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Evolution of a highly active and enantiospecific metalloenzyme from short peptides.
- Source :
-
Science (New York, N.Y.) [Science] 2018 Dec 14; Vol. 362 (6420), pp. 1285-1288. - Publication Year :
- 2018
-
Abstract
- Primordial sequence signatures in modern proteins imply ancestral origins tracing back to simple peptides. Although short peptides seldom adopt unique folds, metal ions might have templated their assembly into higher-order structures in early evolution and imparted useful chemical reactivity. Recapitulating such a biogenetic scenario, we have combined design and laboratory evolution to transform a zinc-binding peptide into a globular enzyme capable of accelerating ester cleavage with exacting enantiospecificity and high catalytic efficiency ( k <subscript>cat</subscript> / K <subscript>M</subscript> ~ 10 <superscript>6</superscript> M <superscript>-1</superscript> s <superscript>-1</superscript> ). The simultaneous optimization of structure and function in a naïve peptide scaffold not only illustrates a plausible enzyme evolutionary pathway from the distant past to the present but also proffers exciting future opportunities for enzyme design and engineering.<br /> (Copyright © 2018 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.)
Details
- Language :
- English
- ISSN :
- 1095-9203
- Volume :
- 362
- Issue :
- 6420
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 30545884
- Full Text :
- https://doi.org/10.1126/science.aau3744