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  2. Ligase - Wikipedia

    en.wikipedia.org/wiki/Ligase

    The naming of ligases is inconsistent and so these enzymes are commonly known by several different names. Generally, the common names of ligases include the word "ligase", such as in DNA ligase , an enzyme commonly used in molecular biology laboratories to join together DNA fragments.

  3. Ligation (molecular biology) - Wikipedia

    en.wikipedia.org/wiki/Ligation_(molecular_biology)

    EcoRI for example generates an AATT end, and since A and T have lower melting temperature than C and G, its melting temperature T m is low at around 6 ° C. [21] For most restriction enzymes, the overhangs generated have a T m that is around 15 ° C. [20] For practical purposes, sticky end ligations are performed at 12-16 ° C, or at room ...

  4. Flavin adenine dinucleotide - Wikipedia

    en.wikipedia.org/wiki/Flavin_adenine_dinucleotide

    The structure of this enzyme is highly conserved to maintain precisely the alignment of electron donor NADPH and acceptor FAD for efficient electron transfer. [26] The two electrons in reduced FAD are transferred one a time to adrenodoxin which in turn donates the single electron to the heme group of the mitochondrial P450. [27]

  5. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    It is an enzyme that accepts electrons from electron-transferring flavoprotein in the mitochondrial matrix, and uses these electrons to reduce ubiquinone. [30] This enzyme contains a flavin and a [4Fe–4S] cluster, but, unlike the other respiratory complexes, it attaches to the surface of the membrane and does not cross the lipid bilayer.

  6. Oxidoreductase - Wikipedia

    en.wikipedia.org/wiki/Oxidoreductase

    For example, an enzyme that catalyzed this reaction would be an oxidoreductase: A – + B → A + B – In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor). In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis:

  7. Flavoprotein - Wikipedia

    en.wikipedia.org/wiki/Flavoprotein

    This enzyme catalyses the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond [12] The B chain of dipicolinate synthase, an enzyme which catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid [13]

  8. List of enzymes - Wikipedia

    en.wikipedia.org/wiki/List_of_enzymes

    Function: Amylase is an enzyme that is responsible for the breaking of the bonds in starches, polysaccharides, and complex carbohydrates to be turned into simple sugars that will be easier to absorb. Clinical Significance: Amylase also has medical history in the use of Pancreatic Enzyme Replacement Therapy (PERT). One of the components is ...

  9. Ubiquitin ligase - Wikipedia

    en.wikipedia.org/wiki/Ubiquitin_ligase

    E3 ligases interact with both the target protein and the E2 enzyme, and so impart substrate specificity to the E2. Commonly, E3s polyubiquitinate their substrate with Lys48-linked chains of ubiquitin, targeting the substrate for destruction by the proteasome. However, many other types of linkages are possible and alter a protein's activity ...