Examining the structure of an enzyme can lead to hypotheses about the relationship between different amino acids in the protein’s structure and the protein’s function. One way to test these hypotheses is to use recombinant DNA technology to generate mutant versions of the enzyme and then examine the structure and function of these altered forms. 

One example of this kind of analysis is the work of A. R. Clarke and colleagues on the enzyme lactate dehydrogenase, published in 1989. Lactate dehydrogenase (LDH) catalyzes the reduction of pyruvate with NADH to form lactate (see Section 14.3). A schematic of the enzyme’s active site is shown below; the pyruvate is in the center.

    

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Lactate dehydrogenase Arg109 His 195. HN NH Asp¹68 NH H H ΝΗ Gin¹02 0= HN O=C CH3 NH₂ H H Arg171 Pyruvate C ΝΗ Thr246 H₂C-C-OH H NH H XN H N-(NADH) H CH3 II H₂C-C-CH₂ lle 250 Lactate dehydrogenase Arg109 His 195. HN NH Asp¹68 NH H H ΝΗ Gin¹02 0= HN O=C CH3 NH₂ H H Arg171 Pyruvate C ΝΗ Thr246 H₂C-C-OH H NH H XN H N-(NADH) H CH3 II H₂C-C-CH₂ lle 250

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a Arginine is a positively charged amino acid while Glutamine is a polar amino acid SO bot... View the full answer