Share This Author
Transfer of carbohydrate-active enzymes from marine bacteria to Japanese gut microbiota
It is shown that porphyranases and agarases are frequent in the Japanese population and that they are absent in metagenome data from North American individuals, which indicates that contact with non-sterile food may be a general factor in CAZyme diversity in human gut microbes.
Environmental and Gut Bacteroidetes: The Food Connection
This review presents the current knowledge on the role and mechanisms of polysaccharide degradation by Bacteroidetes in their respective habitats and addresses the potential links between gut and environmental bacteria through food consumption.
Structural Evidence for the Evolution of Xyloglucanase Activity from Xyloglucan Endo-Transglycosylases: Biological Implications for Cell Wall Metabolism[W]
Comprehensive bioinformatic analyses of XTH gene products, together with detailed kinetic data, strongly suggest that xyloglucanase activity has evolved as a gain of function in an ancestral GH16 XET to meet specific biological requirements during seed germination, fruit ripening, and rapid wall expansion.
The endo-beta-agarases AgaA and AgaB from the marine bacterium Zobellia galactanivorans: two paralogue enzymes with different molecular organizations and catalytic behaviours.
Two beta-agarase genes, agaA and agaB, were functionally cloned from the marine bacterium Zobellia galactanivorans and it is proposed that, reminiscent of the agarolytic system of Pseudoalteromonas atlantica, AgaA is specialized in the initial attack on solid-phase agarose, while AgaB is involved with the degradation of agarOSE fragments.
Bioconversion of red seaweed galactans: a focus on bacterial agarases and carrageenases
- G. Michel, Pi Nyval-Collen, T. Barbeyron, M. Czjzek, W. Helbert
- BiologyApplied Microbiology and Biotechnology
- 21 March 2006
How the active site topologies of these glycoside hydrolases influence their mode of action in heterogeneous phase is examined, to discuss the next challenges in the basic and applied field of the galactans of red algae and of their related degrading microorganisms.
Atomic resolution (1.0 A) crystal structure of Fusarium solani cutinase: stereochemical analysis.
- S. Longhi, M. Czjzek, V. Lamzin, A. Nicolas, C. Cambillau
- ChemistryJournal of Molecular Biology
- 16 May 1997
The availability of an accurate structure at atomic resolution and of meaningful estimates of the errors in its atomic parameters, allowed an extensive analysis of several stereochemical parameters, such as peptide planarity, main-chain and some side-chain bond distances, which revealed an appreciable extent of flexibility in the cutinase active site.
Genome structure and metabolic features in the red seaweed Chondrus crispus shed light on evolution of the Archaeplastida
- J. Collén, Betina M. Porcel, C. Boyen
- BiologyProceedings of the National Academy of Sciences
- 15 March 2013
An evolutionary scenario involving an ancestral red alga that was driven by early ecological forces to lose genes, introns, and intergenetic DNA is proposed; this loss was followed by an expansion of genome size as a consequence of activity of transposable elements.
Characterization of the first alginolytic operons in a marine bacterium: from their emergence in marine Flavobacteriia to their independent transfers to marine Proteobacteria and human gut…
- F. Thomas, T. Barbeyron, T. Tonon, S. Genicot, M. Czjzek, G. Michel
- Biology, Environmental ScienceEnvironmental Microbiology
- 1 September 2012
In-depth phylogenomic analyses reveal that such alginolytic operons originated from an ancestral marine flavobacterium and were independently transferred to marine proteobacteria and Japanese gut Bacteroides, gaining the capacity to assimilate the main polysaccharide of brown algae, an adaptive advantage in coastal environments but also in the gut microbiota of specific human population.
The crystal structure of HasA, a hemophore secreted by Serratia marcescens
The first crystal structure of such a hemophore, bound to a heme group at two different pH values and at a resolution of 1.9 Å is reported, which reveals a new original fold and suggests a hypothetical mechanism for both heme uptake and release.
The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes.
- M. Czjzek, M. Cicek, V. Zamboni, D. Bevan, B. Henrissat, A. Esen
- Chemistry, BiologyProceedings of the National Academy of Sciences…
- 5 December 2000
The mechanism and the site of substrate (i.e., aglycone) recognition and specificity were investigated in maize beta-glucosidase (Glu1) by x-ray crystallography by using crystals of a catalytically inactive mutant in complex with the natural substrate DIMBOAGlc and competitive inhibitor para-hydroxy-S-mandelonitrile beta- glucoside (dhurrin).