Stereoselective hydrolysis catalyzed by a Bacillus endoglucanase in family D.
An endoglucanase in family D, purified from a strain of Bacillus, was found to catalyze the hydrolysis of p-nitrophenyl beta-D-cellotrioside to generate alpha-cellobiose, as determined by 1H-NMR spectroscopy. The hydrolysis of the beta-1,4 glucosidic bond by the enzyme proceeds, therefore, by an inversion mechanism. Furthermore, the interconversion of the alpha- and beta-anomeric protons in the products of hydrolysis, after equilibrium had been reached by mutarotation, was directly characterized by magnetization transfer NMR experiment that exploited the truncated driven nuclear Overhauser effect.
Kawaminami
S
S
Biological Science Laboratories, Kao Corporation, Tochigi, Japan.
Ozaki
K
K
Ito
S
S
D001412:Bacillus subtilis / Q000201:enzymology*; D002475:Cellobiose / Q000378:metabolism; D002480:Cellulase / Q000378:metabolism*; D006868:Hydrolysis; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D009578:Nitrobenzenes / Q000737:chemistry / Q000378:metabolism*; D014312:Trisaccharides / Q000737:chemistry / Q000378:metabolism*
C094834:4-nitrophenyl cellotrioside; D009578:Nitrobenzenes; D014312:Trisaccharides; D002475:Cellobiose; D002480:Cellulase