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An enzyme in disguise
The enzyme carbonic anhydrase binds its zinc ion by three histidine residues in a similar manner to the way copper is bound to nitrite reductase. This remote similarity has now been shown to be real [Andring et al. (2020). IUCrJ, 7, 287–293]. A carbonic anhydrase with two bound copper ions is also a...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7055377/ https://www.ncbi.nlm.nih.gov/pubmed/32148841 http://dx.doi.org/10.1107/S2052252520002481 |
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author | Liljas, Anders |
author_facet | Liljas, Anders |
author_sort | Liljas, Anders |
collection | PubMed |
description | The enzyme carbonic anhydrase binds its zinc ion by three histidine residues in a similar manner to the way copper is bound to nitrite reductase. This remote similarity has now been shown to be real [Andring et al. (2020). IUCrJ, 7, 287–293]. A carbonic anhydrase with two bound copper ions is also a nitrite reductase. |
format | Online Article Text |
id | pubmed-7055377 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-70553772020-03-06 An enzyme in disguise Liljas, Anders IUCrJ Scientific Commentaries The enzyme carbonic anhydrase binds its zinc ion by three histidine residues in a similar manner to the way copper is bound to nitrite reductase. This remote similarity has now been shown to be real [Andring et al. (2020). IUCrJ, 7, 287–293]. A carbonic anhydrase with two bound copper ions is also a nitrite reductase. International Union of Crystallography 2020-02-29 /pmc/articles/PMC7055377/ /pubmed/32148841 http://dx.doi.org/10.1107/S2052252520002481 Text en © Anders Liljas 2020 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Scientific Commentaries Liljas, Anders An enzyme in disguise |
title | An enzyme in disguise |
title_full | An enzyme in disguise |
title_fullStr | An enzyme in disguise |
title_full_unstemmed | An enzyme in disguise |
title_short | An enzyme in disguise |
title_sort | enzyme in disguise |
topic | Scientific Commentaries |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7055377/ https://www.ncbi.nlm.nih.gov/pubmed/32148841 http://dx.doi.org/10.1107/S2052252520002481 |
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