Host–Guest Allosteric Control of an Artificial Phosphatase

[Image: see text] The activity of many enzymes is regulated by associative processes. To model this mechanism, we report here that the conformation of an unstructured bimetallic Zn(II) complex can be controlled by its inclusion in the cavity of a γ-cyclodextrin. This results in the formation of a ca...

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Autores principales: Czescik, Joanna, Lyu, Yanchao, Neuberg, Samuele, Scrimin, Paolo, Mancin, Fabrizio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7997383/
https://www.ncbi.nlm.nih.gov/pubmed/32212681
http://dx.doi.org/10.1021/jacs.9b12699
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author Czescik, Joanna
Lyu, Yanchao
Neuberg, Samuele
Scrimin, Paolo
Mancin, Fabrizio
author_facet Czescik, Joanna
Lyu, Yanchao
Neuberg, Samuele
Scrimin, Paolo
Mancin, Fabrizio
author_sort Czescik, Joanna
collection PubMed
description [Image: see text] The activity of many enzymes is regulated by associative processes. To model this mechanism, we report here that the conformation of an unstructured bimetallic Zn(II) complex can be controlled by its inclusion in the cavity of a γ-cyclodextrin. This results in the formation of a catalytic bimetallic site for the hydrolytic cleavage of the RNA model substrate HPNP, whose reactivity is 30-fold larger with respect to the unstructured complex. Competitive inhibition with 1-adamantanecarboxylate displaces the metal complex from the cyclodextrin decreasing the reactivity.
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spelling pubmed-79973832021-03-29 Host–Guest Allosteric Control of an Artificial Phosphatase Czescik, Joanna Lyu, Yanchao Neuberg, Samuele Scrimin, Paolo Mancin, Fabrizio J Am Chem Soc [Image: see text] The activity of many enzymes is regulated by associative processes. To model this mechanism, we report here that the conformation of an unstructured bimetallic Zn(II) complex can be controlled by its inclusion in the cavity of a γ-cyclodextrin. This results in the formation of a catalytic bimetallic site for the hydrolytic cleavage of the RNA model substrate HPNP, whose reactivity is 30-fold larger with respect to the unstructured complex. Competitive inhibition with 1-adamantanecarboxylate displaces the metal complex from the cyclodextrin decreasing the reactivity. American Chemical Society 2020-03-26 2020-04-15 /pmc/articles/PMC7997383/ /pubmed/32212681 http://dx.doi.org/10.1021/jacs.9b12699 Text en Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Czescik, Joanna
Lyu, Yanchao
Neuberg, Samuele
Scrimin, Paolo
Mancin, Fabrizio
Host–Guest Allosteric Control of an Artificial Phosphatase
title Host–Guest Allosteric Control of an Artificial Phosphatase
title_full Host–Guest Allosteric Control of an Artificial Phosphatase
title_fullStr Host–Guest Allosteric Control of an Artificial Phosphatase
title_full_unstemmed Host–Guest Allosteric Control of an Artificial Phosphatase
title_short Host–Guest Allosteric Control of an Artificial Phosphatase
title_sort host–guest allosteric control of an artificial phosphatase
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7997383/
https://www.ncbi.nlm.nih.gov/pubmed/32212681
http://dx.doi.org/10.1021/jacs.9b12699
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