Covalent Nucleophilic Catalysis

Abstract

Covalent nucleophilic catalysis is the involvement of a nucleophile on an enzyme (usually one of the side‐chain groups of an α‐amino acid residue) in forming a covalent (shared) bond with a reactant to generate an intermediate on the reaction pathway leading to the observed product(s).

Keywords: nucleophilic catalysis; covalent intermediate

Figure 1.

Reaction coordinate versus energy barrier for a hypothetical chemical reaction showing the difference between the uncatalysed reaction and enzyme‐catalysed reaction proceeding via a covalent intermediate.

Scheme
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Further Reading

Jencks WP (1969) Catalysis in Chemistry and Enzymology. New York: Dover.

Cleland WW (1970) Steady state kinetics. In: Boyer PD (ed.) The Enzymes, 3rd edn, vol. 2, pp. 1–65. New York: Academic Press.

Fersht A (1977) Enzyme Structure and Mechanism. San Francisco: W.H. Freeman.

Walsh CT (1979) Enzymatic Reaction Mechanisms. San Francisco: W.H. Freeman.

Fink AL (1987) Acyl group transfer: The serine proteases. In: Page MI and Williams A (eds) Enzyme Mechanisms, pp. 159–177. London: Royal Society of Chemistry.

Kyte J (1995) Mechanism in Protein Chemistry. New York: Garland.

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Kenyon, George L(Apr 2001) Covalent Nucleophilic Catalysis. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1038/npg.els.0000603]