On the functional characterization of lytic polysaccharide monooxygenases (LPMOs) [PDF]
Lytic polysaccharide monooxygenases (LPMOs) are abundant in nature and best known for their role in the enzymatic conversion of recalcitrant polysaccharides such as chitin and cellulose. LPMO activity requires an oxygen co-substrate, which was originally thought to be O2, but which may also be H2O2.
Vincent G. H. Eijsink +7 more
openaire +4 more sources
1H, 13C, 15N resonance assignment of the apo form of the small, chitin-active lytic polysaccharide monooxygenase JdLPMO10A from Jonesia denitrificans [PDF]
The lytic polysaccharide monooxygenase JdLPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated JdLPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to date with a size of only 15.5 ...
Aachmann, Finn Lillelund +7 more
core +1 more source
Classification of fungal and bacterial lytic polysaccharide monooxygenases [PDF]
Lytic polysaccharide monooxygenases are important enzymes for the decomposition of recalcitrant biological macromolecules such as plant cell wall and chitin polymers. These enzymes were originally designated glycoside hydrolase family 61 and carbohydrate-binding module family 33 but are now classified as auxiliary activities 9, 10 and 11 in the CAZy ...
Busk, Peter K., Lange, Lene
openaire +3 more sources
Is density functional theory accurate for lytic polysaccharide monooxygenase enzymes [PDF]
The lytic polysaccharide monooxygenase (LPMO) enzymes boost polysaccharide depolymerization through oxidative chemistry, which has fueled the hope for more energy-efficient production of biofuel. We have recently proposed a mechanism for the oxidation of
Hedegård, Erik D. +10 more
core +2 more sources
Resonance assignments for the apo-form of the cellulose-active lytic polysaccharide monooxygenase TaLPMO9A [PDF]
The apo-form of the 24.4 kDa AA9 family lytic polysaccharide monooxygenase TaLPMO9A from Thermoascus aurantiacus has been isotopically labeled and recombinantly expressed in Pichia pastoris.
Fukamizo, Tamo +5 more
core +1 more source
Heterologous expression of lytic polysaccharide monooxygenases (LPMOs)
Lytic polysaccharide monooxygenases (LPMOs) are relatively new enzymes that have been discovered 10 years ago. LPMOs comprise a diverse group of enzymes which play a pivotal role in the depolymerization of sugar-based biopolymers including cellulose, hemicellulose, chitin, and starch.
Gaber, Yasser +6 more
openaire +4 more sources
A novel expression system for lytic polysaccharide monooxygenases [PDF]
Lytic polysaccharide monooxygenases (LPMOs) are key enzymatic players of lignocellulosic biomass degradation processes. As such, they have been introduced in cellulolytic cocktails for more efficient and less expensive lignocellulose saccharification. The recombinant production of LPMOs in bacteria for scientific investigations using vectors typically ...
Gaston Courtade +4 more
openaire +4 more sources
Understanding the initial events of the oxidative damage and protection mechanisms of the AA9 lytic polysaccharide monooxygenase family. [PDF]
Lytic polysaccharide monooxygenase (LPMO) is a new class of oxidoreductases that boosts polysaccharide degradation employing a copper active site.
Hagemann MM, Wieduwilt EK, Hedegård ED.
europepmc +2 more sources
Capture of activated dioxygen intermediates at the copper-active site of a lytic polysaccharide monooxygenase [PDF]
Metalloproteins perform a diverse array of redox-related reactions facilitated by the increased chemical functionality afforded by their metallocofactors.
Pratul K., Agarwal +4 more
core +2 more sources
Every year, seafood waste produced globally contains about 10 million tons of wasted crab, shrimp and lobster shells, which are rich in chitin resources.
Delong Pan +5 more
doaj +1 more source

