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Issue 4, 2008
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Transient kinetic studies of protein hydrolyses by endo- and exo-proteases on a 27 MHz quartz-crystal microbalance

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Abstract

We have compared endo- and exo-type protease reactions and characterized the enzymatic reaction mechanisms by determining all kinetic parameters (kon, koff, kcat, Kd = koff/kon, and Km = (koff + kcat)/kon) by following the mass change of the formation and the decay of the enzyme–substrate (ES) complex (kon and koff), and the formation of the product (kcat) on a 27 MHz quartz-crystal microbalance in aqueous solutions. The Km value was nearly equal to the Kd value for the endo-type protease (subtilisin and α-chymotrypsin); however, in the case of exo-type protease (carboxypeptidase P), the Km value was quite different from the Kd value, due to kcat ≫ koff.

Graphical abstract: Transient kinetic studies of protein hydrolyses by endo- and exo-proteases on a 27 MHz quartz-crystal microbalance

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Article information


Submitted
06 Nov 2007
Accepted
28 Nov 2007
First published
10 Jan 2008

Org. Biomol. Chem., 2008,6, 727-731
Article type
Paper

Transient kinetic studies of protein hydrolyses by endo- and exo-proteases on a 27 MHz quartz-crystal microbalance

H. Furusawa, H. Takano and Y. Okahata, Org. Biomol. Chem., 2008, 6, 727
DOI: 10.1039/B717171D

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