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- W2794524398 endingPage "91" @default.
- W2794524398 startingPage "80" @default.
- W2794524398 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." @default.
- W2794524398 created "2018-04-06" @default.
- W2794524398 creator A5007437458 @default.
- W2794524398 creator A5064806696 @default.
- W2794524398 date "2018-08-01" @default.
- W2794524398 modified "2023-10-17" @default.
- W2794524398 title "Membrane properties that shape the evolution of membrane enzymes" @default.
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