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Chapter Twenty Four ENZYMES Enzymes catalyze the chemical reactions necessary for growth, repair, and maintenance of a ng organism: Wihout them, it could not survive. The fungus Penicillium, pictured here, produces the potent antibiotic penicilin. Penicilin is lethal to bacteria because it incapacitates an enzyme. Instrumental in the construction of the bacterial cell wall. Because humans lack similar enzurtes, in’ effec. Chapter Objectives + To understand the functions of enzymes. * To be able to distinguish between activators and inhibitors. * To understand the mode of enzyme activity * To be able to distinguish between apoenzymes and coenzymes: © To become familiar with the classificatian of enzymes. * To become aware of the clinical significance of plasma enzyme concentrations, Enzymes 369 Enzymes are biologic catalysts. Catalysts are substances that increase the speed of @ chemical reaction. Although a catalyst influences a chemical reaction, it is not itself permanently changed nor does it cause the reaction to occur; that is, a catalyst can increase the speed of a reaction but cannot cause that reaction if it would not occur in the absence of that catalyst. Since catalysts are not used up, they can be used over and over again, Enzymes are organic catalysts produced by living organisms. The reactant in an enzyme-catalyzed reaction is called the substvate, The active site of an enzyme is that smail portion of the molecule which is responsible for the catalytic action of the enzyme. Enzymes provide a chemical pathway that has a lower "activation ‘energy than the same reaction uncatalyzed. How do enzymes differ from nonbiolo- gic catalysts and why are there so many in the body? Enzymes are superior to ‘other catalysts in several ways, 1. They have a much greater catalytic power. Consider the reaction carhonic anhydrase CO, + HO HCOs which takes place in red blood cells (see page 478). The enzyme carbonic anhydrase increases the reaction rate over 10 million times that of the same reaction without the presence of the enzyme. In general, enzymes increase the rate of reaction from over 1 millon to over 1 trlion times. faster than a corresponding reaction without an enzyme. Few catalysts can ‘cause such an increase in reaction rate. 2. Enzymes are highly specific with varying degrees of specificity, Some en: zymes exhibit absolute specifity. They act on one substrate and only on that substrate. For example, the enzyme succinic dehydrogenase (see Page 417) catalyzes the conversion of succinic acid to furnatic acid, Not only does succinic dehydrogenase act specifically on succinic acid, it pro- duces only a trans isomer (fumaric acid) and never the cis isomer (malic acid). H_C00H ~— HOOC, COOH « cH \ A HOO” H iH “MH fumaric acid (a tans isomer) malic acd a somes) A second example of such an enzyme is NO synthase (ntti oxide syn- thase), which catalyzes the production of NO. While there is a plentiful supply of oxygen in all cells, there is only one source of nitrogen for this Particular reaction. itis the amino acid arginine: arginine MOSM, citrulline + NO Some enzymes exhibit stereospecificity. Such enzymes can detect the difference between optical isomers (mirror images) and select only one of such isomers. For example, the enzyme arginase catalyzes the hydrolysis of L-arginine but has no effect upon the hydrolysis of o-arginine, Some enzymes are linkage specific. That fs, they catalyze the reaction which breaks the bonds only between specific groups. For example, the 370 24-1 Enzyme Reactions 24 Enzymes enzyme thrombin will break the bonds between the amino acids arginine land glycine end does not affect bonds between other amino acids. Other enzymes exhibit reaction specificity. They catalyze certain types of reactions. Esterases (see page 379) catalyze the hydrolysis of esters in enzyme Coenzyme A [CoA, structure (24-1)] Is essential in the metabolism of carbohy:

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