title: Evidence for lysozyme-type mechanism of hydrolysis in xylanases.
abstract: In the last year several new xylanase three-dimensional structures were solved. Examination of these new structures in combination with recently obtained data from site-directed mutagenesis and kinetic analysis provided insights into the catalytic mechanism of xylanases. It is now possible to determine the type of mechanism by which xylanases hydrolyse a complex substrate such as xylan.
authors.affiliation: Centre de recherche en microbiologie appliquée, Institut Armand-Frappiet, Université du Québec, Canada.
authors.forename: C
authors.initials: C
authors.lastname: Dupont
authors.forename: D
authors.initials: D
authors.lastname: Kluepfel
authors.forename: R
authors.initials: R
authors.lastname: Morosoli
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006868:Hydrolysis; D008958:Models, Molecular; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009113:Muramidase / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D017510:Protein Folding; D016415:Sequence Alignment; D013379:Substrate Specificity; D043325:Xylan Endo-1,3-beta-Xylosidase; D014990:Xylans / Q000378:metabolism; D014995:Xylosidases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D014990:Xylans; D014995:Xylosidases; D009113:Muramidase; D043325:Xylan Endo-1,3-beta-Xylosidase