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Evolution of the Thermopsin Peptidase Family (A5)
Thermopsin is a peptidase from Sulfolobus acidocaldarius that is active at low pH and high temperature. From reversible inhibition with pepstatin, thermopsin is thought to be an aspartic peptidase. It is a member of the only family of peptidases to be restricted entirely to the archaea, namely pepti...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2013
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3842238/ https://www.ncbi.nlm.nih.gov/pubmed/24312173 http://dx.doi.org/10.1371/journal.pone.0078998 |
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author | Rawlings, Neil D. |
author_facet | Rawlings, Neil D. |
author_sort | Rawlings, Neil D. |
collection | PubMed |
description | Thermopsin is a peptidase from Sulfolobus acidocaldarius that is active at low pH and high temperature. From reversible inhibition with pepstatin, thermopsin is thought to be an aspartic peptidase. It is a member of the only family of peptidases to be restricted entirely to the archaea, namely peptidase family A5. Evolution within this family has been mapped, using a taxonomic tree based on the known classification of archaea. Homologues are found only in archaeans that are both hyperthermophiles and acidophiles, and this implies lateral transfer of genes between archaea, because species with homologues are not necessarily closely related. Despite the remarkable stability and activity in extreme conditions, no tertiary structure has been solved for any member of the family, and the catalytic mechanism is unknown. Putative catalytic residues have been predicted here by examination of aligned sequences. |
format | Online Article Text |
id | pubmed-3842238 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-38422382013-12-05 Evolution of the Thermopsin Peptidase Family (A5) Rawlings, Neil D. PLoS One Research Article Thermopsin is a peptidase from Sulfolobus acidocaldarius that is active at low pH and high temperature. From reversible inhibition with pepstatin, thermopsin is thought to be an aspartic peptidase. It is a member of the only family of peptidases to be restricted entirely to the archaea, namely peptidase family A5. Evolution within this family has been mapped, using a taxonomic tree based on the known classification of archaea. Homologues are found only in archaeans that are both hyperthermophiles and acidophiles, and this implies lateral transfer of genes between archaea, because species with homologues are not necessarily closely related. Despite the remarkable stability and activity in extreme conditions, no tertiary structure has been solved for any member of the family, and the catalytic mechanism is unknown. Putative catalytic residues have been predicted here by examination of aligned sequences. Public Library of Science 2013-11-27 /pmc/articles/PMC3842238/ /pubmed/24312173 http://dx.doi.org/10.1371/journal.pone.0078998 Text en © 2013 Neil David Rawlings http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Rawlings, Neil D. Evolution of the Thermopsin Peptidase Family (A5) |
title | Evolution of the Thermopsin Peptidase Family (A5) |
title_full | Evolution of the Thermopsin Peptidase Family (A5) |
title_fullStr | Evolution of the Thermopsin Peptidase Family (A5) |
title_full_unstemmed | Evolution of the Thermopsin Peptidase Family (A5) |
title_short | Evolution of the Thermopsin Peptidase Family (A5) |
title_sort | evolution of the thermopsin peptidase family (a5) |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3842238/ https://www.ncbi.nlm.nih.gov/pubmed/24312173 http://dx.doi.org/10.1371/journal.pone.0078998 |
work_keys_str_mv | AT rawlingsneild evolutionofthethermopsinpeptidasefamilya5 |