Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions

Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes secreted by many organisms and viruses. LPMOs catalyze the oxidative cleavage of different types of polysaccharides and are today divided into eight families (AA9–11, AA13–17) within the Auxiliary Activity enzyme class of the CAZy da...

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Autores principales: Ketty C. Tamburrini, Nicolas Terrapon, Vincent Lombard, Bastien Bissaro, Sonia Longhi, Jean-Guy Berrin
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Publicado: MDPI AG 2021
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spelling oai:doaj.org-article:0ae01a8af9024c1885fd60382d45c3c62021-11-25T16:53:05ZBioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions10.3390/biom111116322218-273Xhttps://doaj.org/article/0ae01a8af9024c1885fd60382d45c3c62021-11-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1632https://doaj.org/toc/2218-273XLytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes secreted by many organisms and viruses. LPMOs catalyze the oxidative cleavage of different types of polysaccharides and are today divided into eight families (AA9–11, AA13–17) within the Auxiliary Activity enzyme class of the CAZy database. LPMOs minimal architecture encompasses a catalytic domain, to which can be appended a carbohydrate-binding module. Intriguingly, we observed that some LPMO sequences also display a C-terminal extension of varying length not associated with any known function or fold. Here, we analyzed 27,060 sequences from different LPMO families and show that 60% have a C-terminal extension predicted to be intrinsically disordered. Our analysis shows that these disordered C-terminal regions (dCTRs) are widespread in all LPMO families (except AA13) and differ in terms of sequence length and amino-acid composition. Noteworthily, these dCTRs have so far only been observed in LPMOs. LPMO-dCTRs share a common polyampholytic nature and an enrichment in serine and threonine residues, suggesting that they undergo post-translational modifications. Interestingly, dCTRs from AA11 and AA15 are enriched in redox-sensitive, conditionally disordered regions. The widespread occurrence of dCTRs in LPMOs from evolutionarily very divergent organisms, hints at a possible functional role and opens new prospects in the field of LPMOs.Ketty C. TamburriniNicolas TerraponVincent LombardBastien BissaroSonia LonghiJean-Guy BerrinMDPI AGarticleintrinsically disordered regionslytic polysaccharide monooxygenaseLPMOredox-sensitiveconditionally disordered regionsdisorder predictionMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1632, p 1632 (2021)
institution DOAJ
collection DOAJ
language EN
topic intrinsically disordered regions
lytic polysaccharide monooxygenase
LPMO
redox-sensitive
conditionally disordered regions
disorder prediction
Microbiology
QR1-502
spellingShingle intrinsically disordered regions
lytic polysaccharide monooxygenase
LPMO
redox-sensitive
conditionally disordered regions
disorder prediction
Microbiology
QR1-502
Ketty C. Tamburrini
Nicolas Terrapon
Vincent Lombard
Bastien Bissaro
Sonia Longhi
Jean-Guy Berrin
Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions
description Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes secreted by many organisms and viruses. LPMOs catalyze the oxidative cleavage of different types of polysaccharides and are today divided into eight families (AA9–11, AA13–17) within the Auxiliary Activity enzyme class of the CAZy database. LPMOs minimal architecture encompasses a catalytic domain, to which can be appended a carbohydrate-binding module. Intriguingly, we observed that some LPMO sequences also display a C-terminal extension of varying length not associated with any known function or fold. Here, we analyzed 27,060 sequences from different LPMO families and show that 60% have a C-terminal extension predicted to be intrinsically disordered. Our analysis shows that these disordered C-terminal regions (dCTRs) are widespread in all LPMO families (except AA13) and differ in terms of sequence length and amino-acid composition. Noteworthily, these dCTRs have so far only been observed in LPMOs. LPMO-dCTRs share a common polyampholytic nature and an enrichment in serine and threonine residues, suggesting that they undergo post-translational modifications. Interestingly, dCTRs from AA11 and AA15 are enriched in redox-sensitive, conditionally disordered regions. The widespread occurrence of dCTRs in LPMOs from evolutionarily very divergent organisms, hints at a possible functional role and opens new prospects in the field of LPMOs.
format article
author Ketty C. Tamburrini
Nicolas Terrapon
Vincent Lombard
Bastien Bissaro
Sonia Longhi
Jean-Guy Berrin
author_facet Ketty C. Tamburrini
Nicolas Terrapon
Vincent Lombard
Bastien Bissaro
Sonia Longhi
Jean-Guy Berrin
author_sort Ketty C. Tamburrini
title Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions
title_short Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions
title_full Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions
title_fullStr Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions
title_full_unstemmed Bioinformatic Analysis of Lytic Polysaccharide Monooxygenases Reveals the Pan-Families Occurrence of Intrinsically Disordered C-Terminal Extensions
title_sort bioinformatic analysis of lytic polysaccharide monooxygenases reveals the pan-families occurrence of intrinsically disordered c-terminal extensions
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/0ae01a8af9024c1885fd60382d45c3c6
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