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Introduction to Enzyme and Coenzyme Chemistry - E-Library Home

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All <strong>Enzyme</strong>s are Proteins 23<br />

O<br />

O −<br />

P O −<br />

2+<br />

O Mg<br />

O P O−<br />

O<br />

R<br />

Figure 2.20 Binding of polyphosphate by magnesium.<br />

Figure 2.21 Uses of zinc (a) in a structural role <strong>and</strong> (b) as a Lewis acid.<br />

The other common role of metal ions is as redox reagents. Since none of<br />

the 20 common amino acids are able <strong>to</strong> perform any useful catalytic redox<br />

chemistry, it is not surprising that many redox enzymes employ redox-active<br />

metal ions. We shall meet a number of examples of these redox-active metalloenzymes<br />

in Chapter 6. For a more detailed discussion of the role of metal ions<br />

in biological systems the reader is referred <strong>to</strong> several excellent texts in<br />

bio-inorganic chemistry.<br />

2.9 Membrane-associated enzymes<br />

Although the majority of enzymes are freely soluble in water <strong>and</strong> exist in the<br />

aqueous cy<strong>to</strong>plasm of living cells, there is a substantial class of enzymes that are<br />

associated with the biological membranes which encompass all cells. Biological<br />

membranes are made up of a lipid bilayer composed of phospholipid molecules<br />

containing a polar head group <strong>and</strong> a hydrophobic fatty acid tail. The phospholipid<br />

molecules assemble spontaneously <strong>to</strong> form a stable bilayer in which the<br />

hydrophilic head groups are exposed <strong>to</strong> solvent water <strong>and</strong> the hydrophobic tails<br />

are packed <strong>to</strong>gether in a hydrophobic interior.<br />

<strong>Enzyme</strong>s that are associated with biological membranes fall in<strong>to</strong> two<br />

classes, as illustrated in Figure 2.22:<br />

(1) extrinsic membrane proteins which are bound loosely <strong>to</strong> the surface of the<br />

membrane, often by a non-speciWc hydrophobic interaction, or in some<br />

cases by a non-peptide membrane ‘anchor’ which is covalently attached <strong>to</strong><br />

the protein;

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