A halophile is an extremophile that thrives in high salt concentrations. In chemical terms, halophile refers to a Lewis acidic species that has some ability to extract halides from other chemical species.
Lignin is a class of complex organic polymers that form key structural materials in the support tissues of most plants. 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.
Pyrroloquinoline quinone (PQQ), also called methoxatin, is a redox cofactor and antioxidant. Produced by bacteria, it is found in soil and foods such as kiwifruit, as well as human breast milk. Enzymes using PQQ as a redox cofactor are called quinoproteins and play a variety of redox roles. Quinoprotein glucose dehydrogenase is used as a glucose sensor in bacteria. PQQ stimulates growth in bacteria. Eukaryote targets, including mammalian lactate dehydrogenase, are of more interest to health. It is suggested that PQQ taken as a dietary supplement could promote mitochondrial biogenesis via this pathway as well as PGC-1α.
Endo-1,4-β-xylanase is any of a class of enzymes that degrade the linear polysaccharide xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls:
Cyanophycin, also known as CGP or multi-L-arginyl-poly, is a non-protein, non-ribosomally produced amino acid polymer composed of an aspartic acid backbone and arginine side groups.
Ferroplasma is a genus of Archaea that belong to the family Ferroplasmaceae. Members of the Ferroplasma are typically acidophillic, pleomorphic, irregularly shaped cocci.
Laccases are multicopper oxidases found in plants, fungi, and bacteria. Laccases oxidize a variety of phenolic substrates, performing one-electron oxidations, leading to crosslinking. For example, laccases play a role in the formation of lignin by promoting the oxidative coupling of monolignols, a family of naturally occurring phenols. 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. Other laccases produced by fungi can facilitate the biosynthesis of melanin pigments. Laccases catalyze ring cleavage of aromatic compounds.
Lignin-modifying enzymes (LMEs) are various types of enzymes produced by fungi and bacteria that catalyze the breakdown of lignin, a biopolymer commonly found in the cell walls of plants. The terms ligninases and lignases are older names for the same class, but the name "lignin-modifying enzymes" is now preferred, given that these enzymes are not hydrolytic but rather oxidative by their enzymatic mechanisms. LMEs include peroxidases, such as lignin peroxidase, manganese peroxidase, versatile peroxidase, and many phenoloxidases of the laccase type.
D-amino-acid dehydrogenase is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids.
Chloride peroxidase (EC 1.11.1.10) is a family of enzymes that catalyzes the chlorination of organic compounds. This enzyme combines the inorganic substrates chloride and hydrogen peroxide to produce the equivalent of Cl+, which replaces a proton in hydrocarbon substrate:
Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to catalyse a number of oxidative reactions. Most haem peroxidases follow the reaction scheme:
Cunninghamella elegans is a species of fungus in the genus Cunninghamella found in soil.
In molecular biology, the DyP-type peroxidase family is a family of haem peroxidase enzymes. Haem peroxidases were originally divided into two superfamilies, namely, the animal peroxidases and the plant peroxidases, which include fungal and bacterial peroxidases. The DyP family constitutes a novel class of haem peroxidase. Because these enzymes were derived from fungal sources, the DyP family was thought to be structurally related to the class II secretory fungal peroxidases. However, the DyP family exhibits only low sequence similarity to classical fungal peroxidases, such as LiP and MnP, and does not contain the conserved proximal and distal histidines and an essential arginine found in other plant peroxidase superfamily members.
Thermococcus kodakarensis is a species of thermophilic archaea. The type strain T. kodakarensis KOD1 is one of the best-studied members of the genus.
Unspecific peroxygenase (EC 1.11.2.1, aromatic peroxygenase, mushroom peroxygenase, haloperoxidase-peroxygenase, Agrocybe aegerita peroxidase) is an enzyme with systematic name substrate:hydrogen peroxide oxidoreductase (RH-hydroxylating or -epoxidising). This enzyme catalyses the following chemical reaction
Desulfitobacterium hafniense is a species of gram positive bacteria, its type strain is DCB-2T..
Clostridium cellulovorans is an anaerobic, mesophilic, spore-forming cellulolytic bacterium. Its cells are gram-positive and are non-motile rods which form oblong spores. The type strain is 743B. Its role as an object of study is based on the latter notion.
Shewanella decolorationis is a gram-negative, dye-decolorizing bacterium first isolated from activated sludge of a waste-water treatment plant. It is motile by means of a single polar flagellum. The type strain is S12T. Its genome has been sequenced.
Streptomyces graminearus is a bacterium species from the genus of Streptomyces. Streptomyces graminearus produces the antibiotic gougerotin.
Streptomyces thermoviolaceus is a thermophilic bacterium species from the genus of Streptomyces which has been isolated from composts. Streptomyces thermoviolaceus produces chitinase and peroxidase.
