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Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer

[Image: see text] The enzymes that facilitate phosphate and sulfate hydrolysis are among the most proficient natural catalysts known to date. Interestingly, a large number of these enzymes are promiscuous catalysts that exhibit both phosphatase and sulfatase activities in the same active site and, o...

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Autores principales: Pabis, Anna, Duarte, Fernanda, Kamerlin, Shina C. L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2016
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4899807/
https://www.ncbi.nlm.nih.gov/pubmed/27187273
http://dx.doi.org/10.1021/acs.biochem.6b00297
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author Pabis, Anna
Duarte, Fernanda
Kamerlin, Shina C. L.
author_facet Pabis, Anna
Duarte, Fernanda
Kamerlin, Shina C. L.
author_sort Pabis, Anna
collection PubMed
description [Image: see text] The enzymes that facilitate phosphate and sulfate hydrolysis are among the most proficient natural catalysts known to date. Interestingly, a large number of these enzymes are promiscuous catalysts that exhibit both phosphatase and sulfatase activities in the same active site and, on top of that, have also been demonstrated to efficiently catalyze the hydrolysis of other additional substrates with varying degrees of efficiency. Understanding the factors that underlie such multifunctionality is crucial both for understanding functional evolution in enzyme superfamilies and for the development of artificial enzymes. In this Current Topic, we have primarily focused on the structural and mechanistic basis for catalytic promiscuity among enzymes that facilitate both phosphoryl and sulfuryl transfer in the same active site, while comparing this to how catalytic promiscuity manifests in other promiscuous phosphatases. We have also drawn on the large number of experimental and computational studies of selected model systems in the literature to explore the different features driving the catalytic promiscuity of such enzymes. Finally, on the basis of this comparative analysis, we probe the plausible origins and determinants of catalytic promiscuity in enzymes that catalyze phosphoryl and sulfuryl transfer.
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spelling pubmed-48998072016-06-10 Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer Pabis, Anna Duarte, Fernanda Kamerlin, Shina C. L. Biochemistry [Image: see text] The enzymes that facilitate phosphate and sulfate hydrolysis are among the most proficient natural catalysts known to date. Interestingly, a large number of these enzymes are promiscuous catalysts that exhibit both phosphatase and sulfatase activities in the same active site and, on top of that, have also been demonstrated to efficiently catalyze the hydrolysis of other additional substrates with varying degrees of efficiency. Understanding the factors that underlie such multifunctionality is crucial both for understanding functional evolution in enzyme superfamilies and for the development of artificial enzymes. In this Current Topic, we have primarily focused on the structural and mechanistic basis for catalytic promiscuity among enzymes that facilitate both phosphoryl and sulfuryl transfer in the same active site, while comparing this to how catalytic promiscuity manifests in other promiscuous phosphatases. We have also drawn on the large number of experimental and computational studies of selected model systems in the literature to explore the different features driving the catalytic promiscuity of such enzymes. Finally, on the basis of this comparative analysis, we probe the plausible origins and determinants of catalytic promiscuity in enzymes that catalyze phosphoryl and sulfuryl transfer. American Chemical Society 2016-05-17 2016-06-07 /pmc/articles/PMC4899807/ /pubmed/27187273 http://dx.doi.org/10.1021/acs.biochem.6b00297 Text en Copyright © 2016 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes.
spellingShingle Pabis, Anna
Duarte, Fernanda
Kamerlin, Shina C. L.
Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer
title Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer
title_full Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer
title_fullStr Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer
title_full_unstemmed Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer
title_short Promiscuity in the Enzymatic Catalysis of Phosphate and Sulfate Transfer
title_sort promiscuity in the enzymatic catalysis of phosphate and sulfate transfer
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4899807/
https://www.ncbi.nlm.nih.gov/pubmed/27187273
http://dx.doi.org/10.1021/acs.biochem.6b00297
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