Letter | Published:

Chemical Model of a Biological Reaction

Naturevolume 180pages13541355 (1957) | Download Citation

Subjects

Abstract

WE were searching for a model of an enzymatic reaction in the hope that the relatively simple chemistry of the model reaction might throw some light on the enzyme reaction itself. In particular, we were interested in finding a model which would duplicate some of the properties of lipases, notably their ability to catalyse the hydrolysis of lipids and the characteristic pH dependence of lipolytic activity which reaches a maximum near pH 8.5 with most lipases, and one just below pH 7 with some. Lipases being proteins, the model would have to be restricted to the functional groups available in proteins. The high potency of lipases, despite this restriction, together with the well-known chemical mechanism of ester hydrolysis, made us suspect that bifunctional catalysis1 might play a decisive part.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.

from$8.99

All prices are NET prices.

References

  1. 1

    Swain, C. G., et al., J. Amer. Chem. Soc., 70, 1119 (1948); 74, 2534, 2538 (1952).

  2. 2

    Gero, A., J. Org. Chem., 16, 1222 (1951); Science, 119, 112 (1954).

  3. 3

    Alper, C., in Reiner, M., “Standard Methods of Clinical Chemistry”, 1, 71 (Academic Press, New York, 1953).

Download references

Author information

Affiliations

  1. Hahnemann Medical College, Philadelphia, 2, Penn.

    • ALEXANDER GERO
    •  & CURTIS L. WITHROW

Authors

  1. Search for ALEXANDER GERO in:

  2. Search for CURTIS L. WITHROW in:

About this article

Publication history

Issue Date

DOI

https://doi.org/10.1038/1801354a0

Further reading

Comments

By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.