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  2. Alloenzyme - Wikipedia

    en.wikipedia.org/wiki/Alloenzyme

    These are opposed to isozymes, which are enzymes that perform the same function, but which are coded by genes located at different loci. [ 1 ] Alloenzymes are common biological enzymes that exhibit high levels of functional evolutionary conservation throughout specific phyla and kingdoms .

  3. Aspartate carbamoyltransferase - Wikipedia

    en.wikipedia.org/wiki/Aspartate_carbamoyltransferase

    Aspartate carbamoyltransferase (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway (EC 2.1.3.2). [1]In E. coli, the enzyme is a multi-subunit protein complex composed of 12 subunits (300 kDa in total). [2]

  4. Isozyme - Wikipedia

    en.wikipedia.org/wiki/Isozyme

    3.) Isoenzymes of alkaline phosphatase: [7] Six isoenzymes have been identified. The enzyme is a monomer, the isoenzymes are due to the differences in the carbohydrate content (sialic acid residues). The most important ALP isoenzymes are α 1-ALP, α 2-heat labile ALP, α 2-heat stable ALP, pre-β ALP and γ-ALP.

  5. Cytochrome - Wikipedia

    en.wikipedia.org/wiki/Cytochrome

    Photosystem II, the first protein complex in the light-dependent reactions of oxygenic photosynthesis, contains a cytochrome b subunit. Cyclooxygenase 2, an enzyme involved in inflammation, is a cytochrome b protein. In the early 1960s, a linear evolution of cytochromes was suggested by Emanuel Margoliash [7] that led to the molecular clock ...

  6. Regulatory enzyme - Wikipedia

    en.wikipedia.org/wiki/Regulatory_enzyme

    In a) the allosteric enzyme functions normally. In b), it is inhibited. This type of enzymes presents two binding sites: the substrate of the enzyme and the effectors. Effectors are small molecules which modulate the enzyme activity; they function through reversible, non-covalent binding of a regulatory metabolite in the allosteric site (which ...

  7. Phosphatase - Wikipedia

    en.wikipedia.org/wiki/Phosphatase

    Because a phosphatase enzyme catalyzes the hydrolysis of its substrate, it is a subcategory of hydrolases. [1] Phosphatase enzymes are essential to many biological functions, because phosphorylation (e.g. by protein kinases) and dephosphorylation (by phosphatases) serve diverse roles in cellular regulation and signaling. [2]

  8. Ribonuclease III - Wikipedia

    en.wikipedia.org/wiki/Ribonuclease_III

    Ribonuclease III (RNase III or RNase C) [1] (BRENDA 3.1.26.3) is a type of ribonuclease that recognizes dsRNA and cleaves it at specific targeted locations to transform them into mature RNAs. [2] These enzymes are a group of endoribonucleases that are characterized by their ribonuclease domain, which is labelled the RNase III domain. [3]

  9. ADP-ribose diphosphatase - Wikipedia

    en.wikipedia.org/wiki/ADP-ribose_diphosphatase

    ADP-ribose diphosphatase (EC 3.6.1.13) is an enzyme that catalyzes a hydrolysis reaction in which water nucleophilically attacks ADP-ribose to produce AMP and D-ribose 5-phosphate. Enzyme hydrolysis occurs by the breakage of a phosphoanhydride bond and is dependent on Mg 2+ ions that are held in complex by the enzyme.