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Innovation and tinkering in the evolution of oxidases
Although molecular oxygen is a relative newcomer to the biosphere, it has had a profound impact on metabolism. About 700 oxygen‐dependent enzymatic reactions are known, the vast majority of which emerged only after the appearance of oxygen in the biosphere, circa 3 billion years ago. Oxygen was a ma...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley & Sons, Inc.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9040561/ https://www.ncbi.nlm.nih.gov/pubmed/35481655 http://dx.doi.org/10.1002/pro.4310 |
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author | Jabłońska, Jagoda Tawfik, Dan S. |
author_facet | Jabłońska, Jagoda Tawfik, Dan S. |
author_sort | Jabłońska, Jagoda |
collection | PubMed |
description | Although molecular oxygen is a relative newcomer to the biosphere, it has had a profound impact on metabolism. About 700 oxygen‐dependent enzymatic reactions are known, the vast majority of which emerged only after the appearance of oxygen in the biosphere, circa 3 billion years ago. Oxygen was a major driving force for evolutionary innovation—~60% of all known oxygen‐dependent enzyme families emerged as such; that is, the founding ancestor was an O(2)‐dependent enzyme. The other 40% seem to have diverged by tinkering from pre‐existing proteins whose function was not related to oxygen. Here, we focus on the latter. We describe transitions from various enzyme classes, as well as from non‐enzymatic proteins, and we explore these transitions in terms of catalytic chemistry, metabolism, and protein structure. These transitions vary from subtle ones, such as simply repurposing oxidoreductases by replacing an electron acceptor such as NAD by O(2), to drastic changes in reaction mechanism, such as turning carboxylases and hydrolases into oxidases. The latter is more common and can occur with strikingly minor changes, for example, only one mutation in the active site. We further suggest that engineering enzymes to harness the extraordinary reactivity of oxygen may yield higher catabolic power and versatility. |
format | Online Article Text |
id | pubmed-9040561 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley & Sons, Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-90405612022-04-28 Innovation and tinkering in the evolution of oxidases Jabłońska, Jagoda Tawfik, Dan S. Protein Sci Reviews Although molecular oxygen is a relative newcomer to the biosphere, it has had a profound impact on metabolism. About 700 oxygen‐dependent enzymatic reactions are known, the vast majority of which emerged only after the appearance of oxygen in the biosphere, circa 3 billion years ago. Oxygen was a major driving force for evolutionary innovation—~60% of all known oxygen‐dependent enzyme families emerged as such; that is, the founding ancestor was an O(2)‐dependent enzyme. The other 40% seem to have diverged by tinkering from pre‐existing proteins whose function was not related to oxygen. Here, we focus on the latter. We describe transitions from various enzyme classes, as well as from non‐enzymatic proteins, and we explore these transitions in terms of catalytic chemistry, metabolism, and protein structure. These transitions vary from subtle ones, such as simply repurposing oxidoreductases by replacing an electron acceptor such as NAD by O(2), to drastic changes in reaction mechanism, such as turning carboxylases and hydrolases into oxidases. The latter is more common and can occur with strikingly minor changes, for example, only one mutation in the active site. We further suggest that engineering enzymes to harness the extraordinary reactivity of oxygen may yield higher catabolic power and versatility. John Wiley & Sons, Inc. 2022-04-26 2022-05 /pmc/articles/PMC9040561/ /pubmed/35481655 http://dx.doi.org/10.1002/pro.4310 Text en © 2022 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Reviews Jabłońska, Jagoda Tawfik, Dan S. Innovation and tinkering in the evolution of oxidases |
title | Innovation and tinkering in the evolution of oxidases |
title_full | Innovation and tinkering in the evolution of oxidases |
title_fullStr | Innovation and tinkering in the evolution of oxidases |
title_full_unstemmed | Innovation and tinkering in the evolution of oxidases |
title_short | Innovation and tinkering in the evolution of oxidases |
title_sort | innovation and tinkering in the evolution of oxidases |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9040561/ https://www.ncbi.nlm.nih.gov/pubmed/35481655 http://dx.doi.org/10.1002/pro.4310 |
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