Co(II) Substitution Enhances the Esterase Activity of a de Novo Designed Zn(II) Carbonic Anhydrase

Carbonic Anhydrases (CAs) have been a target for de novo protein designers due to the simplicity of the active site and rapid rate of the reaction. The first reported mimic contained a Zn(II) bound to three histidine imidazole nitrogens and an exogenous water molecule, hence closely mimicking the na...

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Bibliographic Details
Published in:	Chemistry : a European journal Vol. 30; no. 24; pp. e202304367 - n/a
Main Authors:	Borghesani, Valentina, Zastrow, Melissa L., Tolbert, Audrey E., Deb, Aniruddha, Penner‐Hahn, James E., Pecoraro, Vincent L.
Format:	Journal Article
Language:	English
Published:	Germany Wiley Subscription Services, Inc 25-04-2024
Subjects:	Carbonic anhydrase Carbonic anhydrase II Carbonic anhydrases Carbonic Anhydrases - chemistry Carbonic Anhydrases - metabolism Catalysis Catalytic Domain Cobalt Cobalt - chemistry Coordination Coordination Complexes - chemistry Coordination Complexes - metabolism Enzyme activity Esterases - chemistry Esterases - metabolism Histidine Humans Hydrogen-Ion Concentration Hydrolysis Imidazole Kinetics Metals Nitrophenols - chemistry Nitrophenols - metabolism Peptides and proteins pH effects Protein kinase A Spectroscopy Substitution reactions Zinc Zinc - chemistry Hydrolysis Peptides and proteins Enzyme activity Coordination Metals
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