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...

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Main Authors: Ana Obaha, Marko Novinec
Format: Article
Language:English
Published: MDPI AG 2023-12-01
Series:International Journal of Molecular Sciences
Subjects:
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.
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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