Recent insights into lytic polysaccharide monooxygenases (LPMOs)
| Autor: | Jean-Guy Berrin, Leila Lo Leggio, Katja Salomon Johansen, Kristian E. H. Frandsen, Tobias Tandrup |
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| Přispěvatelé: | Department of Chemistry, Sookmyung Women's University , Seoul 04310, Korea., Biodiversité et Biotechnologie Fongiques (BBF), École Centrale de Marseille (ECM)-Aix Marseille Université (AMU)-Institut National de la Recherche Agronomique (INRA), Department of Geosciences and Natural Resource Management [Copenhagen] (IGN), Faculty of Science [Copenhagen], University of Copenhagen = Københavns Universitet (KU)-University of Copenhagen = Københavns Universitet (KU), Institut National de la Recherche Agronomique (INRA)-Aix Marseille Université (AMU)-École Centrale de Marseille (ECM), University of Copenhagen = Københavns Universitet (UCPH)-University of Copenhagen = Københavns Universitet (UCPH), Novo Nordisk Foundation HOPE project NNF17SA0027704, Carlsberg FoundationCF16-0673,CF17-0533, European Project: 609398,EC:FP7:PEOPLE,FP7-PEOPLE-2013-COFUND,AGREENSKILLSPLUS(2014) |
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
metalloenzyme Context (language use) Crystallography X-Ray Polysaccharide Biochemistry xylan xylane Mixed Function Oxygenases Substrate Specificity 03 medical and health sciences Cell Wall Polysaccharides Animals teneur en cuivre chemistry.chemical_classification biology peroxyde d'hydrogène Active site monooxygénase oxygène moléculaire Plants Monooxygenase x ray crystallography 030104 developmental biology chemistry Lytic cycle plant cell wall degradation cristallographie rayon x biology.protein lytic polysaccharide monooxygenase structure biochimique Molecular oxygen substrat [CHIM.OTHE]Chemical Sciences/Other Oxidation-Reduction |
| Zdroj: | Biochemical Society transactions Biochemical Society transactions, 2018, 46 (6), pp.1431-1447. ⟨10.1042/BST20170549⟩ Biochemical Society Transactions Biochemical Society Transactions, 2018, 46 (6), pp.1431-1447. ⟨10.1042/BST20170549⟩ Biochemical Society Transactions, Portland Press, 2018, 46 (6), pp.1431-1447. ⟨10.1042/BST20170549⟩ |
| ISSN: | 1470-8752 0300-5127 |
| DOI: | 10.1042/BST20170549⟩ |
| Popis: | Lytic polysaccharide monooxygenases (LPMOs) are copper enzymes discovered within the last 10 years. By degrading recalcitrant substrates oxidatively, these enzymes are major contributors to the recycling of carbon in nature and are being used in the biorefinery industry. Recently, two new families of LPMOs have been defined and structurally characterized, AA14 and AA15, sharing many of previously found structural features. However, unlike most LPMOs to date, AA14 degrades xylan in the context of complex substrates, while AA15 is particularly interesting because they expand the presence of LPMOs from the predominantly microbial to the animal kingdom. The first two neutron crystallography structures have been determined, which, together with high-resolution room temperature X-ray structures, have putatively identified oxygen species at or near the active site of LPMOs. Many recent computational and experimental studies have also investigated the mechanism of action and substrate-binding mode of LPMOs. Perhaps, the most significant recent advance is the increasing structural and biochemical evidence, suggesting that LPMOs follow different mechanistic pathways with different substrates, co-substrates and reductants, by behaving as monooxygenases or peroxygenases with molecular oxygen or hydrogen peroxide as a co-substrate, respectively. |
| Databáze: | OpenAIRE |
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