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

The role of conserved arginine residue in loop 4 of glycoside hydrolase family 10 xylanases.

Bioscience, biotechnology, and biochemistry - 1 May 2005

Nishimoto Mamoru, Kitaoka Motomitsu, Fushinobu Shinya, Hayashi Kiyoshi

Abstract excerpt

An arginine residue in loop 4 connecting beta strand 4 and alpha-helix 4 is conserved in glycoside hydrolase family 10 (GH10) xylanases. The arginine residues, Arg(204) in xylanase A from Bacillus halodurans C-125 (XynA) and Arg(196) in xylanase B from Clostridium stercorarium F9 (XynB), were replaced by glutamic acid, lysine, or glutamine residues (XynA R204E, K and Q, and XynB R196E, K and Q). The...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Bacillus
Share to Clostridium

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

Share to Conserved Sequence

Share to Endo-1,4-beta Xylanases

Share to Hydrogen-Ion Concentration

Share to Protein Conformation

Share to Protein Structure, Secondary

Source

Identifiers

PMID: 15914908
DOI: 10.1271/bbb.69.904

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

The role of conserved arginine residue in loop 4 of glycoside hydrolase family 10 xylanases.PMID 15914908Read ↗

Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability.Semantic proximity Read ↗

A highly Conserved Aspartic Acid Residue of the Chitosanase from Bacillus Sp. TS Is Involved in the Substrate Binding.Semantic proximity Read ↗

Point mutation of a conserved arginine (104) to lysine introduces hypersensitivity to inhibition by glyphosate in the 5-enolpyruvylshikimate-3-phosphate synthase of Bacillus subtilis.Semantic proximity Read ↗

Improving the alkalophilic performances of the Xyl1 xylanase from Streptomyces sp. S38: structural comparison and mutational analysis.Semantic proximity Read ↗

How the substitution of K188 of trypsin binding site by aromatic amino acids can influence the processing of beta-casein.Semantic proximity Read ↗

Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase.Semantic proximity Read ↗

Activity-stability trade-off observed in variants at position 315 of the GH10 xylanase XynR.Semantic proximity Read ↗

On the functional role of Arg172 in substrate binding and allosteric transition in Escherichia coli glucosamine-6-phosphate deaminase.Semantic proximity Read ↗

Specific characterization of substrate and inhibitor binding sites of a glycosyl hydrolase family 11 xylanase from Aspergillus niger.Semantic proximity Read ↗

Structural and functional role of Gly281 in L-asparaginase from Erwinia carotovora.Semantic proximity Read ↗

Engineering the pH-optimum of activity of the GH12 family endoglucanase by site-directed mutagenesis.Semantic proximity Read ↗

Study of the active site residues of a glycoside hydrolase family 8 xylanase.Semantic proximity Read ↗

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