#LPMOs
After analyzing 72 structures of NcAA9D, it was found that X-rays progressively reduce the active-site copper from Cu(II) to Cu(I), forming an electron-density feature that is easy to misinterpret #RadiationDamage #LPMOs #DioxygenBinding doi.org/10.1107/S205...
September 28, 2026 at 3:24 PM
Conserved copper(I)-binding auxiliary domains link virulence-associated LPMOs to copper homeostasis in the intestinal environment https://www.biorxiv.org/content/10.64898/2026.08.05.742968v1
August 6, 2026 at 1:47 PM
Conserved copper(I)-binding auxiliary domains link virulence-associated LPMOs to copper homeostasis in the intestinal environment https://www.biorxiv.org/content/10.64898/2026.08.05.742968v1
August 6, 2026 at 1:47 PM
Some papers highlighted in this collection:

"Selective oxidation of active site aromatic residues in engineered Cu proteins" doi.org/10.1039/D4SC...

"Nickel model complexes to mimic carbon monoxide dehydrogenase reactions" doi.org/10.1039/D4SC...
Selective oxidation of active site aromatic residues in engineered Cu proteins
Recent studies have revealed critical roles for the local environments surrounding metallocofactors, such as the newly identified CuD site in particulate methane monooxygenases (pMMOs) and the second sphere aromatic residues in lytic polysaccharide monooxygenases (LPMOs), implicated in the protection against
doi.org
May 26, 2025 at 9:00 AM
Light-ning Talks #LorneProteins2025 Kelsi Hall on lytic polysaccharides monoogygenases. LPMOs cleave polysaccharides using hydrogen peroxide. Flat binding surface. Monocopper active site. Primed by a reductant like ascorbic acid. Can make their own peroxide! 2nd sphere functional variation.
February 11, 2025 at 1:58 AM
“อ่านนิยายเสวของคุณชิรณะแล้วไม่เคยผิดหวังเลย แซ่บกีลุก🔥”

“ภาษาสวยมาก NCก็เซ็กซี่มาก เสียวมาก กรีดร้องงง“

“ภาษาสวย เห็นภาพชัด แต่ไม่หยาบคาย อ่านได้แบบสบายใจ เพราะไม่มีการบีบบังคับหรือฝืนใจเลย”

