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Substrate specificity, regiospecificity, and processivity in glycoside hydrolase family 74
- Source :
- Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (36), pp.13233-13247. ⟨10.1074/jbc.RA119.009861⟩, Journal of Biological Chemistry 36 (294), 13233-13247. (2019), Journal of Biological Chemistry, 2019, 294 (36), pp.13233-13247. ⟨10.1074/jbc.RA119.009861⟩
- Publication Year :
- 2019
- Publisher :
- HAL CCSD, 2019.
-
Abstract
- International audience; Glycoside hydrolase family 74 (GH74) is a historically important family of endo--glucanases. On the basis of early reports of detectable activity on cellulose and soluble cellulose derivatives, GH74 was originally considered to be a "cellulase" family, although more recent studies have generally indicated a high specificity toward the ubiquitous plant cell wall matrix glycan xyloglucan. Previous studies have indicated that GH74 xyloglu-canases differ in backbone cleavage regiospecificities and can adopt three distinct hydrolytic modes of action: exo, endo-dis-sociative, and endo-processive. To improve functional predictions within GH74, here we coupled in-depth biochemical characterization of 17 recombinant proteins with structural biology-based investigations in the context of a comprehensive molecular phylogeny, including all previously characterized family members. Elucidation of four new GH74 tertiary structures , as well as one distantly related dual seven-bladed -propeller protein from a marine bacterium, highlighted key structure-function relationships along protein evolutionary trajectories. We could define five phylogenetic groups, which delineated the mode of action and the regiospecificity of GH74 members. At the extremes, a major group of enzymes diverged to hydrolyze the backbone of xyloglucan nonspecifically with a dissociative mode of action and relaxed backbone regiospecific-ity. In contrast, a sister group of GH74 enzymes has evolved a large hydrophobic platform comprising 10 subsites, which facilitates processivity. Overall, the findings of our study refine our understanding of catalysis in GH74, providing a framework for future experimentation as well as for bioinformatics predictions of sequences emerging from (meta)genomic studies.
- Subjects :
- Models, Molecular
0301 basic medicine
enzyme structure-function relationships cellulase
Glycoside Hydrolases
enzyme evolution
Protein Conformation
[SDV]Life Sciences [q-bio]
Context (language use)
xyloglucanase
Crystallography, X-Ray
Biochemistry
Substrate Specificity
carbohydrate-active enzymes (CAZymes)
03 medical and health sciences
chemistry.chemical_compound
xyloglucan
glycobiology
Phylogenetics
Hydrolase
plant cell wall
Editors' Picks
Glycoside hydrolase
carbohydrate metabolism
Mode of action
protein evolution
Molecular Biology
molecular phylogeny
X-ray crystallography
Bacteria
030102 biochemistry & molecular biology
glycoside hydrolase family 74 (GH74)
Fungi
Stereoisomerism
Cell Biology
Processivity
hemicellulose
Xyloglucan
phylogenetics
Kinetics
polysaccharide
glycosidase
processivity
structure-function
enzyme structure-function relationships
cellulase
030104 developmental biology
chemistry
Structural biology
processivity structure-function
Biocatalysis
Subjects
Details
- Language :
- English
- ISSN :
- 00219258 and 1083351X
- Database :
- OpenAIRE
- Journal :
- Journal of Biological Chemistry, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2019, 294 (36), pp.13233-13247. ⟨10.1074/jbc.RA119.009861⟩, Journal of Biological Chemistry 36 (294), 13233-13247. (2019), Journal of Biological Chemistry, 2019, 294 (36), pp.13233-13247. ⟨10.1074/jbc.RA119.009861⟩
- Accession number :
- edsair.doi.dedup.....2e765d801c74cfa53138766eeeda1980