New lives for old: evolution of pseudoenzyme function illustrated by iRhoms

Colin Adrain, Matthew Freeman

Research output: Contribution to journalReview articlepeer-review

100 Citations (Scopus)

Abstract

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 languageEnglish
Pages (from-to)489-98
Number of pages10
JournalBiochemistry and cell biology = Biochimie et biologie cellulaire
Volume13
Issue number8
DOIs
Publication statusPublished - 11 Jul 2012
Externally publishedYes

Keywords

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

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