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Curr Opin Struct Biol. 2018 Aug;51:80-91. doi: 10.1016/j.sbi.2018.03.013. Epub 2018 Mar 27.

Membrane properties that shape the evolution of membrane enzymes.

Author information

1
Center for Structural Biology and Department of Biochemistry, Vanderbilt University, Nashville, TN, USA. Electronic address: chuck.sanders@vanderbilt.edu.
2
Center for Structural Biology and Department of Biochemistry, Vanderbilt University, Nashville, TN, USA.

Abstract

Spectacular recent progress in structural biology has led to determination of the structures of many integral membrane enzymes that catalyze reactions in which at least one substrate also is membrane bound. A pattern of results seems to be emerging in which the active site chemistry of these enzymes is usually found to be analogous to what is observed for water soluble enzymes catalyzing the same reaction types. However, in light of the chemical, structural, and physical complexity of cellular membranes plus the presence of transmembrane gradients and potentials, these enzymes may be subject to membrane-specific regulatory mechanisms that are only now beginning to be uncovered. We review the membrane-specific environmental traits that shape the evolution of membrane-embedded biocatalysts.

PMID:
29597094
PMCID:
PMC6158105
[Available on 2019-08-01]
DOI:
10.1016/j.sbi.2018.03.013

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