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  2. Denaturation (biochemistry) - Wikipedia

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

    Protein denaturation is also a consequence of cell death. [4] [5] Denatured proteins can exhibit a wide range of characteristics, from conformational change and loss of solubility or dissociation of cofactors to aggregation due to the exposure of hydrophobic groups. The loss of solubility as a result of denaturation is called coagulation. [6]

  3. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may ...

  4. Deamination - Wikipedia

    en.wikipedia.org/wiki/Deamination

    Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy. The amino group is removed from the amino acid and converted to ammonia.

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. [1]: 8.1 Metabolic pathways depend upon enzymes to catalyze individual steps.

  6. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Post-translational modifications can occur before protein folding or after. Common biological methods of modifying peptide chains after translation include methylation, phosphorylation, and disulfide bond formation. Methylation often occurs to arginine or lysine and involves adding a methyl group to a nitrogen (replacing a hydrogen).

  7. Protease - Wikipedia

    en.wikipedia.org/wiki/Protease

    Ribbon diagram of a protease (TEV protease) complexed with its peptide substrate in black with catalytic residues in red.(. A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2]

  8. Metabolism - Wikipedia

    en.wikipedia.org/wiki/Metabolism

    Metabolism (/ m ə ˈ t æ b ə l ɪ z ə m /, from Greek: μεταβολή metabolē, "change") is the set of life-sustaining chemical reactions in organisms.The three main functions of metabolism are: the conversion of the energy in food to energy available to run cellular processes; the conversion of food to building blocks of proteins, lipids, nucleic acids, and some carbohydrates; and the ...

  9. Gluconeogenesis - Wikipedia

    en.wikipedia.org/wiki/Gluconeogenesis

    This system of reciprocal control allow glycolysis and gluconeogenesis to inhibit each other and prevents a futile cycle of synthesizing glucose to only break it down. Pyruvate kinase can be also bypassed by 86 pathways [ 28 ] not related to gluconeogenesis, for the purpose of forming pyruvate and subsequently lactate; some of these pathways ...