Structural analysis by circular dichroism of some enzymes involved in plant cell wall degradation.
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.
Goodenough
P W
PW
Department of Protein Engineering Reading Laboratory, AFRC Institute of Food Research, UK.
Clark
D C
DC
Durrant
A J
AJ
Gilbert
H J
HJ
Hazlewood
G P
GP
Waksman
G
G
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
D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; D011096:Polygalacturonase; D043325:Xylan Endo-1,3-beta-Xylosidase; D002480:Cellulase