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Large-scale sequencing of genomes has revealed that most enzyme families include inactive homologues. These pseudoenzymes are often well conserved, implying a selective pressure to retain them during evolution, and therefore that they have significant function. Mechanistic insights and evolutionary lessons are now emerging from the study of a broad range of such 'dead' enzymes. The recently discovered iRhoms - inactive homologues of rhomboid proteases - have joined derlins and other members of the rhomboid-like clan in regulating the fate of proteins as they pass through the secretory pathway. There is a strong case that dead enzymes, which have been rather overlooked, may be a rich source of biological regulators.

Original publication




Journal article


Nat Rev Mol Cell Biol

Publication Date





489 - 498


Animals, Carrier Proteins, Catalysis, Drosophila melanogaster, Enzymes, Evolution, Molecular, Genome, Humans, Mice, Phylogeny, Selection, Genetic, Sequence Homology, Amino Acid