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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

DOI

10.1038/nrm3392

Type

Journal article

Journal

Nat Rev Mol Cell Biol

Publication Date

11/07/2012

Volume

13

Pages

489 - 498

Keywords

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