81972-21-6Relevant articles and documents
Effect of Aryl Substituents on the Kinetics of Inactivation of Glycosidases by Glycosylmethylaryltriazenes: Examination of the 'Suicide' Nature of these Inactivations
Sinnott, Michael L.,Tzotzos, George T.,Marshall, Susan E.
, p. 1665 - 1670 (2007/10/02)
The inactivation of the Mg2+-free form of the lacZ-β-galactosidase of Escherichia coli at 25.0 deg C by various β-D-galactopyranosylmethylaryltriazenes resembles the spontaneous, rather than the acid-catalysed decomposition of alkylaryltriazenes in that both the maximum first-order rate constant, and the second-order rate constant, are governed by a negative βlg value at pH 7.0 and at pH 8.0.Less extensive data with the β-xylosidase of Penicillium wortmanni and β-D-xylopyranosylmethylaryltriazenes give a similar result.Although the decomposition of the 2-(β-D-galactopyranosyl)ethyl compounds in aqueous solution is 5-10 fold faster than their lower homologues, β-galactosidase inactivation is 3-13 slower. β-D-Galactopyranosylmethyl-p-nitrophenyltriazene does not inactivate the lectin, RCA ricin.