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Article Dans Une Revue (Article De Synthèse) Essays in Biochemistry Année : 2023

Effect of multi-modularity and spatial organization of glycoside hydrolases on catalysis

Résumé

The wide diversity among the carbohydrate active enzymes (CAZymes) reflects the equally broad versatility in terms of composition and chemicals bonds found in the plant cell wall polymers on which they are active. This diversity, is also expressed through the various strategies developed to circumvent the recalcitrance of these substrates to biological degradation. Glycoside hydrolases (GHs) are the most abundant of the CAZymes and are expressed as isolated catalytic modules or in association with carbohydrate binding module (CBM), acting in synergism within complex arrays of enzymes. This multi-modularity can be even more complex. The cellulosome presents a scaffold protein immobilized to the outer membrane of some microorganisms on which enzymes are grafted to prevent their dispersion and increase catalytic synergism. In Polysaccharide-Utilization Loci (PUL), GHs are also distributed across the membranes of some bacteria to coordinate the deconstruction of polysaccharides and the internalization of metabolizable carbohydrates. Although the study and characterization of these enzymatic activities need to take into account the entirety of this complex organization-in particular because of the dynamics involved in it-technical problems limit this study to isolated enzymes. However, these enzymatic complexes also have a spatio-temporal organization, whose still neglected aspect must be considered. In this review, the different levels of multi-modularity that can occur in GHs will be reviewed, from its simplest forms to the most complex. In addition, attempts to characterize or study the effect on catalytic activity of the spatial organization within GHs will be addressed.
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Dates et versions

hal-04038640 , version 1 (21-03-2023)

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Víctor Barba-Cedillo, Cédric Y Montanier. Effect of multi-modularity and spatial organization of glycoside hydrolases on catalysis. Essays in Biochemistry, 2023, 67 (3), pp.629-638. ⟨10.1042/EBC20220167⟩. ⟨hal-04038640⟩
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