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  2. Lysozyme - Wikipedia

    en.wikipedia.org/wiki/Lysozyme

    Lysozyme is part of the innate immune system. Reduced lysozyme levels have been associated with bronchopulmonary dysplasia in newborns. [35] Piglets fed with human lysozyme milk can recover from diarrheal disease caused by E. coli faster. The concentration of lysozyme in human milk is 1,600 to 3,000 times greater than the concentration in ...

  3. Lysin - Wikipedia

    en.wikipedia.org/wiki/Lysin

    The prototypical holin is the lambda phage S protein, which assists the lambda phage R protein (lysin). All holins embed themselves in the cell membrane and contain at least two transmembrane helical domains. The hole making process is thought to be achieved by holin oligomerization at a specific moment when progeny virions are set to be released.

  4. 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).

  5. Lysyl hydroxylase - Wikipedia

    en.wikipedia.org/wiki/Lysyl_hydroxylase

    Lysyl hydroxylases (or procollagen-lysine 5-dioxygenases) are alpha-ketoglutarate-dependent hydroxylases enzymes that catalyze the hydroxylation of lysine to hydroxylysine. [1] [2] Lysyl hydroxylases require iron and vitamin C as cofactors for their oxidation activity.

  6. Intracellular transport - Wikipedia

    en.wikipedia.org/wiki/Intracellular_transport

    Prokaryotes are able to subsist by allowing materials to enter the cell via simple diffusion. Intracellular transport is more specialized than diffusion; it is a multifaceted process which utilizes transport vesicles. Transport vesicles are small structures within the cell consisting of a fluid enclosed by a lipid bilayer that hold cargo. These ...

  7. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Many cofactors are vitamins, and their role as vitamins is directly linked to their use in the catalysis of biological process within metabolism. Catalysis of biochemical reactions in the cell is vital since many but not all metabolically essential reactions have very low rates when uncatalysed. One driver of protein evolution is the ...

  8. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Organisation of enzyme structure and lysozyme example. Binding sites in blue, catalytic site in red and peptidoglycan substrate in black. (In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.

  9. Glycoside hydrolase - Wikipedia

    en.wikipedia.org/wiki/Glycoside_hydrolase

    In the gut they are found as glycosylphosphatidyl anchored enzymes on endothelial cells. The enzyme lactase is required for degradation of the milk sugar lactose and is present at high levels in infants, but in most populations will decrease after weaning or during infancy, potentially leading to lactose intolerance in adulthood.