Cofactor engineering, a subset of metabolic engineering, is defined as the manipulation of the use of cofactors in an organism’s metabolic pathways. In...

A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases...

Another computing method, IPRO, successfully engineered the switching of cofactor specificity of Candida boidinii xylose reductase. Iterative Protein Redesign...

carboxylase). An example of an enzyme that contains a cofactor is carbonic anhydrase, which uses a zinc cofactor bound as part of its active site. These tightly...

Nicotinamide cofactor analogues (mNADs), also called nicotinamide coenzyme biomimetics (NCBs), are artificial compounds that mimic the natural nicotinamide...

{\displaystyle F_{x'}} are sometimes called the positive and negative Shannon cofactors, respectively, of F {\displaystyle F} with respect to x {\displaystyle...

congenital cofactor deficiency. A congenital molybdenum cofactor deficiency disease, seen in infants, is an inability to synthesize molybdenum cofactor, the...

switching the iron-protoporphyrin cofactor in thermostable P450 enzyme CYP119A1 with an iridium-methyl-protoporphyrin cofactor (Ir(Me)-PIX), followed by directed...

contains a pigmented prosthetic group (or cofactor). A common example is haemoglobin, which contains a heme cofactor, which is the iron-containing molecule...

(biotin and thiamine) are organosulfur compounds crucial for life. Many cofactors also contain sulfur, including glutathione, and iron–sulfur proteins....

hydroxylase enzymes performing these reactions require vitamin C as a cofactor, a long-term deficiency in this vitamin results in impaired collagen synthesis...

proteins, however, generate and maintain a superoxidized form of the flavin cofactor, the flavin-N(5)-oxide. Flavoproteins were first discovered in 1879 by...

enzymes for which vitamin C is a cofactor, with function potentially compromised in a deficiency state, and any enzyme cofactor or other physiological function...

catabolized and reduced by donating their electrons to other organic molecules (cofactors, coenzymes, etc.). Fermentation is important in several areas of human...

molecule: as an electron transporter, an oxygen carrier, and as an enzyme cofactor, heme binding proteins have consistently attracted the attention of protein...

P450 (P450s or CYPs) are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. However,...

proteins, the formation of nitriles is favored instead. Ascorbate is a known cofactor of myrosinase, serving as a base catalyst in glucosinolate hydrolysis....

bacteria, but the production pathway requires the cofactor NADPH, whereas E. coli makes the cofactor NADH. To circumvent this problem, she evolved the...

avidin can significantly increase the catalytic capacity of Rhodium(I) cofactor in aqueous phosphate buffer. Another pioneering work was conducted by Kaiser...

involved in metabolism. One of eight B vitamins, it serves as a vital cofactor in DNA synthesis and both fatty acid and amino acid metabolism. It plays...

Although this reaction requires nicotinamide adenine dinucleotide (NAD) as a cofactor, the enzymic mechanism regenerates it, resulting in the net use of no NAD...

tons of nicotinamide were sold in 2014. Nicotinamide, as a part of the cofactor nicotinamide adenine dinucleotide (NADH / NAD+) is crucial to life. In...

metabolite. In humans, L-2-hydroxyglutarate dehydrogenase uses FAD as the cofactor, while the E. coli enzyme reduces molecular oxygen. Pre-emption prevents...

Although this reaction requires nicotinamide adenine dinucleotide (NAD) as a cofactor, the enzymic mechanism regenerates it, resulting in the net use of no NAD...

matrix if the bases are orthonormal. Adjugate matrix, the transpose of the cofactor matrix Conjugate transpose Converse relation Moore–Penrose pseudoinverse...

the function of citrulline as part of the nitric oxide cycle. It is a cofactor and acts on glutathione peroxidase. Glutathione is used to produce S-sulfanylglutathione...

motif to construct synthetic systems. The binding of enzymes with their cofactors has been used as a route to produce modified enzymes, electrically contacted...

metabolism. Fritz Lipmann won the Nobel Prize in 1953 for his discovery of the cofactor coenzyme A. Acetyl-CoA is a metabolic intermediate that is involved in...

a heterologous carbon sink in engineered strains. A lot of metabolic engineering work on the MEP pathway has been done in cyanobacteria, photo-autotrophic...

groups (Types I, II, III, IV, and V) based on their composition and enzyme cofactor requirements, the nature of their target sequence, and the position of...