The amino acids of histidine, aspartate, glutamate, lysine, cysteine, and argini

Question

The amino acids of histidine, aspartate, glutamate, lysine, cysteine, and arginine are all greatly overrepresented in active sites compared with their abundance in proteins in general. Why might this be? The amino acids of histidine, aspartate, glutamate, lysine, cysteine, and arginine are all greatly overrepresented in active sites compared with their abundance in proteins in general. Why might this be? The amino acids of histidine, aspartate, glutamate, lysine, cysteine, and arginine are all greatly overrepresented in active sites compared with their abundance in proteins in general. Why might this be?

Explanation / Answer

These are the amino acids which possess a specific structure that take part in a various catalytic reactions.

For example: the presence of an imidazole ring in the side chain of histidine, takes part in catalytic reactions, the side chains of glutamate, aspartate, lysine and arginine form ionic bonds.

Moreover, these amino acids also function as catalytic triads - three amino acids function together at the centre of the active site of some enzymes such as hydrolase and transferase.

eg. cysteine-histidine-aspartate,

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