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tetrahedron report number 124 suicide substrates
tetrahedron report number 124 suicide substrates

... The second generation of enzyme-specific inactivation reagents have been in use for about the past decade and differ from the first in that the reactive functional group is latent in the molecules in solution. Only after binding to the target enzyme and after the enzyme begins catalysis is the react ...
products  of  the  dioxygenase  reaction ... useful  intermediates  for  natural-product  syntheses ...
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Catalytic triad



A catalytic triad refers to the three amino acid residues that function together at the centre of the active site of some hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An Acid-Base-Nucleophile triad is 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 regenerate free enzyme. The nucleophile is most commonly a serine or cysteine amino acid, but occasionally threonine. Because enzymes fold into complex three-dimensional structures, the residues of a catalytic triad can be far from each other along the amino-acid sequence (primary structure), however, they are brought close together in the final fold.As well as divergent evolution of function (and even the triad's nucleophile), catalytic triads show some of the best examples of convergent evolution. Chemical constraints on catalysis have led to the same catalytic solution independently evolving in at least 23 separate superfamilies. Their mechanism of action is consequently one of the best studied in biochemistry.
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