Literature DB >> 414801

Diffusion control in reversible enzyme reactions. Applications to carbonic anhydrase.

B Jönsson, H Wennerström.   

Abstract

The limit to the possible rate of reversible enzymatic reactions set by the diffusional motion has been considered. It is found that not only the diffusion of the reactants to the enzyme but also the diffusion away of the products can be rate limiting. To avoid assumptions about the detailed nature of the enzyme only diffusion in the bulk aqueous medium is treated. By such an approach one obtains an upper limit to the possible rate. In the latter half of the paper the derived general equations are applied to the possible suggested reaction schemes for the enzyme carbonic anhydrase. It is found that a scheme involving HCO3- as substrate for the dehydration process and a direct reaction between buffer and enzyme is comsistent with the limits set by the diffusional motion, while several other possibilities can be ruled out.

Entities:  

Mesh:

Substances:

Year:  1978        PMID: 414801     DOI: 10.1016/0301-4622(78)85005-4

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  1 in total

1.  Mechanism of inactivation on prion conversion of the Saccharomyces cerevisiae Ure2 protein.

Authors:  Ulrich Baxa; Vladislav Speransky; Alasdair C Steven; Reed B Wickner
Journal:  Proc Natl Acad Sci U S A       Date:  2002-04-16       Impact factor: 11.205

  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.