รีวิวเริดขนาดนี้ ชิมเล้ย 🤤

#อนุยวนเย้า
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October 23, 2024 at 6:59 AM
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เล่ม 2 : shorturl.at/zFQ36
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October 20, 2024 at 7:07 AM
Structural & electronic modulations of copper enzyme lytic polysaccharide monooxygenase upon chitin binding (via @chemicalscience.rsc.org)
doi.org/10.1039/D5SC...
Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy
Lytic polysaccharide monooxygenases (LPMOs) play a critical role in the depolymerization of recalcitrant polysaccharides, such as chitin, making them of interest in biotechnological applications. Thes...
doi.org
December 30, 2025 at 8:58 AM
Really happy to share our recent publication on LPMO metalloenzymes, with new mechanistic insights into these fascinating copper enzymes. And the paper was selected for the back cover.
@chemicalscience.rsc.org
Grateful for the collaboration and excited for what’s next!
pubs.rsc.org/en/content/a...
Structural and electronic modulations of lytic polysaccharide monooxygenase (LPMO) upon chitin binding: insights from X-ray spectroscopy
Lytic polysaccharide monooxygenases (LPMOs) play a critical role in the depolymerization of recalcitrant polysaccharides, such as chitin, making them of interest in biotechnological applications. Thes...
pubs.rsc.org
December 23, 2025 at 1:42 PM
📢Check out the ICF_research by Erik D. Hedegård et al. from the University of Southern Denmark
👉The mechanism behind the oxidase activity of cellulose-active AA10 lytic polysaccharide monooxygenases
#bioinorganic
doi.org/10.1039/D5QI...
The mechanism behind the oxidase activity of cellulose-active AA10 lytic polysaccharide monooxygenases
Lytic polysaccharide monooxygenases (LPMOs) are copper enzymes that boost the degradation of different polysaccharides and play important roles in the sustainable production of biofuels, in human and ...
doi.org
June 13, 2025 at 9:05 AM
Curious about how #Biotechnology can help modern society transition into a #Sustainable future? Follow our project twitter: https://x.com/HOPE59966358 and discover our ongoing #research in #LPMOs and how these amazing #enzymes can help us produce sustainable chemicals #dkgreen
April 14, 2025 at 11:53 AM
Thanks to everyone attending the @LPMOsympos2018 for being so welcoming to newcomers to the field! @rennig_m, @HdezRollan, and I were pleasantly surprised that you found or work interesting, despite it not being directly connected to #LPMOs.
April 14, 2025 at 11:48 AM
Wrapping your head around #LPMOs can be a bit overwhelming. For me the review "Oxygen Activation by Cu LPMOs in Recalcitrant Carbohydrate Polysaccharide Conversion to Monomer Sugars" from @ACSChemRev was especially helpful. Long but thorough!
April 14, 2025 at 11:48 AM
April 14, 2025 at 11:30 AM
LPMOs in the making for @HOPE59966358
April 14, 2025 at 10:45 AM
What does this mean for biologists?
— You can functionally annotate LPMOs even with novel or borderline sequences
— You can use structure to discover or repurpose enzymes
— You get a clearer idea of why an LPMO behaves the way it does 8/10
July 5, 2025 at 1:35 AM
With these features, we trained several ML models.
🥇 Best performer? SVM with an RBF kernel — 98% accuracy
🥈 MLP (tanh + adam) also did well — 97% accuracy
These models can classify LPMOs just from structural fingerprints! 7/10
July 5, 2025 at 1:35 AM
LPMOs (Lytic Polysaccharide Monooxygenases) are copper enzymes that cleave cellulose and chitin.
They’re central to biofuels and industrial enzyme applications.
CAZy groups them into 8 families: AA9 to AA17. 2/10
July 5, 2025 at 1:35 AM
🚨🚨🚨Preprint Time!!!
Excited to share our latest work on LPMOs—enzymes that break down biomass 🪵
We built a structure-based ML tool that can classify all 8 LPMO families using features extracted from 3D structures—including AlphaFold models.
It works surprisingly well. 🧵👇
Machine learning-based structural classification of lytic polysaccharide monooxygenases https://www.biorxiv.org/content/10.1101/2025.07.02.662747v1
July 5, 2025 at 1:35 AM
📢 Please share if you believe science should stay open, collaborative, and hopeful.
📖 Read the preprint: www.biorxiv.org/content/10.1...
👨‍🔬 Team: Kavin, Priyadharshini, Vaishnavi & Ragothaman Yennamalli

Even in dark times, we keep building. 🔬✨

#ScienceTwitter #MLforBiology #Bioenergy #OpenScience
PreDSLpmo V2.0: A deep learning-based prediction tool for functional annotation of lytic polysaccharide monooxygenases
Lytic polysaccharide monooxygenases (LPMOs) are redox enzymes in the oxidative cleavage of recalcitrant polysaccharides, facilitating efficient biomass deconstruction for biofuel production. While com...
www.biorxiv.org
June 13, 2025 at 3:04 AM
🌱 Why it matters:
LPMOs are at the frontier of bioenergy. Identifying new ones helps unlock better biocatalysts.
With PreDSLpmo v2.0, we make high-throughput, sequence-based annotation possible.

Let’s decode enzymes to power a greener future.
6/8
June 13, 2025 at 3:04 AM
🧪 What’s the challenge?
Lytic polysaccharide monooxygenases (LPMOs) break down tough plant material—vital for sustainable biofuels and green chemistry.

But most tools only classify a few families. Many LPMO sequences remain unannotated.
2/8
June 13, 2025 at 3:04 AM
The world feels heavy these days. But here’s something small and hopeful from our corner of science.

We just posted our preprint on a deep learning tool for enzyme annotation:
🔗 www.biorxiv.org/content/10.1...

#Bioinformatics #DeepLearning
1/8
June 13, 2025 at 3:04 AM
Functional characterization of multi-domain LPMOs from marine Vibrio species reveals modulation of enzyme activity by domain-domain interactions https://www.biorxiv.org/content/10.1101/2025.07.04.663128v1
July 6, 2025 at 5:46 AM
Tangled up in fibers: How a lytic polysaccharide monooxygenase binds its chitin substrate https://www.biorxiv.org/content/10.1101/2023.09.21.558757v1
Tangled up in fibers: How a lytic polysaccharide monooxygenase binds its chitin substrate https://www.biorxiv.org/content/10.1101/2023.09.21.558757v1
Lytic polysaccharide monooxygenases (LPMOs) are redox-enzymes that bind to and oxidize insoluble car
www.biorxiv.org
September 22, 2023 at 5:46 AM