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Introduction to Enzyme and Coenzyme Chemistry - E-Library Home

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3 <strong>Enzyme</strong>s are Wonderful<br />

Catalysts<br />

3.1 <strong>Introduction</strong><br />

The function of enzymes is <strong>to</strong> catalyse biochemical reactions. Each enzyme has<br />

evolved over millions of years <strong>to</strong> catalyse one particular reaction, so it is<br />

perhaps not surprising <strong>to</strong> Wnd that they are extremely good catalysts when<br />

compared with man-made catalysts.<br />

The hallmarks of enzyme catalysis are: speed, selectivity <strong>and</strong> speciWcity.<br />

<strong>Enzyme</strong>s are capable of catalysing reactions at rates well in excess of a million-fold<br />

faster than the uncatalysed reaction, typical ratios of k cat =k uncat being<br />

10 6 ---10 14 . Figure 3.1 shows an illustration of the speed of enzyme-catalysed<br />

glycoside hydrolysis. The rate of acid-catalysed glycoside catalysis is accelerated<br />

10 3 -fold by intramolecular acid catalysis, but enzyme-catalysed glycoside hydrolysis<br />

is 10 4 -fold faster still – some 10 7 faster than the uncatalysed reaction<br />

carried out at pH 1.<br />

Rate of hydrolysis<br />

HO<br />

HO<br />

OH<br />

O<br />

OH<br />

H +<br />

OPh<br />

acid-catalysed<br />

hydrolysis<br />

k obs = 1.9 10 −6 s −1 in 0.1 M HCl<br />

HO<br />

HO<br />

OH<br />

O<br />

OH<br />

H<br />

O<br />

O<br />

O<br />

intramolecular<br />

catalysis<br />

k uni = 1.4 10 −3 s −1<br />

Enz<br />

OH<br />

OH O O<br />

H<br />

O<br />

HO<br />

OPh<br />

β-galac<strong>to</strong>sidase k cat = 40 s −1<br />

OH<br />

Figure 3.1 Rate acceleration of glycoside hydrolysis by intramolecular <strong>and</strong> enzyme catalysis.<br />

29

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