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  2. Lysozyme - Wikipedia

    en.wikipedia.org/wiki/Lysozyme

    Lysozyme (EC 3.2.1.17, muramidase, N-acetylmuramide glycanhydrolase; systematic name peptidoglycan N-acetylmuramoylhydrolase) is an antimicrobial enzyme produced by animals that forms part of the innate immune system. It is a glycoside hydrolase that catalyzes the following process:

  3. Cofactor (biochemistry) - Wikipedia

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

    The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.. 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 the rate of a chemical reaction).

  4. Cofactor engineering - Wikipedia

    en.wikipedia.org/wiki/Cofactor_Engineering

    Cofactors can be both organic and inorganic compounds. Some examples of inorganic cofactors are iron or magnesium, and some examples of organic cofactors include ATP or coenzyme A. Organic cofactors are more specifically known as coenzymes, and many enzymes require the addition of coenzymes to assume normal catalytic function in a metabolic ...

  5. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    If an enzyme needs coenzyme to work itself, it is called an apoenzyme. In fact, it alone cannot catalyze reactions properly. Only when its cofactor comes in and binds to the active site to form holoenzyme does it work properly. One example of the coenzyme is Flavin. It contains a distinct conjugated isoalloxazine ring system.

  6. Glycosyltransferase - Wikipedia

    en.wikipedia.org/wiki/Glycosyltransferase

    Most glycosyltransferase enzymes form one of two folds: GT-A or GT-B. Glycosyltransferases (GTFs, Gtfs) are enzymes that establish natural glycosidic linkages.They catalyze the transfer of saccharide moieties from an activated nucleotide sugar (also known as the "glycosyl donor") to a nucleophilic glycosyl acceptor molecule, the nucleophile of which can be oxygen- carbon-, nitrogen-, or sulfur ...

  7. Lysin - Wikipedia

    en.wikipedia.org/wiki/Lysin

    Double-stranded DNA phage lysins tend to lie within the 25 to 40 kDa range in terms of size. A notable exception is the streptococcal PlyC endolysin, which is 114 kDa. PlyC is not only the biggest and most potent lysin, but also structurally unique since it is composed of two different gene products, PlyCA and PlyCB, with a ratio of eight PlyCB subunits for each PlyCA in its active conformation.

  8. Lysosome - Wikipedia

    en.wikipedia.org/wiki/Lysosome

    The word lysosome (/ ˈ l aɪ s oʊ s oʊ m /, / ˈ l aɪ z ə z oʊ m /) is Neo-Latin that uses the combining forms lyso-(referring to lysis and derived from the Latin lysis, meaning "to loosen", via Ancient Greek λύσις [lúsis]), and -some, from soma, "body", yielding "body that lyses" or "lytic body".

  9. α-Amylase - Wikipedia

    en.wikipedia.org/wiki/Α-Amylase

    α-Amylase is an enzyme (EC 3.2.1.1; systematic name 4-α-D-glucan glucanohydrolase) that hydrolyses α bonds of large, α-linked polysaccharides, such as starch and glycogen, yielding shorter chains thereof, dextrins, and maltose, through the following biochemical process: [2]

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