Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease
This comprehensive review addresses the intricate and multifaceted regulation of peptidase activity in human health and disease, providing a comprehensive investigation that extends well beyond the boundaries of the active site. Our review focuses on multiple mechanisms and highlights the important...
Main Authors: | , |
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Format: | Article |
Language: | English |
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MDPI AG
2023-12-01
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Series: | International Journal of Molecular Sciences |
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Online Access: | https://www.mdpi.com/1422-0067/24/23/17120 |
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author | Ana Obaha Marko Novinec |
author_facet | Ana Obaha Marko Novinec |
author_sort | Ana Obaha |
collection | DOAJ |
description | This comprehensive review addresses the intricate and multifaceted regulation of peptidase activity in human health and disease, providing a comprehensive investigation that extends well beyond the boundaries of the active site. Our review focuses on multiple mechanisms and highlights the important role of exosites, allosteric sites, and processes involved in zymogen activation. These mechanisms play a central role in shaping the complex world of peptidase function and are promising potential targets for the development of innovative drugs and therapeutic interventions. The review also briefly discusses the influence of glycosaminoglycans and non-inhibitory binding proteins on enzyme activities. Understanding their role may be a crucial factor in the development of therapeutic strategies. By elucidating the intricate web of regulatory mechanisms that control peptidase activity, this review deepens our understanding in this field and provides a roadmap for various strategies to influence and modulate peptidase activity. |
first_indexed | 2024-03-09T01:49:01Z |
format | Article |
id | doaj.art-875cf88bed704a6b894d64e43d51cce6 |
institution | Directory Open Access Journal |
issn | 1661-6596 1422-0067 |
language | English |
last_indexed | 2024-03-09T01:49:01Z |
publishDate | 2023-12-01 |
publisher | MDPI AG |
record_format | Article |
series | International Journal of Molecular Sciences |
spelling | doaj.art-875cf88bed704a6b894d64e43d51cce62023-12-08T15:18:28ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-12-0124231712010.3390/ijms242317120Regulation of Peptidase Activity beyond the Active Site in Human Health and DiseaseAna Obaha0Marko Novinec1Faculty of Chemistry and Chemical Technology, Department of Chemistry and Biochemistry, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, SloveniaFaculty of Chemistry and Chemical Technology, Department of Chemistry and Biochemistry, University of Ljubljana, Večna pot 113, SI-1000 Ljubljana, SloveniaThis comprehensive review addresses the intricate and multifaceted regulation of peptidase activity in human health and disease, providing a comprehensive investigation that extends well beyond the boundaries of the active site. Our review focuses on multiple mechanisms and highlights the important role of exosites, allosteric sites, and processes involved in zymogen activation. These mechanisms play a central role in shaping the complex world of peptidase function and are promising potential targets for the development of innovative drugs and therapeutic interventions. The review also briefly discusses the influence of glycosaminoglycans and non-inhibitory binding proteins on enzyme activities. Understanding their role may be a crucial factor in the development of therapeutic strategies. By elucidating the intricate web of regulatory mechanisms that control peptidase activity, this review deepens our understanding in this field and provides a roadmap for various strategies to influence and modulate peptidase activity.https://www.mdpi.com/1422-0067/24/23/17120proteaseinhibitionallosteryexositeglycosaminoglycaninteraction |
spellingShingle | Ana Obaha Marko Novinec Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease International Journal of Molecular Sciences protease inhibition allostery exosite glycosaminoglycan interaction |
title | Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease |
title_full | Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease |
title_fullStr | Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease |
title_full_unstemmed | Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease |
title_short | Regulation of Peptidase Activity beyond the Active Site in Human Health and Disease |
title_sort | regulation of peptidase activity beyond the active site in human health and disease |
topic | protease inhibition allostery exosite glycosaminoglycan interaction |
url | https://www.mdpi.com/1422-0067/24/23/17120 |
work_keys_str_mv | AT anaobaha regulationofpeptidaseactivitybeyondtheactivesiteinhumanhealthanddisease AT markonovinec regulationofpeptidaseactivitybeyondtheactivesiteinhumanhealthanddisease |