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The Fate of Duplicated Enzymes in Prokaryotes: The Case of Isomerases
The isomerases are a unique enzymatic class of enzymes that carry out a great diversity of chemical reactions at the intramolecular level. This class comprises about 300 members, most of which are involved in carbohydrate and terpenoid/polyketide metabolism. Along with oxidoreductases and translocas...
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Published in: | Journal of molecular evolution 2023-02, Vol.91 (1), p.76-92 |
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description | The isomerases are a unique enzymatic class of enzymes that carry out a great diversity of chemical reactions at the intramolecular level. This class comprises about 300 members, most of which are involved in carbohydrate and terpenoid/polyketide metabolism. Along with oxidoreductases and translocases, isomerases are one of the classes with the highest ratio of paralogous enzymes. Due to its relatively small number of members, it is plausible to explore it in greater detail to identify specific cases of gene duplication. Here, we present an analysis at the level of individual isomerases and identify different members that seem to be involved in duplication events in prokaryotes. As was suggested in a previous study, there is no homogeneous distribution of paralogs, but rather they accumulate into a few subcategories, some of which differ between Archaea and Bacteria. As expected, the metabolic processes with more paralogous isomerases have to do with carbohydrate metabolism but also with RNA modification (a particular case involving an rRNA-modifying isomerase is thoroughly discussed and analyzed in detail). Overall, our findings suggest that the most common fate for paralogous enzymes is the retention of the original enzymatic function, either associated with a dosage effect or with differential expression in response to changing environments, followed by subfunctionalization and, to a much lesser degree, neofunctionalization, which is consistent with what has been reported elsewhere. |
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This class comprises about 300 members, most of which are involved in carbohydrate and terpenoid/polyketide metabolism. Along with oxidoreductases and translocases, isomerases are one of the classes with the highest ratio of paralogous enzymes. Due to its relatively small number of members, it is plausible to explore it in greater detail to identify specific cases of gene duplication. Here, we present an analysis at the level of individual isomerases and identify different members that seem to be involved in duplication events in prokaryotes. As was suggested in a previous study, there is no homogeneous distribution of paralogs, but rather they accumulate into a few subcategories, some of which differ between Archaea and Bacteria. As expected, the metabolic processes with more paralogous isomerases have to do with carbohydrate metabolism but also with RNA modification (a particular case involving an rRNA-modifying isomerase is thoroughly discussed and analyzed in detail). 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genetics</topic><topic>Bacteria - genetics</topic><topic>Biomedical and Life Sciences</topic><topic>Carbohydrate metabolism</topic><topic>Carbohydrates</topic><topic>Cell Biology</topic><topic>Changing environments</topic><topic>Chemical reactions</topic><topic>Environmental changes</topic><topic>Enzymes</topic><topic>Evolution, Molecular</topic><topic>Evolutionary Biology</topic><topic>Gene Duplication</topic><topic>Isomerases - genetics</topic><topic>Life Sciences</topic><topic>Metabolism</topic><topic>Microbiology</topic><topic>Original Article</topic><topic>Plant Genetics and Genomics</topic><topic>Plant Sciences</topic><topic>Prokaryotes</topic><topic>Reproduction (copying)</topic><topic>RNA modification</topic><topic>rRNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Álvarez-Lugo, Alejandro</creatorcontrib><creatorcontrib>Becerra, Arturo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular evolution</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Álvarez-Lugo, Alejandro</au><au>Becerra, Arturo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Fate of Duplicated Enzymes in Prokaryotes: The Case of Isomerases</atitle><jtitle>Journal of molecular evolution</jtitle><stitle>J Mol Evol</stitle><addtitle>J Mol Evol</addtitle><date>2023-02-01</date><risdate>2023</risdate><volume>91</volume><issue>1</issue><spage>76</spage><epage>92</epage><pages>76-92</pages><issn>0022-2844</issn><eissn>1432-1432</eissn><abstract>The isomerases are a unique enzymatic class of enzymes that carry out a great diversity of chemical reactions at the intramolecular level. 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Overall, our findings suggest that the most common fate for paralogous enzymes is the retention of the original enzymatic function, either associated with a dosage effect or with differential expression in response to changing environments, followed by subfunctionalization and, to a much lesser degree, neofunctionalization, which is consistent with what has been reported elsewhere.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>36580111</pmid><doi>10.1007/s00239-022-10085-x</doi><tpages>17</tpages><orcidid>https://orcid.org/0000-0002-7076-0342</orcidid></addata></record> |
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subjects | Animal Genetics and Genomics Archaea Archaea - genetics Bacteria - genetics Biomedical and Life Sciences Carbohydrate metabolism Carbohydrates Cell Biology Changing environments Chemical reactions Environmental changes Enzymes Evolution, Molecular Evolutionary Biology Gene Duplication Isomerases - genetics Life Sciences Metabolism Microbiology Original Article Plant Genetics and Genomics Plant Sciences Prokaryotes Reproduction (copying) RNA modification rRNA |
title | The Fate of Duplicated Enzymes in Prokaryotes: The Case of Isomerases |
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