Regulation of peptidase activity beyond the active site in human health and disease

Obaha, Ana (author), Novinec, Marko (author)

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.

• Language: English
• Keywords: protease, inhibition, allostery, exosite, glycosaminoglycan, interaction
• Typology: 1.02 - Review Article
• Organization: FKKT - Faculty of Chemistry and Chemical Technology
• Publication status: Published
• Publication version: Version of Record
• Publication date: 01.12.2023
• Year: 2023
• Number of pages: 24 str.
• Numbering: Vol. 24, iss. 23, art.17120
• PID: 20.500.12556/RUL-152765
• UDC: 577.15
• ISSN on article: 1422-0067
• DOI: 10.3390/ijms242317120
• COBISS.SI-ID: 174916355
• Publication date in RUL: 06.12.2023

Record is a part of a journal

• Title: International journal of molecular sciences
• Shortened title: Int. j. mol. sci.
• Publisher: MDPI
• ISSN: 1422-0067
• COBISS.SI-ID: 2779162

Licences

• License: CC BY 4.0, Creative Commons Attribution 4.0 International
• Link: http://creativecommons.org/licenses/by/4.0/
• Description: This is the standard Creative Commons license that gives others maximum freedom to do what they want with the work as long as they credit the author.

Secondary language

• Language: Slovenian
• Keywords: proteaze, inhibicija, alosterija, ekso-mesto, glikozaminoglikan, interakcije

Projects

• Funder: ARRS - Slovenian Research Agency
• Project number: N1-0211
• Name: Uvedba kooperativnosti v peptidaze za izboljšanje njihove aktivnosti in uravnavanja

• Funder: ARRS - Slovenian Research Agency
• Project number: P1-0179
• Name: Napredna organska sinteza in kataliza