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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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Autor principal: Rawlings, Neil D.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
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.
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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.
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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
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