title: Current perspectives on the families of glycoside hydrolases of Mycobacterium tuberculosis: their importance and prospects for assigning function to unknowns.
abstract: Glycoside hydrolases (GHs) are enzymes that catalyze the hydrolysis of glycosidic bonds in glycoconjugates, oligo- and polysaccharides. A classification of these enzymes based on conserved sequence and structure motifs supported by the Carbohydrate Active Enzyme (CAZy) database has proven useful in the systematic groupings of similar enzymes into families. The human pathogen Mycobacterium tuberculosis employs 30 GHs to perform a variety of different functions, which can be divided into four broad categories: α-glucan metabolism, peptidoglycan remodeling, β-glycan hydrolysis and α-demannosylation. The review presented here shows how the GHs that have been characterized play a role in each category. Expanding the genomic analysis of GH presence to other Mycobacterium species has highlighted the importance of certain families-most notably GH13 and GH23-in the general genomic make-up of mycobacteria. Since many GHs are still uncharacterized and considered as "conserved hypothetical" proteins, the grouping of them into respective families provides a strong prediction on their putative biological functions.
authors.affiliation: Centre d'études d'agents Pathogènes et Biotechnologies pour la Santé (CPBS), Centre National de la Recherche Scientifique FRE3689, Université de Montpellier, 1919 route de Mende, 34293 Montpellier, France nielvw@gmail.com.|Division of Molecular Biology and Human Genetics, Department of Biomedical Sciences, DST/NRF Centre of Excellence for Biomedical Tuberculosis Research/SAMRC Centre for Molecular and Cellular Biology, Faculty of Medicine and Health Sciences, Stellenbosch University, Stellenbosch, South Africa.|Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes, Centre National de la Recherche Scientifique (CNRS), Institut de Recherche pour le Développement, Faculté de Médecine, Aix-Marseille Université, 27 Bd Jean Moulin, 13005 Marseille, France.
authors.forename: Niël
authors.initials: N
authors.lastname: van Wyk
authors.affiliation: Unité de Recherche sur les Maladies Infectieuses et Tropicales Emergentes, Centre National de la Recherche Scientifique (CNRS), Institut de Recherche pour le Développement, Faculté de Médecine, Aix-Marseille Université, 27 Bd Jean Moulin, 13005 Marseille, France.
authors.forename: Michel
authors.initials: M
authors.lastname: Drancourt
authors.affiliation: Architecture et Fonction des Macromolécules Biologiques (AFMB), UMR 7257 CNRS, Université Aix-Marseille, 163 Avenue de Luminy, 13288 Marseille, France.|INRA, USC 1408 AFMB, 13288 Marseille, France.|Department of Biological Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.
authors.forename: Bernard
authors.initials: B
authors.lastname: Henrissat
authors.affiliation: Centre d'études d'agents Pathogènes et Biotechnologies pour la Santé (CPBS), Centre National de la Recherche Scientifique FRE3689, Université de Montpellier, 1919 route de Mende, 34293 Montpellier, France.|INSERM, CPBS, 34293 Montpellier, France.
authors.forename: Laurent
authors.initials: L
authors.lastname: Kremer
mesh_terms: D050260:Carbohydrate Metabolism / Q000235:genetics; D002473:Cell Wall / Q000201:enzymology* / Q000235:genetics; D017124:Conserved Sequence; D006001:Glycoconjugates / Q000235:genetics / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000145:classification / Q000235:genetics*; D006801:Humans; D006868:Hydrolysis; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000235:genetics / Q000472:pathogenicity; D011134:Polysaccharides / Q000235:genetics / Q000378:metabolism; D047071:beta-Glucans / Q000378:metabolism*
chemical_list: D006001:Glycoconjugates; D011134:Polysaccharides; D047071:beta-Glucans; D006026:Glycoside Hydrolases
keywords: CAZy database; Mycobacterium tuberculosis; Rpfs; glycoside hydrolase; trehalose