglycone subsite of a GH11 xylanase for the synthesis of xylosides by transglycosylation reactions.Semantic proximity Read ↗

Active site architecture of an acetyl xylan esterase indicates a novel cold adaptation strategy.Semantic proximity Read ↗

The four Arabidopsis reduced wall acetylation genes are expressed in secondary wall-containing cells and required for the acetylation of xylan.Semantic proximity Read ↗

Insights into the roles of non-catalytic residues in the active site of a GH10 xylanase with activity on cellulose.Semantic proximity Read ↗

Improvement the thermostability and specific activity of acidic xylanase PjxA from Penicillium janthinellum via rigid flexible sites.Semantic proximity Read ↗

Mutations of Arabidopsis TBL32 and TBL33 Affect Xylan Acetylation and Secondary Wall Deposition.Semantic proximity Read ↗

Rational Engineering of a β-Glucosidase (H0HC94) from Glycosyl Hydrolase Family I (GH1) to Improve Catalytic Performance on Cellobiose.Semantic proximity Read ↗

Improving the Catalytic Properties of Xylanase from Alteromones Macleadii H35 Through Sequence Analysis.Semantic proximity Read ↗

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