Allied Journal of Medical Research

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Allied Journal of Medical Research 44 7897 074717

Catalytic Triad Scholarly Peer-review Journal

A catalytic triad may be a set of three coordinated amino acids which will be found within the site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, and acylases). An Acid-Base-Nucleophile triad may be a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the merchandise and regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine or even selenocysteine. The 3D structure of the enzyme brings together the triad residues in a precise orientation, even though they may be far apart in the sequence (primary structure).

As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show a number of the simplest samples of convergent evolution. Chemical constraints on catalysis have led to an equivalent catalytic solution independently evolving in a minimum of 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.

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