PMID: 2492229Jan 2, 1989Paper

Mechanism and binding specificity of beta-glucosidase-catalyzed hydrolysis of cellobiose analogues studied by competition enzyme kinetics monitored by 1H-NMR spectroscopy

European Journal of Biochemistry
K Bock, B W Sigurskjold

Abstract

The application of high-resolution 1H-NMR spectroscopy to monitor substrate and product time dependencies in progress curve enzyme kinetics is described with beta-glucosidase-catalyzed hydrolyses of cellobiose analogues as examples. It is demonstrated that inhibition patterns, relative binding specificities and catalytic rates can be inferred from competition experiments with two or more substrates. It could be concluded from competition experiments that substrates which form less stable enzyme-substrate complexes than methyl beta-cellobioside are hydrolyzed faster than this reference substrate when they are the sole substrate, due to a lower activation energy in the catalytic step, but that they are hydrolyzed slower than the reference compound in direct competition, due to the formation of the less stable enzyme-substrate complex in the binding step.

References

Aug 1, 1975·The Biochemical Journal·A Cornish-Bowden
Sep 14, 1986·Biochemical and Biophysical Research Communications·S G WithersN R Gilkes
Apr 1, 1988·Analytical Biochemistry·S Y HwangC Gilvarg
Jan 15, 1986·The Biochemical Journal·E I Canela, R Franco
Apr 1, 1982·The Biochemical Journal·E A Boeker

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Citations

Sep 26, 2019·The Journal of Biological Chemistry·Robbins Puthenveetil, Olga Vinogradova

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