Biochemical properties of a beta-xylosidase from Clostridium cellulolyticum.
A 43-kDa beta-xylosidase from Clostridium cellulolyticum was purified to homogeneity. The enzyme releases xylose from p-nitrophenylxylose and xylodextrins with a degree of polymerization ranging between 2 and 5. The N-terminal amino acid sequence of the enzyme showed homologies with three other bacterial beta-xylosidases. By proton nuclear magnetic resonance spectroscopy, the enzyme was found to act by inverting the beta-anomeric configuration.
Saxena
S
S
Laboratoire de Biochimie et Génétique Moléculaire des Anaérobies, IFRC1, Centre National de la Recherche Scientifique, Marseille, France.
Fierobe
H P
HP
Gaudin
C
C
Guerlesquin
F
F
Belaich
J P
JP
D000595:Amino Acid Sequence; D003013:Clostridium / Q000201:enzymology* / Q000235:genetics; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D013237:Stereoisomerism; D014994:Xylose / Q000737:chemistry; D014995:Xylosidases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D014994:Xylose; D014995:Xylosidases; C026579:exo-1,4-beta-D-xylosidase