Search results
Results from the WOW.Com Content Network
Lignin is found to be degraded by enzyme lignin peroxidases produced by some fungi like Phanerochaete chrysosporium. The mechanism by which lignin peroxidase (LiP) interacts with the lignin polymer involves veratrole alcohol , which is a secondary metabolite of white rot fungi that acts as a cofactor for the enzyme.
Lignin-modifying enzymes benefit industry as they can break down lignin; a common waste product of the paper and pulp industry. These enzymes have been used in the refinement of poplar as lignin inhibits the enzymatic hydrolysis of treated poplar and Lignin-modifying enzymes can efficiently degrade the lignin thus fixing this problem. [4]
In biochemistry, a zymogen (/ ˈ z aɪ m ə dʒ ən,-m oʊ-/ [1] [2]), also called a proenzyme (/ ˌ p r oʊ ˈ ɛ n z aɪ m / [3] [4]), is an inactive precursor of an enzyme.A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme.
This was a result of the gas (carbon dioxide) becoming trapped within the crust so it could not diffuse out (like it would have normally) and causing abnormal pore size. [12] Resistance and extensibility was a function of dosage, but at very high dosage the dough showed contradictory results: maximum resistance was reduced drastically.
Lignin is a class of complex organic polymers that form key structural materials in the support tissues of most plants. [1] Lignins are particularly important in the formation of cell walls, especially in wood and bark, because they lend rigidity and do not rot easily. Chemically, lignins are polymers made by cross-linking phenolic precursors. [2]
Cinnamoyl-CoA reductase (EC 1.2.1.44), systematically named cinnamaldehyde:NADP+ oxidoreductase (CoA-cinnamoylating) but commonly referred to by the acronym CCR, is an enzyme that catalyzes the reduction of a substituted cinnamoyl-CoA to its corresponding cinnamaldehyde, utilizing NADPH and H + and releasing free CoA and NADP + in the process. [1]
A preproenzyme is an enzyme with two additional characteristics: "pre" refers to a signal sequence (signal peptide) which directs the enzyme to a specific organelle or subcellular localization; "pro" indicates that the enzyme is present in an inactive form and requires modification (e.g. cleavage) for activation.
The two enzymes were renamed COX-1, referring to the original enzyme and COX-2. [5] Building on those results, scientists started focusing on selective COX-2 inhibitors . Enormous effort was spent on the development of NSAIDs between the 1960s and 1980 so there were numerous pharmacophores to test when COX-2 was discovered.