Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II.

ABSTRACT:

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Bioengineering of a thermophilic enzyme starting from a mesophilic scaffold has proven to be a significant challenge, as several stabilizing elements have been proposed to be the foundation of thermal stability, including disulfide bridges, surface loop reduction, ionic pair networks, proline substitutions and aromatic clusters. This study emphasizes the effect of increasing the rigidity of human carbonic anhydrase II (HCA II; EC 4.2.1.1) via incorporation of proline residues at positions 170 and 234, which are located in surface loops that are able to accommodate restrictive main-chain conformations without rearrangement of the surrounding peptide backbone. Additionally, the effect of the compactness of HCA II was examined by deletion of a surface loop (residues 230-240

SUBMITTER: Boone CD 

PROVIDER: S-EPMC4400229 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature