A de novo designed metalloenzyme for the hydration of CO2.

ABSTRACT: Protein design will ultimately allow for the creation of artificial enzymes with novel functions and unprecedented stability. To test our current mastery of nature's approach to catalysis, a Zn(II) metalloenzyme was prepared using de novo design. α3DH3 folds into a stable single-stranded three-helix bundle and binds Zn(II) with high affinity using His3 O coordination. The resulting metalloenzyme catalyzes the hydration of CO2 better than any small molecule model of carbonic anhydrase and with an efficiency within 1400-fold of the fastest carbonic anhydrase isoform, CAII, and 11-fold of CAIII.

SUBMITTER: Cangelosi VM 

PROVIDER: S-EPMC4107010 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature