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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    The malfunction of just one type of enzyme out of the thousands of types present in the human body can be fatal. An example of a fatal genetic disease due to enzyme insufficiency is Tay–Sachs disease, in which patients lack the enzyme hexosaminidase. [101] [102] One example of enzyme deficiency is the most common type of phenylketonuria.

  4. Biosynthesis - Wikipedia

    en.wikipedia.org/wiki/Biosynthesis

    Biosynthesis, i.e., chemical synthesis occurring in biological contexts, is a term most often referring to multi-step, enzyme-catalyzed processes where chemical substances absorbed as nutrients (or previously converted through biosynthesis) serve as enzyme substrates, with conversion by the living organism either into simpler or more complex ...

  5. Restriction map - Wikipedia

    en.wikipedia.org/wiki/Restriction_map

    One approach in constructing a restriction map of a DNA molecule is to sequence the whole molecule and to run the sequence through a computer program that will find the recognition sites that are present for every restriction enzyme known. Before sequencing was automated, it would have been prohibitively expensive to sequence an entire DNA ...

  6. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: An enzyme that is produced by animals that forms part of the innate immune system and is abundant in the secretions of saliva, human milk, tears, and mucus. It functions as an antimicrobial agent by splitting the peptidoglycan component of bacterial cell walls, which then leads to cell death.

  7. Nicotinamide adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Nicotinamide_adenine_di...

    Other NAD-dependent enzymes include bacterial DNA ligases, which join two DNA ends by using NAD + as a substrate to donate an adenosine monophosphate (AMP) moiety to the 5' phosphate of one DNA end. This intermediate is then attacked by the 3' hydroxyl group of the other DNA end, forming a new phosphodiester bond . [ 81 ]

  8. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    Bacteria generally have one bi-functional enzyme, but archaea and eukaryotes usually employ two distinct enzymes. [9] Current research indicates that distinct isoforms exist in the cytosol and mitochondria. [9] It seems that FAD is synthesized in both locations and potentially transported where needed. [11]

  9. Glutathione reductase - Wikipedia

    en.wikipedia.org/wiki/Glutathione_reductase

    Glutathione reductase (GR) also known as glutathione-disulfide reductase (GSR) is an enzyme that in humans is encoded by the GSR gene.Glutathione reductase (EC 1.8.1.7) catalyzes the reduction of glutathione disulfide to the sulfhydryl form glutathione (), which is a critical molecule in resisting oxidative stress and maintaining the reducing environment of the cell.