New lives for old: evolution of pseudoenzyme function illustrated by iRhoms.
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...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
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2012
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| _version_ | 1797069395752648704 |
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| author | Adrain, C Freeman, M |
| author_facet | Adrain, C Freeman, M |
| author_sort | Adrain, C |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T22:23:49Z |
| format | Journal article |
| id | oxford-uuid:55f7de29-5a51-4e31-a1c9-efda4d38a07f |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:23:49Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:55f7de29-5a51-4e31-a1c9-efda4d38a07f2022-03-26T16:47:25ZNew lives for old: evolution of pseudoenzyme function illustrated by iRhoms.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:55f7de29-5a51-4e31-a1c9-efda4d38a07fEnglishSymplectic Elements at Oxford2012Adrain, CFreeman, MLarge-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. |
| spellingShingle | Adrain, C Freeman, M New lives for old: evolution of pseudoenzyme function illustrated by iRhoms. |
| title | New lives for old: evolution of pseudoenzyme function illustrated by iRhoms. |
| title_full | New lives for old: evolution of pseudoenzyme function illustrated by iRhoms. |
| title_fullStr | New lives for old: evolution of pseudoenzyme function illustrated by iRhoms. |
| title_full_unstemmed | New lives for old: evolution of pseudoenzyme function illustrated by iRhoms. |
| title_short | New lives for old: evolution of pseudoenzyme function illustrated by iRhoms. |
| title_sort | new lives for old evolution of pseudoenzyme function illustrated by irhoms |
| work_keys_str_mv | AT adrainc newlivesforoldevolutionofpseudoenzymefunctionillustratedbyirhoms AT freemanm newlivesforoldevolutionofpseudoenzymefunctionillustratedbyirhoms |