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  2. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. [7] It contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7, [8] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7 ...

  3. Turnover number - Wikipedia

    en.wikipedia.org/wiki/Turnover_number

    In chemistry, the term "turnover number" has two distinct meanings.. In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1]

  4. Diffusion-limited enzyme - Wikipedia

    en.wikipedia.org/wiki/Diffusion-limited_enzyme

    Kinetically perfect enzymes have a specificity constant, k cat /K m, on the order of 10 8 to 10 9 M −1 s −1.The rate of the enzyme-catalysed reaction is limited by diffusion and so the enzyme 'processes' the substrate well before it encounters another molecule.

  5. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    Curve of the Michaelis–Menten equation labelled in accordance with IUBMB recommendations. In biochemistry, Michaelis–Menten kinetics, named after Leonor Michaelis and Maud Menten, is the simplest case of enzyme kinetics, applied to enzyme-catalysed reactions of one substrate and one product.

  6. Photorespiration - Wikipedia

    en.wikipedia.org/wiki/Photorespiration

    Hydrogen peroxide is a dangerously strong oxidant which must be immediately split into water and oxygen by the enzyme catalase. The conversion of 2× 2Carbon glycine to 1× C 3 serine in the mitochondria by the enzyme glycine-decarboxylase is a key step, which releases CO 2, NH 3, and reduces NAD to NADH. Thus, one CO

  7. Catechol oxidase - Wikipedia

    en.wikipedia.org/wiki/Catechol_oxidase

    Catechol oxidase is a copper oxidase that contains a type 3 di-copper cofactor and catalyzes the oxidation of ortho-diphenols into ortho-quinones coupled with the reduction of molecular oxygen to water.

  8. Oxidase - Wikipedia

    en.wikipedia.org/wiki/Oxidase

    In biochemistry, an oxidase is an oxidoreductase (any enzyme that catalyzes a redox reaction) that uses dioxygen (O 2) as the electron acceptor.In reactions involving donation of a hydrogen atom, oxygen is reduced to water (H 2 O) or hydrogen peroxide (H 2 O 2).

  9. Enzyme catalysis - Wikipedia

    en.wikipedia.org/wiki/Enzyme_catalysis

    These conformational changes also bring catalytic residues in the active site close to the chemical bonds in the substrate that will be altered in the reaction. After binding takes place, one or more mechanisms of catalysis lowers the energy of the reaction's transition state, by providing an alternative chemical pathway for the reaction.