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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 Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. [1] As a system of enzyme nomenclature, every EC number is associated with a recommended name for the corresponding enzyme-catalyzed reaction. EC numbers do not specify enzymes but enzyme-catalyzed reactions.
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 )
In the pulsed state, both the heme a 3 and the Cu B nuclear centers are oxidized; this is the conformation of the enzyme that has the highest activity. A two-electron reduction initiates a conformational change that allows oxygen to bind at the active site to the partially-reduced enzyme. Four electrons bind to COX to fully reduce the enzyme.
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.
Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of the various adenosine phosphates (ATP, ADP, and AMP). By constantly monitoring phosphate nucleotide levels inside the cell, ADK plays an important role in cellular energy homeostasis .
Figure 13 shows a common way to illustrate the effect of an enzyme on a given biochemical reaction. [11] Figure 12: An energy profile, showing the products (Y), reactants (X), activation energy (E a) for the endothermic and exothermic reaction, and the enthalpy (ΔH). The profile for same reaction but with a catalyst is also shown.
The enzyme's reaction pathway contains binding to the substrate and active site, splitting of glycosidic bonds, unsaturated products forming, and product release. Pectin lyase is crucial to decaying plant materials and is commonly used in the food industry and biotechnology.