Structural basis for catalysis at the membrane-water interface

Meagan Belcher Dufrisne, Vasileios I. Petrou, Oliver B. Clarke, Filippo Mancia

Research output: Contribution to journalReview articlepeer-review

4 Scopus citations

Abstract

The membrane-water interface forms a uniquely heterogeneous and geometrically constrained environment for enzymatic catalysis. Integral membrane enzymes sample three environments – the uniformly hydrophobic interior of the membrane, the aqueous extramembrane region, and the fuzzy, amphipathic interfacial region formed by the tightly packed headgroups of the components of the lipid bilayer. Depending on the nature of the substrates and the location of the site of chemical modification, catalysis may occur in each of these environments. The availability of structural information for alpha-helical enzyme families from each of these classes, as well as several beta-barrel enzymes from the bacterial outer membrane, has allowed us to review here the different ways in which each enzyme fold has adapted to the nature of the substrates, products, and the unique environment of the membrane. Our focus here is on enzymes that process lipidic substrates. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.

Original languageEnglish (US)
Pages (from-to)1368-1385
Number of pages18
JournalBiochimica et Biophysica Acta - Molecular and Cell Biology of Lipids
Volume1862
Issue number11
DOIs
StatePublished - Nov 2017
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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