
Dependence upon pH of Steady‐State Parameters for the β‐Galactosidase‐Catalysed Hydrolyses of β‐D‐Galactopyranosyl Derivatives of Different Chemical Types
Author(s) -
WITHERS Stephen G.,
SINNOTT Michael L.,
JULLIEN Magali,
YON Jeanine M.,
VIRATELLE Odile M.
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12373.x
Subject(s) - pyridinium , galactosides , chemistry , hydrolysis , catalysis , steady state (chemistry) , aryl , galactosidases , organic chemistry , stereochemistry , enzyme , beta galactosidase , biochemistry , alkyl , gene expression , gene
The effect of pH upon the β‐glactosidase‐catalyzed hydrolyses of aryl galactosides is essentially similar for each of the three steps of their hydrolysis. It differs markedly from that on the hydrolysis of galactosyl pyridinium salts; these proceed through a ‘non‐bottleneck’ pathway. While pH increase abolishes the rate of every step of the reaction for aryl galactosides, it favors the first step of hydrolysis of the galactosyl pyridinium salts, which supports the hypothesis that catalysis of these compounds originates largely in non‐covalent interactions.