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Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications
Proteases or peptidases are hydrolases that catalyze the breakdown of polypeptide chains into smaller peptide subunits. Proteases exist in all life forms, including archaea, bacteria, protozoa, insects, animals, and plants due to their vital functions in cellular processing and regulation. There are...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9147577/ https://www.ncbi.nlm.nih.gov/pubmed/35631755 http://dx.doi.org/10.3390/plants11101330 |
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author | Baharin, Anis Ting, Tiew-Yik Goh, Hoe-Han |
author_facet | Baharin, Anis Ting, Tiew-Yik Goh, Hoe-Han |
author_sort | Baharin, Anis |
collection | PubMed |
description | Proteases or peptidases are hydrolases that catalyze the breakdown of polypeptide chains into smaller peptide subunits. Proteases exist in all life forms, including archaea, bacteria, protozoa, insects, animals, and plants due to their vital functions in cellular processing and regulation. There are several classes of proteases in the MEROPS database based on their catalytic mechanisms. This review focuses on post-proline cleaving enzymes (PPCEs) from different peptidase families, as well as prolyl endoprotease/oligopeptidase (PEP/POP) from the serine peptidase family. To date, most PPCEs studied are of microbial and animal origins. Recently, there have been reports of plant PPCEs. The most common PEP/POP are members of the S9 family that comprise two conserved domains. The substrate-limiting β-propeller domain prevents unwanted digestion, while the α/β hydrolase catalyzes the reaction at the carboxyl-terminal of proline residues. PPCEs display preferences towards the Pro-X bonds for hydrolysis. This level of selectivity is substantial and has benefited the brewing industry, therapeutics for celiac disease by targeting proline-rich substrates, drug targets for human diseases, and proteomics analysis. Protein engineering via mutagenesis has been performed to improve heat resistance, pepsin-resistant capability, specificity, and protein turnover of PPCEs for pharmacological applications. This review aims to synthesize recent structure–function studies of PPCEs from different families of peptidases to provide insights into the molecular mechanism of prolyl cleaving activity. Despite the non-exhaustive list of PPCEs, this is the first comprehensive review to cover the biochemical properties, biological functions, and biotechnological applications of PPCEs from the diverse taxa. |
format | Online Article Text |
id | pubmed-9147577 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-91475772022-05-29 Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications Baharin, Anis Ting, Tiew-Yik Goh, Hoe-Han Plants (Basel) Review Proteases or peptidases are hydrolases that catalyze the breakdown of polypeptide chains into smaller peptide subunits. Proteases exist in all life forms, including archaea, bacteria, protozoa, insects, animals, and plants due to their vital functions in cellular processing and regulation. There are several classes of proteases in the MEROPS database based on their catalytic mechanisms. This review focuses on post-proline cleaving enzymes (PPCEs) from different peptidase families, as well as prolyl endoprotease/oligopeptidase (PEP/POP) from the serine peptidase family. To date, most PPCEs studied are of microbial and animal origins. Recently, there have been reports of plant PPCEs. The most common PEP/POP are members of the S9 family that comprise two conserved domains. The substrate-limiting β-propeller domain prevents unwanted digestion, while the α/β hydrolase catalyzes the reaction at the carboxyl-terminal of proline residues. PPCEs display preferences towards the Pro-X bonds for hydrolysis. This level of selectivity is substantial and has benefited the brewing industry, therapeutics for celiac disease by targeting proline-rich substrates, drug targets for human diseases, and proteomics analysis. Protein engineering via mutagenesis has been performed to improve heat resistance, pepsin-resistant capability, specificity, and protein turnover of PPCEs for pharmacological applications. This review aims to synthesize recent structure–function studies of PPCEs from different families of peptidases to provide insights into the molecular mechanism of prolyl cleaving activity. Despite the non-exhaustive list of PPCEs, this is the first comprehensive review to cover the biochemical properties, biological functions, and biotechnological applications of PPCEs from the diverse taxa. MDPI 2022-05-18 /pmc/articles/PMC9147577/ /pubmed/35631755 http://dx.doi.org/10.3390/plants11101330 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Baharin, Anis Ting, Tiew-Yik Goh, Hoe-Han Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications |
title | Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications |
title_full | Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications |
title_fullStr | Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications |
title_full_unstemmed | Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications |
title_short | Post-Proline Cleaving Enzymes (PPCEs): Classification, Structure, Molecular Properties, and Applications |
title_sort | post-proline cleaving enzymes (ppces): classification, structure, molecular properties, and applications |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9147577/ https://www.ncbi.nlm.nih.gov/pubmed/35631755 http://dx.doi.org/10.3390/plants11101330 |
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