Primordial-like enzymes from bacteria with reduced genomes
The first cells probably possessed rudimentary metabolic networks, built using a handful of multifunctional enzymes. The promiscuous activities of modern enzymes are often assumed to be relics of this primordial era; however, by definition these activities are no longer physiological. There are many...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Wiley
2017
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| _version_ | 1797083788373655552 |
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| author | Ferla, MP Brewster, JL Hall, KR Evans, GB Patrick, WM |
| author_facet | Ferla, MP Brewster, JL Hall, KR Evans, GB Patrick, WM |
| author_sort | Ferla, MP |
| collection | OXFORD |
| description | The first cells probably possessed rudimentary metabolic networks, built using a handful of multifunctional enzymes. The promiscuous activities of modern enzymes are often assumed to be relics of this primordial era; however, by definition these activities are no longer physiological. There are many fewer examples of enzymes using a single active site to catalyze multiple physiologically-relevant reactions. Previously, we characterized the promiscuous alanine racemase (ALR) activity of Escherichia coli cystathionine β-lyase (CBL). Now we have discovered that several bacteria with reduced genomes lack alr, but contain metC (encoding CBL). We characterized the CBL enzymes from three of these: Pelagibacter ubique, the Wolbachia endosymbiont of Drosophila melanogaster (wMel) and Thermotoga maritima. Each is a multifunctional CBL/ALR. However, we also show that CBL activity is no longer required in these bacteria. Instead, the wMel and T. maritima enzymes are physiologically bi-functional alanine/glutamate racemases. They are not highly active, but they are clearly sufficient. Given the abundance of the microorganisms using them, we suggest that much of the planet's biochemistry is carried out by enzymes that are quite different from the highly-active exemplars usually found in textbooks. Instead, primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. |
| first_indexed | 2024-03-07T01:46:23Z |
| format | Journal article |
| id | oxford-uuid:98903c1a-ff2d-4ba0-bfba-293ce820ef76 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T01:46:23Z |
| publishDate | 2017 |
| publisher | Wiley |
| record_format | dspace |
| spelling | oxford-uuid:98903c1a-ff2d-4ba0-bfba-293ce820ef762022-03-27T00:07:55ZPrimordial-like enzymes from bacteria with reduced genomesJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:98903c1a-ff2d-4ba0-bfba-293ce820ef76EnglishSymplectic Elements at OxfordWiley2017Ferla, MPBrewster, JLHall, KREvans, GBPatrick, WMThe first cells probably possessed rudimentary metabolic networks, built using a handful of multifunctional enzymes. The promiscuous activities of modern enzymes are often assumed to be relics of this primordial era; however, by definition these activities are no longer physiological. There are many fewer examples of enzymes using a single active site to catalyze multiple physiologically-relevant reactions. Previously, we characterized the promiscuous alanine racemase (ALR) activity of Escherichia coli cystathionine β-lyase (CBL). Now we have discovered that several bacteria with reduced genomes lack alr, but contain metC (encoding CBL). We characterized the CBL enzymes from three of these: Pelagibacter ubique, the Wolbachia endosymbiont of Drosophila melanogaster (wMel) and Thermotoga maritima. Each is a multifunctional CBL/ALR. However, we also show that CBL activity is no longer required in these bacteria. Instead, the wMel and T. maritima enzymes are physiologically bi-functional alanine/glutamate racemases. They are not highly active, but they are clearly sufficient. Given the abundance of the microorganisms using them, we suggest that much of the planet's biochemistry is carried out by enzymes that are quite different from the highly-active exemplars usually found in textbooks. Instead, primordial-like enzymes may be an essential part of the adaptive strategy associated with streamlining. |
| spellingShingle | Ferla, MP Brewster, JL Hall, KR Evans, GB Patrick, WM Primordial-like enzymes from bacteria with reduced genomes |
| title | Primordial-like enzymes from bacteria with reduced genomes |
| title_full | Primordial-like enzymes from bacteria with reduced genomes |
| title_fullStr | Primordial-like enzymes from bacteria with reduced genomes |
| title_full_unstemmed | Primordial-like enzymes from bacteria with reduced genomes |
| title_short | Primordial-like enzymes from bacteria with reduced genomes |
| title_sort | primordial like enzymes from bacteria with reduced genomes |
| work_keys_str_mv | AT ferlamp primordiallikeenzymesfrombacteriawithreducedgenomes AT brewsterjl primordiallikeenzymesfrombacteriawithreducedgenomes AT hallkr primordiallikeenzymesfrombacteriawithreducedgenomes AT evansgb primordiallikeenzymesfrombacteriawithreducedgenomes AT patrickwm primordiallikeenzymesfrombacteriawithreducedgenomes |