Related Experiment Video
Updated: Sep 23, 2026

Anti-virulent Disruption of Pathogenic Biofilms using Engineered Quorum-quenching Lactonases
Published on: January 1, 2016
Interrupted catalytic domain structures in xylanases from two distantly related strains of Prevotella ruminicola
H J Flint1, T R Whitehead, J C Martin
1Rowett Research Institute, Bucksburn, Aberdeen, UK. h.nflint@rri.sari.ac.uk
Abstract:
Two xylanases from the rumen anaerobic bacterium Prevotella ruminicola were found to possess highly unusual structures in which family 10 catalytic domains are interrupted by unrelated sequences. XynC from P. ruminicola B(1)4 carries a 160 amino-acid insertion, while a P. ruminicola D31d xylanase carries an unrelated region of 280 amino acids, containing an imperfect 130 amino-acid duplication. Both regions of family 10 similarity were shown to be essential for activity of the D31d enzyme.
More Related Videos
11:49Sequencing of Plant Wall Heteroxylans Using Enzymic, Chemical (Methylation) and Physical (Mass Spectrometry, Nuclear Magnetic Resonance) Techniques
Published on: March 24, 2016
11:27X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Related Concept Videos
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Oligosaccharide Assembly
Multiple sugar molecules that may or may...
Catalytically Perfect Enzymes
Restriction Enzymes
The host bacteria protect their own genomic DNA from these enzymes by methylating these sites. Some...
Bacterial Phylum Spirochaetes
Archaeal Cell Wall