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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. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme Optimum pH pH description Pepsin 1.5–1.6 Highly acidic Invertase 4.5 Acidic Lipase (stomach) ... Catalase 7.0 Neutral Urease 7.0 Neutral Cholinesterase 7.0

  4. Urease - Wikipedia

    en.wikipedia.org/wiki/Urease

    Sumner's work was the first demonstration that a protein can function as an enzyme and led eventually to the recognition that most enzymes are in fact proteins. Urease was the first enzyme crystallized. For this work, Sumner was awarded the Nobel prize in chemistry in 1946. [6] The crystal structure of urease was first solved by P. A. Karplus ...

  5. Catechol oxidase - Wikipedia

    en.wikipedia.org/wiki/Catechol_oxidase

    While a number of inhibitory strategies exist such as high temperature treatments(70-90 °C) to eliminate catechol oxidase catalytic activity, [6] a popular strategy is decreasing the pH with citric acid. Catechol oxidase is more catalytically active in the pH 4-8 range due to coordination of the histidine residues to the catalytic copper centers.

  6. Enzyme unit - Wikipedia

    en.wikipedia.org/wiki/Enzyme_unit

    The enzyme unit, or international unit for enzyme (symbol U, sometimes also IU) is a unit of enzyme's catalytic activity. [ 1 ] 1 U (μmol/min) is defined as the amount of the enzyme that catalyzes the conversion of one micro mole of substrate per minute under the specified conditions of the assay method .

  7. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    If the answer is yes then the reaction is the general type. Since most enzymes have an optimum pH of 6 to 7, the amino acids in the side chain usually have a pK a of 4~10. Candidate include aspartate, glutamate, histidine, cysteine. These acids and bases can stabilise the nucleophile or electrophile formed during the catalysis by providing ...

  8. Diffusion-limited enzyme - Wikipedia

    en.wikipedia.org/wiki/Diffusion-limited_enzyme

    Most enzymes have a rate around 10 5 s −1 M −1. The fastest enzymes in the dark box on the right (>10 8 s −1 M −1) are constrained by the diffusion limit. (Data adapted from reference [1]) A diffusion-limited enzyme catalyses a reaction so efficiently that the rate limiting step is that of substrate diffusion into the active site, or ...

  9. Cobetia amphilecti - Wikipedia

    en.wikipedia.org/wiki/Cobetia_amphilecti

    Cobetia amphilecti is a Gram-negative, aerobic, oxidase-negative, catalase-positive, bacterium.It has non-pigmented, rod-shaped cells, 0.8–0.9 μm in diameter and 1.1–1.3 μm long, motile by means of one polar and/or two or three lateral flagella.