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  2. Isomerase - Wikipedia

    en.wikipedia.org/wiki/Isomerase

    The isomerization energy, for example, for converting from a stable cis isomer to the less stable trans isomer is greater than for the reverse reaction, explaining why in the absence of isomerases or an outside energy source such as ultraviolet radiation a given cis isomer tends to be present in greater amounts than the trans isomer.

  3. Isomerization - Wikipedia

    en.wikipedia.org/wiki/Isomerization

    In chemistry, isomerization or isomerisation is the process in which a molecule, polyatomic ion or molecular fragment is transformed into an isomer with a different chemical structure. [1] Enolization is an example of isomerization, as is tautomerization .

  4. Glucose-6-phosphate isomerase - Wikipedia

    en.wikipedia.org/wiki/Glucose-6-phosphate_isomerase

    The protein encoded by this gene is a dimeric enzyme that catalyzes the reversible isomerization of G6P and F6P. [12] [13] Since the reaction is reversible, its direction is determined by G6P and F6P concentrations. [9] glucose 6-phosphate ↔ fructose 6-phosphate. The protein has different functions inside and outside the cell.

  5. Triosephosphate isomerase - Wikipedia

    en.wikipedia.org/wiki/Triosephosphate_isomerase

    However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. In humans, deficiencies in TPI are associated with a progressive, severe neurological disorder called triose phosphate isomerase deficiency. Triose phosphate isomerase deficiency is characterized by chronic hemolytic anemia.

  6. Histone-modifying enzymes - Wikipedia

    en.wikipedia.org/wiki/Histone-modifying_enzymes

    Isomerization involves transforming a molecule so that it adopts a different structural conformation; proline isomerization plays an integral role in the modification of histone tails. [36] Fpr4 is the prolyl isomerase enzyme (PPIase) which converts the amino acid proline (P) on histones between the cis and trans conformations .

  7. Ribose-5-phosphate isomerase - Wikipedia

    en.wikipedia.org/wiki/Ribose-5-phosphate_isomerase

    If it does bind the furanose ring, it next opens the ring. Then the enzyme forms the eneldiol which is stabilized by a lysine or arginine residue. [ 6 ] [ 8 ] Calculations have demonstrated that this stabilization is the most significant contributor to the overall catalytic activity of this isomerase and a number of others like it.

  8. Pseudouridine - Wikipedia

    en.wikipedia.org/wiki/Pseudouridine

    The proteins that do this modification are called pseudouridine synthases (PUS) and are found in all kingdoms of life. Most research has been done on how PUS modify tRNA, so mechanisms involving snRNA, and mRNA are not clearly defined. PUS can vary on RNA specificity, structure, and isomerization mechanisms. The different structures of PUS are ...

  9. Alkyne zipper reaction - Wikipedia

    en.wikipedia.org/wiki/Alkyne_zipper_reaction

    The alkyne zipper reaction is an organic reaction that involves isomerization of a non terminal alkyne into a terminal alkyne. This reaction was first reported by Alexey Favorsky in 1887 (J. Russ. Phys.-Chem. Soc., 19, 414 (1887)).