Mechanistic study of beta-xylosidase from Trichoderma koningii G-39

• Published in: Journal of biochemistry (Tokyo) Vol. 127; no. 2; pp. 315 - 320
• Main Authors: Li, Y.K, Yao, H.J, Pan, I.H
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.02.2000; The Japanese Biochemical Society
• Subjects: analogs & derivatives; antagonists & inhibitors; aryl-beta-d-xylopyranosides; arylxylosides; Beta; Binding, Competitive; Bronsted plot; chemistry; Deuterium; Dithiothreitol; Dithiothreitol - pharmacology; enzyme activity; Enzyme Inhibitors; Enzyme Inhibitors - pharmacology; enzyme reaction mechanisms; enzymology; Gluconates; Gluconates - pharmacology; glycosides; Glycosides - metabolism; Hypocrea koningii; Kinetics; Lactones; Magnetic Resonance Spectroscopy; Mechanics; mechanism; metabolism; pharmacology; Pyrones; Pyrones - pharmacology; secondary deuterium isotope effect; Stereoisomerism; Substrate Specificity; substrates; Trichoderma; Trichoderma - enzymology; Trichoderma koningii; xylan; Xylose; Xylose - analogs & derivatives; Xylose - pharmacology; Xylosidases; Xylosidases - antagonists & inhibitors; Xylosidases - chemistry; Xylosidases - metabolism; β-xylosidase

The catalytic mechanism of the β-xylosidase purified from the culture filtrate of Trichoderma koningii G-39 was investigated. By NMR spectroscopy, the stereochemistry of the enzyme catalyzing the hydrolysis of 2,4-dinitrophenyl and p-nitrophenyl-β-D-xylosides was found unequivocally to involve reten...