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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

    That is, the chemical catalysis is defined as the reduction of E a ‡ (when the system is already in the ES ‡) relative to E a ‡ in the uncatalyzed reaction in water (without the enzyme). The induced fit only suggests that the barrier is lower in the closed form of the enzyme but does not tell us what the reason for the barrier reduction is.

  5. Lysine 2,3-aminomutase - Wikipedia

    en.wikipedia.org/wiki/Lysine_2,3-aminomutase

    Four key cofactors are required for the reaction catalyzed by the lysine 2,3-aminomutase enzyme. They are: S-Adenosyl methionine (SAM): Helps generate the radical intermediate by borrowing an electron. [5] Pyridoxal phosphate (PLP): Responsible for binding of the amino acid during reaction. The pi-system of this molecule facilitates radical ...

  6. Cofactor (biochemistry) - Wikipedia

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

    Here, cofactors were defined as an additional substance apart from protein and substrate that is required for enzyme activity and a prosthetic group as a substance that undergoes its whole catalytic cycle attached to a single enzyme molecule. However, the author could not arrive at a single all-encompassing definition of a "coenzyme" and ...

  7. 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.

  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. Biocatalysis - Wikipedia

    en.wikipedia.org/wiki/Biocatalysis

    Chemoselectivity: Since the purpose of an enzyme is to act on a single type of functional group, other sensitive functionalities, which would normally react to a certain extent under chemical catalysis, survive. As a result, biocatalytic reactions tend to be "cleaner" and laborious purification of product(s) from impurities emerging through ...