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New insight into plant intramembrane proteases
New insight into plant intramembrane proteases

prosthetic group as non polypeptide biocatalyst essential for
prosthetic group as non polypeptide biocatalyst essential for

... are different types of enzyme helpers, too, with different enzymes requiring different helpers or different kinds of friends. There are examples of cofactors, coenzymes and prosthetic groups in many biological processes. For example, cellular respiration occurs in all of your cells, which is a proce ...
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... Which of the following statements about the first tetrahedral intermediate in the chymotrypsin catalyzed hydrolysis of a peptide bond is/are correct? (Circle) When this intermediate collapses, the charge relay system relays the negative charge (of the tetrahedral intermediate) from the oxyanion hole ...
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Hamster Placental Lactogen-ll Contains a Structural Feature Unique
Hamster Placental Lactogen-ll Contains a Structural Feature Unique

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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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