Covalent Nucleophilic Catalysis

George L Kenyon, University of California – San Francisco, San Francisco, California, USA

Published online: April 2001

DOI: 10.1038/npg.els.0000603

Covalent nucleophilic catalysis is the involvement of a nucleophile on an enzyme (usually one of the side-chain groups of an -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 1.
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 Further Reading
    book Jencks WP (1969) Catalysis in Chemistry and Enzymology. New York: Dover.
    book Cleland WW (1970) "Steady state kinetics". In: Boyer PD (ed.) The Enzymes, 3rd edn, vol. 2, pp. 1–65. New York: Academic Press.
    book Fersht A (1977) Enzyme Structure and Mechanism. San Francisco: W.H. Freeman.
    book Walsh CT (1979) Enzymatic Reaction Mechanisms. San Francisco: W.H. Freeman.
    book 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.
    book Kyte J (1995) Mechanism in Protein Chemistry. New York: Garland.

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Enzymes: Structure and Action Mechanism
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Article Title: Covalent Nucleophilic Catalysis
 
How to Cite close
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]