Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 11 July 2008:
Vol. 321. no. 5886, pp. 213 - 216
DOI: 10.1126/science.1151118
Prev | Table of Contents | Next

Review

Enzymes Without Borders: Mobilizing Substrates, Delivering Products

Federico Forneris and Andrea Mattevi*

Many cellular reactions involve both hydrophobic and hydrophilic molecules that reside within the chemically distinct environments defined by the phospholipid-based membranes and the aqueous lumens of cytoplasm and organelles. Enzymes performing this type of reaction are required to access a lipophilic substrate located in the membranes and to catalyze its reaction with a polar, water-soluble compound. Here, we explore the different binding strategies and chemical tricks that enzymes have developed to overcome this problem. These reactions can be catalyzed by integral membrane proteins that channel a hydrophilic molecule into their active site, as well as by water-soluble enzymes that are able to capture a lipophilic substrate from the phospholipid bilayer. Many chemical and biological aspects of this type of enzymology remain to be investigated and will require the integration of protein chemistry with membrane biology.

Department of Genetics and Microbiology, University of Pavia, Via Ferrata 1, 27100 Pavia, Italy.

* To whom correspondence should be addressed. E-mail: mattevi{at}ipvgen.unipv.it

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
From the Cover: Crystal structure of native RPE65, the retinoid isomerase of the visual cycle.
P. D. Kiser, M. Golczak, D. T. Lodowski, M. R. Chance, and K. Palczewski (2009)
PNAS 106, 17325-17330
   Abstract »    Full Text »    PDF »
The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration.
M. Marcia, U. Ermler, G. Peng, and H. Michel (2009)
PNAS 106, 9625-9630
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)