BRAINCAKEEffect of pH on Enzyme Action
The tertiary structure of the active site of the enzyme is determined by hydrogen and ionic bonds between -NH2 and -COOH groups and bonding and interactions between the R-groups.
Each enzyme has an optimum pH.
Since the pH is a measure of the hydrogen ion concentration, changes to the H+ concentration may alter the shape of the active site by:
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Key terms in this lesson
- ionic bond
- A strong bond formed by the electrostatic attraction between oppositely charged ions.
- tertiary structure
- The further coiling and folding of a polypeptide into a specific three-dimensional shape, held by ionic bonds, hydrogen bonds and disulfide bridges between R-groups.
- active site
- The region of an enzyme, formed by the tertiary structure, with a shape complementary to its substrate, where the substrate binds.
- denaturation
- A permanent change to the tertiary or quaternary structure of a protein, caused by heat or pH extremes, that alters the shape of the active site so it is no longer complementary to its substrate.