Literature DB >> 27358

Dependence upon pH of steady-state parameters for the beta-galactosidase-catalysed hydrolyses of beta-D-galactopyranosyl derivatives of different chemical types.

S G Withers, M Jullien, M L Sinnott, O M Viratelle, J M Yon.   

Abstract

The effect of pH upon the beta-galactosidase-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.

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Year:  1978        PMID: 27358     DOI: 10.1111/j.1432-1033.1978.tb12373.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  1 in total

1.  The catalytic consequences of experimental evolution. Transition-state structure during catalysis by the evolved beta-galactosidases of Escherichia coli (ebg enzymes) changed by a single mutational event.

Authors:  B F Li; D Holdup; C A Morton; M L Sinnott
Journal:  Biochem J       Date:  1989-05-15       Impact factor: 3.857

  1 in total

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