title: Structural analysis by circular dichroism of some enzymes involved in plant cell wall degradation.
abstract: Three enzymes which degrade different polysaccharide components of plant cell walls have been characterized by circular dichroism (CD). A bacterial endoglucanase, which in the native state forms part of a multiprotein cellulase complex, showed a tendency to form aggregates as measured by CD. Depending on its degree of aggregation, this enzyme displayed between 50% and 100% helical structure, whereas a bacterial xylanase and a fungal polygalacturonase exhibited more beta-sheet structure. The polygalacturonase was apparently devoid of helical structure.
authors.affiliation: Department of Protein Engineering Reading Laboratory, AFRC Institute of Food Research, UK.
authors.forename: P W
authors.initials: PW
authors.lastname: Goodenough
authors.forename: D C
authors.initials: DC
authors.lastname: Clark
authors.forename: A J
authors.initials: AJ
authors.lastname: Durrant
authors.forename: H J
authors.initials: HJ
authors.lastname: Gilbert
authors.forename: G P
authors.initials: GP
authors.lastname: Hazlewood
authors.forename: G
authors.initials: G
authors.lastname: Waksman
mesh_terms: D002473:Cell Wall / Q000378:metabolism*; D002480:Cellulase / Q000648:ultrastructure*; D002942:Circular Dichroism; D003013:Clostridium / Q000201:enzymology*; D005658:Fungi / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000648:ultrastructure*; D011096:Polygalacturonase / Q000648:ultrastructure*; D011487:Protein Conformation; D011551:Pseudomonas fluorescens / Q000201:enzymology*; D011994:Recombinant Proteins; D043325:Xylan Endo-1,3-beta-Xylosidase
chemical_list: D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; D011096:Polygalacturonase; D043325:Xylan Endo-1,3-beta-Xylosidase; D002480:Cellulase