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Enzyme regulation. Enzyme Regulation Enzymes allow many chemical reactions to
occur within the homeostasis constraints of a living system. ...
... Something that has a major effect on enzyme regulation and stability is temperature. ...
Another example of enzyme regulation is that of competitive inhibitors. ...
... Understanding the biochemical properties of isozymes, also presents new possibilities
for treatment by induced regulation of enzyme activity. ...
... The mechanism for this powerful regulation of enzyme activity by diet is not clear
from this work; however, it most likely involves the glucose/insulin axis. ...
... The enzyme molecule has no change, therefore reacts the best. ... They are
indispensable for signal transduction and cell regulation. ...
Submitted by siralphred on October 23, 2007
Category: Science
Words: 1690 | Pages: 7
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Enzyme Regulation
Enzymes allow many chemical reactions to occur within the homeostasis constraints of a living system. Enzymes function as organic catalysts. A catalyst is a chemical involved in, but not changed by, a chemical reaction. Many enzymes function by lowering the activation energy of reactions. By bringing the reactants closer together, chemical bonds may be weakened and reactions will proceed faster than without the catalyst. Enzymes are proteins, the functioning of the enzyme is determined by the shape of the protein. The arrangement of molecules on the enzyme produces an area known as the active site within which the specific substrate(s) will "fit". It recognizes, confines and orients the substrate in a particular direction.
Enzymes function under very specific conditions including temperature and pH and are highly regulated. Enzyme regulation, specifically allosteric regulation will be discussed in this essay.
The term allosteric derives from the Greek for "another shape (or state)," thereby indicating that all enzymes capable of allosteric regulation can exist in two different states ( Hammes ). In one of the two forms, the enzyme has a high affinity for its substrate, whereas in the other form, it has little or no affinity for its substrate. Enzymes with this property are called allosteric enzymes. The two different forms of an allosteric enzyme are readily interconvertible and are, in fact, in equilibrium with each other. Obviously, the reaction rate is high when the enzyme is in its high-affinity form and low or even zero when the enzyme is in its low-affinity form.
Whether the active or inactive form of an allosteric enzyme is favored depends on the cellular concentration of the appropriate regulatory substance, called an allosteric effector. In the case of isoleucine synthesis, the allosteric enzyme is threonine deaminase and the allosteric effector is isoleucine(Sacher). More generally, an allosteric...
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