Lytic Polysaccharide Monooxygenase
Lytic Polysaccharide Monooxygenase - Related Videos
01:30
Lytic Cycle of Bacteriophages
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2019
Bacteriophages, also known as phages, are specialized viruses that infect bacteria. A key characteristic of phages is their distinctive “head-tail” morphology. A phage begins the infection process (i.e., lytic cycle) by attaching to the outside of a bacterial cell. Attachment is accomplished via proteins in the phage tail that bind to specific receptor proteins on the outer surface of the bacterium. The tail injects the phage’s DNA genome into the bacterial cytoplasm. In the lytic replication...
01:26
Biosynthesis of Polysaccharides
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2025
Polysaccharides such as glycogen and starch are synthesized from nucleoside diphosphate sugars, primarily uridine diphosphate glucose (UDPG) and adenosine diphosphate glucose (ADPG). These activated glucose donors act as key intermediates in carbohydrate metabolism and biosynthesis. UDPG primarily involves glycogen synthesis in animals and many bacteria, while ADPG plays a fundamental role in starch synthesis in plants and certain bacteria.UDPG is formed when glucose-1-phosphate reacts with...
02:52
Inducing the Prophage Lytic Replication for Transcriptomic Analysis
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2026
Source: Krishnamurthi, R., et al. Understanding the Impact of Temperate Bacteriophages on Their Lysogens Through Transcriptomics. J. Vis. Exp. (2024)This video demonstrates the induction of lytic replication in a prophage integrated into the bacterial genome and the capture of gene expression changes through timed sampling for transcriptomic analysis.
07:10
Establishment and Quantification of De Novo Lytic Infection by Cell-free Kaposi's Sarcoma-Associated Herpesvirus
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2025
This protocol describes an in vitro system to model de novo lytic infection of Kaposi's sarcoma-associated herpesvirus using BAC16-derived virions. The method enables investigation of early viral replication and dissemination. Infectious virus production is quantified by GFP-based infectious units assays and real-time PCR of encapsidated viral genomes.
11:28
Dissecting Host-virus Interaction in Lytic Replication of a Model Herpesvirus
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Cited by 2 •
2011
We describe a protocol to identify key roles of host signaling molecules in lytic replication of a model herpesvirus, gamma herpesvirus 68 (γHV68). Utilizing genetically modified mouse strains and embryonic fibroblasts for γHV68 lytic replication, the protocol permits both phenotypic characterization and molecular interrogation of virus-host interactions in viral lytic replication.
FAQs
The copper center is held in place by conserved residues, creating the reactive site that governs oxidation. Reducing agents supply the activation needed before the enzyme can use molecular oxygen or hydrogen peroxide. This coordination and activation sequence is central to LPMO catalysis because it links the enzyme’s protein structure to its ability to attack otherwise resistant carbohydrate material.
LPMOs can use either molecular oxygen or hydrogen peroxide as the oxidizing input for carbohydrate modification. In both cases, the copper site must be activated by reducing agents. This chemistry allows the enzyme to introduce oxidative changes at selected positions in a polysaccharide, rather than relying only on the hydrolytic cleavage mechanisms used by conventional carbohydrate-active enzymes.
Their crystalline structure makes these polysaccharides resistant to straightforward enzymatic breakdown. LPMOs address this barrier by oxidizing specific carbon positions within the polymer, disrupting its structure and making previously inaccessible regions more vulnerable. The resulting changes do not simply release sugars directly; they improve access for hydrolytic enzymes that complete the conversion into soluble products.
LPMOs and hydrolytic enzymes contribute different functions. Oxidative activity first disrupts the structure of resistant cellulose or chitin, while hydrolytic enzymes act more effectively on the modified material and release soluble sugars. This complementarity explains why adding LPMO activity can improve overall polysaccharide conversion compared with relying on hydrolytic enzymes alone.
A basic experimental system requires the enzyme, a resistant polysaccharide such as crystalline cellulose or chitin, a reducing agent, and an oxidizing source consisting of molecular oxygen or hydrogen peroxide. After oxidative treatment, hydrolytic enzymes can be included to assess whether the substrate has become more accessible and whether soluble sugar release increases.
Successful activity is reflected in disruption of the polymer structure and improved accessibility to hydrolytic enzymes. A practical outcome is enhanced release of soluble sugars when the oxidatively modified material undergoes hydrolytic treatment. These observations connect the chemical event at selected carbon positions with a measurable improvement in downstream polysaccharide conversion.
The chemistry supports biomass conversion strategies aimed at making renewable carbohydrate resources easier to process. Research applications include biofuel production, food and feed processing, and studies of enzyme catalysis. In each setting, the relevant benefit is the same: oxidative modification can help overcome substrate resistance and improve the efficiency of subsequent carbohydrate breakdown.