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  2. Ubiquitin-conjugating enzyme - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin-conjugating_enzyme

    A ubiquitin-activating enzyme, or E1, first activates the ubiquitin by covalently attaching the molecule to its active site cysteine residue. The activated ubiquitin is then transferred to an E2 cysteine. Once conjugated to ubiquitin, the E2 molecule binds one of several ubiquitin ligases or E3s via a structurally conserved binding region.

  3. Holoprotein - Wikipedia

    en.wikipedia.org/wiki/Holoprotein

    A holoprotein or conjugated protein is an apoprotein combined with its prosthetic group. [1]Some enzymes do not need additional components to show full activity. Others require non-protein molecules called cofactors to be bound for activity. [2]

  4. Conjugated protein - Wikipedia

    en.wikipedia.org/wiki/Conjugated_protein

    A conjugated protein is a protein that functions in interaction with other (non-polypeptide) chemical groups attached by covalent bonding or weak interactions. [ 1 ] Many proteins contain only amino acids and no other chemical groups, and they are called simple proteins.

  5. Glucuronosyltransferase - Wikipedia

    en.wikipedia.org/wiki/Glucuronosyltransferase

    Arguably the most important of the Phase II (conjugative) enzymes, UGTs have been the subject of increasing scientific inquiry since the mid-to-late 1990s. The reaction catalyzed by the UGT enzyme involves the addition of a glucuronic acid moiety to xenobiotics and is the most important pathway for the human body's elimination of the most ...

  6. Horseradish peroxidase - Wikipedia

    en.wikipedia.org/wiki/Horseradish_peroxidase

    Horseradish peroxidase is a 44,173.9-dalton glycoprotein with six lysine residues which can be conjugated to a labeled molecule. It produces a coloured, fluorimetric [6] or luminescent derivative of the labeled molecule when incubated with a proper substrate, allowing it to be detected and quantified.

  7. Bioconjugation - Wikipedia

    en.wikipedia.org/wiki/Bioconjugation

    The nucleophilic lysine residue is commonly targeted site in protein bioconjugation, typically through amine-reactive N-hydroxysuccinimidyl (NHS) esters. [3] To obtain optimal number of deprotonated lysine residues, the pH of the aqueous solution must be below the pKa of the lysine ammonium group, which is around 10.5, so the typical pH of the reaction is about 8 and 9.

  8. Bilirubin - Wikipedia

    en.wikipedia.org/wiki/Bilirubin

    Instead the conjugated bilirubin is converted back into the unconjugated form by the enzyme β-glucuronidase (in the gut, this enzyme is located in the brush border of the lining intestinal cells) and a large proportion is reabsorbed through the enterohepatic circulation. In addition, recent studies point towards high total bilirubin levels as ...

  9. Conjugated system - Wikipedia

    en.wikipedia.org/wiki/Conjugated_system

    Cinnamaldehyde is a naturally-occurring compound that has a conjugated system penta-1,3-diene is a molecule with a conjugated system Diazomethane conjugated pi-system. In theoretical chemistry, a conjugated system is a system of connected p-orbitals with delocalized electrons in a molecule, which in general lowers the overall energy of the molecule and increases stability.

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