Search results
Results from the WOW.Com Content Network
The Lineweaver–Burk plot derives from a transformation of the Michaelis–Menten equation, = + in which the rate is a function of the substrate concentration and two parameters , the limiting rate, and , the Michaelis constant.
The plot is occasionally attributed to Augustinsson [5] and referred to the Woolf–Augustinsson–Hofstee plot [6] [7] [8] or simply the Augustinsson plot. [9] However, although Haldane, Woolf or Eadie were not explicitly cited when Augustinsson introduced the versus / equation, both the work of Haldane [10] and of Eadie [3] are cited at other places of his work and are listed in his ...
A decade before Michaelis and Menten, Victor Henri found that enzyme reactions could be explained by assuming a binding interaction between the enzyme and the substrate. [11] His work was taken up by Michaelis and Menten, who investigated the kinetics of invertase, an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose. [12]
Enzymes are listed here by their classification in the International Union of Biochemistry and Molecular Biology's Enzyme Commission (EC) numbering system: Category:Oxidoreductases (EC 1) ( Oxidoreductase )
As shown on the right, enzymes with a substituted-enzyme mechanism can exist in two states, E and a chemically modified form of the enzyme E*; this modified enzyme is known as an intermediate. In such mechanisms, substrate A binds, changes the enzyme to E* by, for example, transferring a chemical group to the active site, and is then released.
AO catalyzes the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide.. an aldehyde + H 2 O + O 2 ⇌ a carboxylate + H 2 O 2 + H +; Though the enzyme uses molecular oxygen as an electron acceptor, the oxygen atom that is incorporated into the carboxylate product is from water; however, the exact mechanism of reduction is still not known for AO.
Kexin (EC 3.4.21.61) is a prohormone-processing protease, specifically a yeast serine peptidase, [1] found in the budding yeast (S. cerevisiae).It catalyzes the cleavage of -Lys-Arg- and -Arg-Arg- bonds to process yeast alpha-factor pheromone and killer toxin precursors.
Thus, the two substrates of this enzyme are xyloglucan and H 2 O, whereas its product is xyloglucan oligosaccharides. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O- and S-glycosyl compounds. The systematic name of this enzyme class is [(1->6)-alpha-D-xylo]-(1->4)-beta-D-glucan glucanohydrolase.