Hardcover Springer. Produktbeschreibung Molecular and Cellular Enzymology addresses not only experienced enzymologists but also students, teachers and academic and industrial researchers who are confronted with enzymological problems during their fundamental or applied research.
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In this field there is an urgent need for training in order to meet the requirements of both research and industrial endeavours. This book consists of several levels. In order to facilitate the task of students, two typographies have been adopted. The main text corresponds to basic knowledge, whereas text in a smaller font provides more specialised information. Specialists will also find topics more deeply expounded with the principal bibliographic references cited.
The bibliography, however, is not exhaustive; the choice includes general books and review articles as well as some specialised articles. Most central metabolic pathways are regulated at a few key steps, typically through enzymes whose activity involves the hydrolysis of ATP. Because this reaction releases so much energy, other reactions that are thermodynamically unfavorable can be coupled to ATP hydrolysis, driving the overall series of linked metabolic reactions.
There are five main ways that enzyme activity is controlled in the cell. Enzymes can be either activated or inhibited by other molecules. For example, the end product s of a metabolic pathway are often inhibitors for one of the first enzymes of the pathway usually the first irreversible step, called committed step , thus regulating the amount of end product made by the pathways. Such a regulatory mechanism is called a negative feedback mechanism , because the amount of the end product produced is regulated by its own concentration.
This helps with effective allocations of materials and energy economy, and it prevents the excess manufacture of end products. Like other homeostatic devices , the control of enzymatic action helps to maintain a stable internal environment in living organisms. Examples of post-translational modification include phosphorylation , myristoylation and glycosylation. Chymotrypsin , a digestive protease , is produced in inactive form as chymotrypsinogen in the pancreas and transported in this form to the stomach where it is activated.
This stops the enzyme from digesting the pancreas or other tissues before it enters the gut.
This type of inactive precursor to an enzyme is known as a zymogen  : —53 or proenzyme. Enzyme production transcription and translation of enzyme genes can be enhanced or diminished by a cell in response to changes in the cell's environment. This form of gene regulation is called enzyme induction. For example, bacteria may become resistant to antibiotics such as penicillin because enzymes called beta-lactamases are induced that hydrolyse the crucial beta-lactam ring within the penicillin molecule.
Induction or inhibition of these enzymes can cause drug interactions. Enzymes can be compartmentalized, with different metabolic pathways occurring in different cellular compartments. In multicellular eukaryotes , cells in different organs and tissues have different patterns of gene expression and therefore have different sets of enzymes known as isozymes available for metabolic reactions. This provides a mechanism for regulating the overall metabolism of the organism.
For example, hexokinase , the first enzyme in the glycolysis pathway, has a specialized form called glucokinase expressed in the liver and pancreas that has a lower affinity for glucose yet is more sensitive to glucose concentration. Since the tight control of enzyme activity is essential for homeostasis , any malfunction mutation, overproduction, underproduction or deletion of a single critical enzyme can lead to a genetic disease.
The malfunction of just one type of enzyme out of the thousands of types present in the human body can be fatal. An example of a fatal genetic disease due to enzyme insufficiency is Tay—Sachs disease , in which patients lack the enzyme hexosaminidase. One example of enzyme deficiency is the most common type of phenylketonuria. Many different single amino acid mutations in the enzyme phenylalanine hydroxylase , which catalyzes the first step in the degradation of phenylalanine , result in build-up of phenylalanine and related products.
Some mutations are in the active site, directly disrupting binding and catalysis, but many are far from the active site and reduce activity by destabilising the protein structure, or affecting correct oligomerisation. Another way enzyme malfunctions can cause disease comes from germline mutations in genes coding for DNA repair enzymes. Defects in these enzymes cause cancer because cells are less able to repair mutations in their genomes.
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This causes a slow accumulation of mutations and results in the development of cancers. An example of such a hereditary cancer syndrome is xeroderma pigmentosum , which causes the development of skin cancers in response to even minimal exposure to ultraviolet light. Enzymes are used in the chemical industry and other industrial applications when extremely specific catalysts are required. Enzymes in general are limited in the number of reactions they have evolved to catalyze and also by their lack of stability in organic solvents and at high temperatures. As a consequence, protein engineering is an active area of research and involves attempts to create new enzymes with novel properties, either through rational design or in vitro evolution.
From Wikipedia, the free encyclopedia. For the use of natural catalysts in organic chemistry, see Biocatalysis. Index Outline. See also: Protein structure. See also: Enzyme catalysis and Transition state theory. See also: Protein dynamics. Main article: Allosteric regulation.
Main article: Cofactor biochemistry. Main articles: Activation energy , Thermodynamic equilibrium , and Chemical equilibrium. A chemical reaction mechanism with or without enzyme catalysis. The enzyme E binds substrate S to produce product P. Saturation curve for an enzyme reaction showing the relation between the substrate concentration and reaction rate. Main article: Enzyme kinetics.
An enzyme binding site that would normally bind substrate can alternatively bind a competitive inhibitor , preventing substrate access. Dihydrofolate reductase is inhibited by methotrexate which prevents binding of its substrate, folic acid. The coenzyme folic acid left and the anti-cancer drug methotrexate right are very similar in structure differences show in green. As a result, methotrexate is a competitive inhibitor of many enzymes that use folates. Main article: Enzyme inhibitor.
See also: Genetic disorder. Main article: Industrial enzymes. Biology portal Metabolism portal Food portal. Biochemistry 5th ed. San Francisco: W. Biochem Soc Trans. Biochemical Journal. Nucleic Acids Research. Bibcode : Sci Bioorganic Chemistry. Histoire de l'Academie Royale des Sciences. A History of Science: in Five Volumes. Harper and Brothers. Annales de chimie et de physique. Trends in Biotechnology.
Verhandlungen des Naturhistorisch-medicinischen Vereins zu Heidelberg.
In Heilbron JL ed. Oxford: Oxford University Press. Nobel Laureate Biography. Retrieved 23 February Paris, France: Masson and Co. See Chapter 1, especially page 9.
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