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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.
For example, laccases play a role in the formation of lignin by promoting the oxidative coupling of monolignols, a family of naturally occurring phenols. [ 1 ] [ 2 ] Other laccases, such as those produced by the fungus Pleurotus ostreatus , play a role in the degradation of lignin, and can therefore be classed as lignin-modifying enzymes . [ 3 ]
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]
The enzyme is notable for its promiscuity, affecting the O-demethylation of a range of substrates, including lignin. It is a heterodimeric protein derived from the products of two genes. The component proteins are a cytochrome P450 enzyme (encoded by the gcoA gene from the family CYP255A) and a three-domain reductase (encoded by the gcoB gene ...
The Network of Cancer Genes (NCG) is a freely accessible web resource of genes that, when altered in their sequence, drive clonal expansion of normal tissues (healthy drivers) or cancer (cancer drivers). The project was launched in 2010 and has reached its 7th release in 2022.
The enzyme phenylalanine ammonia lyase (EC 4.3.1.24) catalyzes the conversion of L-phenylalanine to ammonia and trans-cinnamic acid.: [1] L -phenylalanine = trans -cinnamate + NH 3 Phenylalanine ammonia lyase (PAL) is the first and committed step in the phenyl propanoid pathway and is therefore involved in the biosynthesis of the polyphenol ...
The systematic name of this enzyme class is Mn(II):hydrogen-peroxide oxidoreductase. Other names in common use include peroxidase-M2, and Mn-dependent (NADH-oxidizing) peroxidase. It employs one cofactor, heme. This enzyme needs Ca 2+ for activity. White rot fungi secrete this enzyme to aid lignin degradation.
In humans, 5ALA is a precursor to heme. [3] Biosynthesized, 5ALA goes through a series of transformations in the cytosol and finally gets converted to Protoporphyrin IX inside the mitochondria. [25] [26] This protoporphyrin molecule chelates with iron in presence of enzyme ferrochelatase to produce Heme. [25] [26]