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Unit 6

Unit 6

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Published by Moon Phạm

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Published by: Moon Phạm on Mar 06, 2012
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Enzymes
Living systems contain large protein molecules called enzymes. Those largeglobular proteins range in molecular weight from about 10.000 to several million.Each of the thousands of known enzymes has a characteristic three- dimensionalshape with a specific surface configuration as a result of it primary, secondary, andtertiary structures. The unique configuration of each enzyme enables it to “find”the correct substrate from among the large number of diverse molecules in the cell.Although some enzymes consist entirely of proteins, most consist of both a protein portion called an apoenzyme and a nonprotein component called a cofactor.Together, the apoenzyme and cofactor form a holoenzyme, or whose enzyme. If the cofactor is removed, the apoenzyme will not function. The cofactor can be ametal ion or a complex organic molecule called a coenzyme. Coenzymes mayassist the enzyme by accepting atoms removed from the substrate or by donatingthem to other molecules in subsequent reactions. Many coenzymes are derivedfrom vitamins.The name of enzymes usually end in- ase. All enzymes can be grouped intosix classes, according to the type of chemical reaction they catalyze. Enzymeswithin each of the major classes are named according to the more specific types of reactions they assist. They are:1.Oxidoreductase: oxidation-reduction in which oxygen andhydrogen are gained or lost.2.Transfuse: transfer of functional groups, such as an aminogroup, acetyl group, or phosphate group3.Hydrolase: hydrolysis (addition of water)4.Lyase: removal of groups of atoms without hydrolysis.5.Isomerate: rearrangement of atoms within a molecule6.Ligase: joining of two molecules (using energy usually derivedfrom break down of ATP)
Mechanism of enzymatic action
 
Enzymes can speed up chemical reaction in several ways. Whatever themethod, the result is that the enzyme lowers the activation energy for the reactionwithout increasing the temperature or pressure inside the cell. Although scientistsdo not completely understand how enzymes lower the activation energy of chemical reaction, the general sequence of events in enzyme reaction is asfollows:1.The surface of the substrate contacts a specific region of thesurface of the enzyme molecule, called the active site.2.A temporary intermediate compound forms, called an enzyme-substrate complex.3.The substrate molecule is transformed by the rearrangement oexisting atoms, the breakdown of the substrate molecule, or combinationwith another substrate molecule.4.The transformed substrate molecules-the products of thereaction-are released from the enzyme molecule because they no longer fitin the active site of the enzyme.5.The unchanged enzyme is now free to react with other substratemolecules.Enzymes are extremely efficient. Under optimum conditions, they cancatalyze reaction at rates 10
8
to 10
10
times (up to 10 billion times) higher thanthose of comparable reactions without enzymes.In living cells, enzymes serve as biological catalysts. As catalysts, enzymesare specific. Each acts on a substrate (or substrates, when there are two or morereactants), and each catalyzes only one reaction. For example, a specific enzymemay be able to hydrolyze a peptide bond only between two specific amino acids.Other enzymes can hydrolyze starch but not cellulose; even though both starchand cellulose are polysaccharides composed of glucose subunits, the orientationof the subunits in the two polysaccharides differ. Enzymes have this specificity because the three dimensional shape of the active site fits the substrate somewhatas a lock fits with its key. However, the active site and substrate are flexible, andthey change shape somewhat as they meet to fit together more tightly. The
 
substrate is usually much smaller than the enzyme, and relatively few of theenzyme’s amino acids make up the active site.A certain compound can be a substrate for s number of different enzymesthat catalyze different reactions, so the fate of a compound depends on theenzymes that acts upon it. Glucose 6-photphate, a molecule that is important incell metabolism, can be acted upon by at least four different enzymes, and eachreaction will yield a different product.
Factors influence enzyme activity.
Several factors influence the activity ò enzyme. The more important aretemperature, pH, substrate concentration, and presence or absence of inhibitors.The rate of most chemical reactions increases as the temperature increases.Molecules move more slowly at lower temperatures than at higher temperaturesand so may not have enough energy to cause s chemical reaction. For enzymaticreactions, however, elevation beyond a certain temperature drastically reducesthe rate of reaction. This decrease is due to the enzyme’s denaturation, the lost of its characteristic three dimensional structure (tertiary configuration).Denaturation of protein a involves breakage of hydrogen bonds and othenoncovalent bonds. As might be expected, denaturation of an enzyme changesthe arrangement of the amino acids in the active site, altering its shape andcausing the enzyme to lose its catalytic ability. In some cases, denaturation is partially or fully reversible. However, if denaturation continues until the enzymehas lost its solubility and coagulates (as with cooked the albumin) the enzymecannot regain its original properties. Enzymes can be denatured by concentratedacids, bases, heavy-metal ions (such as lead, arsenic, or mercury), alcohol, andultraviolet radiation.Most enzymes have an optimum pH at with their activity is characteristicallymaximal. Above or bellow this pH value, enzyme activity, and therefore thereaction rate, declines. When the H
+
concentration (pH) in the medium ischanged, many of the enzyme’s amino acids are effected and the protein’s three-dimensional structure is altered. Extreme changes in pH can cause denaturation.

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