History of Enzyme Chemistry

Abstract

Enzymes have been recognized as the catalysts necessary for all physiological processes since the end of the nineteenth century. Before then their study was complicated by arguments over vitalism, which only subsided after Buchner showed that a cell‐free extract from yeast could carry out alcoholic fermentation. This led to the flowering of studies of metabolism, and with it a corresponding increase in studies of enzyme catalysis, which were no longer mainly limited to extracellular enzymes such as pepsin. The groundwork for kinetic studies was laid by Henri and by Michaelis and Menten, and understanding of enzyme catalysis was later strengthened when Sumner demonstrated that enzymes could be crystallized. The principal features of three‐dimensional structure became known by the 1950s, by which time hundreds of enzymes had been characterized, making it necessary to create a rational classification of reactions catalysed, the basis of the modern EC system.

Key Concepts:

  • Nearly all physiological processes are catalysed by proteins known as enzymes.

  • A few reactions are catalysed by non‐protein enzymes based on RNA.

  • Enzymes are highly specific, with all apart from degradative enzymes extremely restrictive in the reactions they catalyse.

  • Most enzymes are similar in amino acid sequence to their homologues in other species even between organisms that are phylogenetically very different.

  • Enzyme catalysis was initially studied primarily by kinetic measurements, but is now based also on three‐dimensional structural information derived from crystallography or NMR.

Keywords: enzymes; vitalism; ferments; catalysis; proteins

Figure 1.

Polarimeter of the type used in early studies of invertase.

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References

Anonymous (but known to be Wöhler F and Liebig J) (1839) Das enträthseltre Geheimniss der geistigen Gährung. Annalen der Pharmacie 29: 100–104.

Blake CC, Koenig DF, Mair GA et al. (1967) Structure of hen egg‐white lysozyme. A three‐dimensional Fourier synthesis at 2 Angstrom resolution. Nature 206(986): 757–761.

Buchner E (1897) Alkoholische Gährung ohne Hefezellen. Berichte der Deutschen Chemischen Gesellschaft 30: 117–124.

Kluyver AJ (1926) Über die Nichtexistenz einiger Fermente. Hoppe‐Seyler's Zeitschrift für Physiologische Chemie 158: 111–112.

Knowles JR (1991) Enzyme catalysis: not different, just better. Nature 350(6314): 121–124.

Kühne W (1877) Über das Verhalten verschiedener organisirter und sog. ungeformter Fermente. Verhandlungen des naturhistorisch‐medicinischen Vereins zu Heidelberg. ( Neue Folge) 1: 190–193.

Michaelis L and Menten ML (1913) Kinetik der Invertinwirkung. Biochemisches Zeitschrift 49: 333–369.

Pasteur L (1879) Quatrième réponse à M. Berthelot. Comptes Rendus de l'Académie des Sciences 88: 255–261.

Pauling L, Corey RB and Branson HR (1951) The structure of poteins: two hydrogen‐bonded helical configurations of the polypeptide chain. Proceedings of the National Academy of Sciences 37(4): 205–211.

Snell EE and di Mari SJ (1970) Schiff base intermediates in enzyme catalysis. In: Boyer PD (ed.) The Enzymes, 3rd edn, pp. 335–370. New York: Academic Press.

Further Reading

Friedmann HC (1997) From Friedrich Wöhler's urine to Eduard Buchner's alcohol. In: Cornish‐Bowden A (ed.) New Beer in an Old Bottle. Valencia, Spain: Universitat de València.

Fruton JS (1999) Proteins, Enzymes, Genes: The Interplay of Chemistry and Biology. New Heavan, CN: Yale University Press.

Tanford C and Reynolds J (2001) Nature's Robots: a History of Proteins. Oxford: Oxford University Press.

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How to Cite close
Cornish‐Bowden, Athel(May 2011) History of Enzyme Chemistry. In: eLS. John Wiley & Sons Ltd, Chichester. http://www.els.net [doi: 10.1002/9780470015902.a0003466]