anaerobic

Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair. NrdD Protein, E. coli, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 84.0 kDa and the accession number is P28903.

A structural component of the cornified envelope of the stratum corneum involved in innate cutaneous host defense (Probable). Possesses defensin-like antimicrobial activity against a broad spectrum of Gram-positive and Gram-negative bacteria, both aerobic and anaerobic species. Upon inflammation, may regulate skin barrier repair by shaping cutaneous microbiota composition and immune response to bacterial antigens. LCE3A Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 14.6 kDa and the accession number is Q5TA76.

The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction.

Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions.

Clostridium perfringens / C. perfringens (formerly known as C. welchii) is a Gram-positive, rod-shaped, anaerobic, spore-forming bacterium of the genus Clostridium. C. perfringens is ubiquitous in nature and can be found as a normal component of decaying vegetation, marine sediment, the intestinal tract of humans and other vertebrates, insects, and soil. C. perfringens is commonly encountered in infections as a benign component of the normal flora. In this case, its role in disease is minor. Infections due to C. perfringens show evidence of tissue necrosis, bacteremia, emphysematous cholecystitis, and gas gangrene, which is also known as clostridial myonecrosis. NA, also called sialidases, specifically catalyze the hydrolysis removal of terminal sialic acid residues from viral and cellular glycoconjugates. C. Perfringens neuraminidase catalyzes the hydrolysis of alpha-(2->3)-, alpha-(2->6)-, glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates, but has little activity against the α2-8 glycosidic linkages. The function of the neuraminidase is to release sialic acids for use as carbon and energy sources for the non-pathogenic bacterium, while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors

L-Lactate Dehydrogenase A Chain (LDHA) is an enzyme that catalyzes the conversion of L-lactate and NAD+ to pyruvate and NADH in the final step of anaerobic glycolysis. LDHA contains an N-terminal coenzyme binding region, a central catalytic site, and at least nine utilized Lys acetylation and two Tyr phosphorylation sites. LDHA belongs to the lactate dehydrogenase family, expressed predominantly in muscle tissue. LDHA mutations have been linked to exertional myoglobinuria.

Chlorite dismutase (Cld) found in prokaryotic organisms, also known as Chlorite O2-lyase, is a b-type heme containing enzyme that catalyzes the reduction of chlorite into chloride plus dioxygen. The subunit of chlorite dismutase consists of a heme free N-terminal and a heme b containing C-terminal ferredoxin-like fold with high structural homology to the dye-decolorizing peroxidases (DyPs). The physiological role of Cld in prokaryote has been shown that some microorganisms can use perchlorate or chlorate as terminal electron acceptors for anaerobic respiration thereby producing chlorite that must be detoxified. This enzyme has gained attention because it can be used in the development of bioremediation processes, biosensors, and controlled dioxygen production.