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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. 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.

  4. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    Most enzymes are made predominantly of proteins, either a single protein chain or many such chains in a multi-subunit complex. Enzymes often also incorporate non-protein components, such as metal ions or specialized organic molecules known as cofactor (e.g. adenosine triphosphate). Many cofactors are vitamins, and their role as vitamins is ...

  5. Cofactor engineering - Wikipedia

    en.wikipedia.org/wiki/Cofactor_Engineering

    Cofactors are required by many important metabolic pathways, and it is possible for the concentrations of a single type of cofactor to affect the fluxes of many different pathways . Minerals and metallic ions that organisms uptake through their diet provide prime examples of inorganic cofactors.

  6. Cyclic enzyme system - Wikipedia

    en.wikipedia.org/wiki/Cyclic_enzyme_system

    A cyclic enzyme system is a theoretical system of two enzymes sharing a single substrate or cofactor, also referred to as a biochemical switching device. [1] It has been used as a biochemical implementation of a simple computational device , acting as a chemical diode .

  7. 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).

  8. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzymes that require a cofactor but do not have one bound are called apoenzymes or apoproteins. An enzyme together with the cofactor(s) required for activity is called a holoenzyme (or haloenzyme). The term holoenzyme can also be applied to enzymes that contain multiple protein subunits, such as the DNA polymerases ; here the holoenzyme is the ...

  9. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    A catalytic triad charge-relay system as commonly found in proteases. The acid residue (commonly glutamate or aspartate) aligns and polarises the base (usually histidine) which activates the nucleophile (often serine or cysteine, occasionally threonine). The triad reduces the pK a of the nucleophilic residue which then attacks the substrate.