What is the most important factor in determining the specificity of an enzyme quizlet?

Since the substrate must fit into the active site of the enzyme before catalysis can occur, only properly designed molecules can serve as substrates for a specific enzyme; in many cases, an enzyme will react with only one naturally occurring molecule. Two oxidoreductase enzymes will serve to illustrate the principle of enzyme specificity. One (alcohol dehydrogenase) acts on alcohol, the other (lactic dehydrogenase) on lactic acid; the activities of the two, even though both are oxidoreductase enzymes, are not interchangeable—i.e., alcohol dehydrogenase will not catalyze a reaction involving lactic acid or vice versa, because the structure of each substrate differs sufficiently to prevent its fitting into the active site of the alternative enzyme. Enzyme specificity is essential because it keeps separate the many pathways, involving hundreds of enzymes, that function during metabolism.

Not all enzymes are highly specific. Digestive enzymes such as pepsin and chymotrypsin, for example, are able to act on almost any protein, as they must if they are to act upon the varied types of proteins consumed as food. On the other hand, thrombin, which reacts only with the protein fibrinogen, is part of a very delicate blood-clotting mechanism and thus must act only on one compound in order to maintain the proper functioning of the system.

When enzymes were first studied, it was thought that most of them were “absolutely specific”—that they would react with only one compound. In most cases, however, a molecule other than the natural substrate can be synthesized in the laboratory; it is enough like the natural substrate to react with the enzyme. Use of these synthetic substrates has been valuable in understanding enzymatic action. It must be remembered, however, that, in the living cell, many enzymes are absolutely specific for the compounds found there.

All enzymes isolated thus far are specific for the type of chemical reaction they catalyze—i.e., oxidoreductases do not catalyze hydrolase reactions, and hydrolases do not catalyze reactions involving oxidation and reduction. An enzyme therefore catalyzes a specific chemical reaction but may be able to do so on several similar compounds.

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What is the most important factor in determining the specific of an enzyme?

The most important factor governing the fit of a substrate for an enzyme is the amino acid sequence around the bond to be cleaved. Trypsin cleaves amides and esters of the basic amino acids arginine and lysine. Thrombin has a similar preference, but is more specific for arginine than for lysine.

What is important in determining specificity in enzyme?

The shape of the active site (and therefore the specificity of the enzyme) is determined by the complex tertiary structure of the protein that makes up the enzyme: Proteins are formed from chains of amino acids held together by peptide bonds. The order of amino acids determines the shape of an enzyme.

What determines the specificity of an enzyme for its substrate quizlet?

An enzyme's ability to react with its substrate is due to the complementary shape of the enzyme and substrate. The concentration of the substrate determines the specificity of the enzyme for its substrate.