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Hydrogen peroxide. Catalase is used in the food industry for removing hydrogen peroxide from milk prior to cheese production. [43] Another use is in food wrappers, where it prevents food from oxidizing. [44] Catalase is also used in the textile industry, removing hydrogen peroxide from fabrics to make sure the material is peroxide-free. [45]
d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...
Like glycolysis, the pentose phosphate pathway appears to have a very ancient evolutionary origin. The reactions of this pathway are mostly enzyme catalyzed in modern cells, however, they also occur non-enzymatically under conditions that replicate those of the Archean ocean, and are catalyzed by metal ions, particularly ferrous ions (Fe(II)). [5]
Enzyme 5.3.1.1 at KEGG Pathway Database. Compound C00118 at KEGG Pathway Database. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria.
Class I, the intracellular peroxidases, includes: cytochrome c peroxidase (CCP), a soluble protein found in the mitochondrial electron transport chain, where it probably protects against toxic peroxides; ascorbate peroxidase (AP), the main enzyme responsible for hydrogen peroxide removal in chloroplasts and cytosol of higher plants; [4] and ...
The optimum pH for the human enzyme is 6.5. [4] Enolase is present in all tissues and organisms capable of glycolysis or fermentation. The enzyme was discovered by Lohmann and Meyerhof in 1934, [5] and has since been isolated from a variety of sources including human muscle and erythrocytes. [4]
β-Fructofuranosidase is an enzyme that catalyzes the hydrolysis (breakdown) of the table sugar sucrose into fructose and glucose. [1] [2] Alternative names for β-fructofuranosidase EC 3.2.1.26 include invertase, saccharase, glucosucrase, β-fructosidase, invertin, fructosylinvertase, alkaline invertase, and acid invertase.
In enzymology, a NADH peroxidase (EC 1.11.1.1) is an enzyme that catalyzes the chemical reaction. NADH + H + + H 2 O 2 NAD + + 2 H 2 O. The presumed function of NADH peroxidase is to inactivate H 2 O 2 generated within the cell, for example by glycerol-3-phosphate oxidase during glycerol metabolism or dismutation of superoxide, before the H 2 O 2 causes damage to essential cellular components.
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