Structural insights into the effect of active-site mutation on the catalytic mechanism of carbonic anhydrase.

ABSTRACT: Enzymes are catalysts of biological processes. Significant insight into their catalytic mechanisms has been obtained by relating site-directed mutagenesis studies to kinetic activity assays. However, revealing the detailed relationship between structural modifications and functional changes remains challenging owing to the lack of information on reaction intermediates and of a systematic way of connecting them to the measured kinetic parameters. Here, a systematic approach to investigate the effect of an active-site-residue mutation on a model enzyme, human carbonic anhydrase II (CA II), is described. Firstly, structural analysis is performed on the crystallographic intermediate states of native CA II and its V143I variant. The structural comparison shows that the binding affinities and co

SUBMITTER: Kim JK 

PROVIDER: S-EPMC7642793 | biostudies-literature | 2020 Nov

REPOSITORIES: biostudies-literature