Characterization of a novel L-fuconate dehydratase involved in the non-phosphorylated pathway of L-fucose metabolism from bacteria
ABSTRACT A sugar acid dehydratase from Paraburkholderia mimosarum, potentially involved in the non-phosphorylated L-fucose pathway, was functionally characterized. A biochemical analysis revealed its unique heterodimeric structure and higher specificity toward L-fuconate than D-arabinonate, D-altron...
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Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2024-01, Vol.88 (2), p.177-180 |
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description | ABSTRACT
A sugar acid dehydratase from Paraburkholderia mimosarum, potentially involved in the non-phosphorylated L-fucose pathway, was functionally characterized. A biochemical analysis revealed its unique heterodimeric structure and higher specificity toward L-fuconate than D-arabinonate, D-altronate, and L-xylonate, which differed from homomeric homologs. This unique L-fuconate dehydratase has a poor phylogenetic relationship with other functional members of the D-altronate dehydratase/galactarate dehydratase protein family. |
doi_str_mv | 10.1093/bbb/zbad161 |
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A sugar acid dehydratase from Paraburkholderia mimosarum, potentially involved in the non-phosphorylated L-fucose pathway, was functionally characterized. A biochemical analysis revealed its unique heterodimeric structure and higher specificity toward L-fuconate than D-arabinonate, D-altronate, and L-xylonate, which differed from homomeric homologs. This unique L-fuconate dehydratase has a poor phylogenetic relationship with other functional members of the D-altronate dehydratase/galactarate dehydratase protein family.</description><identifier>ISSN: 1347-6947</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1093/bbb/zbad161</identifier><identifier>PMID: 38017627</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Bacteria - metabolism ; Fucose - metabolism ; Hydro-Lyases - genetics ; Phylogeny</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2024-01, Vol.88 (2), p.177-180</ispartof><rights>The Author(s) 2023. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry. 2023</rights><rights>The Author(s) 2023. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c315t-48e714161a7ea10f6ee75792f1b6f5f0136e036940b8fe0776ddb01a7269d3d3</cites><orcidid>0000-0002-6530-9047</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1584,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38017627$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Watanabe, Seiya</creatorcontrib><title>Characterization of a novel L-fuconate dehydratase involved in the non-phosphorylated pathway of L-fucose metabolism from bacteria</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>ABSTRACT
A sugar acid dehydratase from Paraburkholderia mimosarum, potentially involved in the non-phosphorylated L-fucose pathway, was functionally characterized. A biochemical analysis revealed its unique heterodimeric structure and higher specificity toward L-fuconate than D-arabinonate, D-altronate, and L-xylonate, which differed from homomeric homologs. This unique L-fuconate dehydratase has a poor phylogenetic relationship with other functional members of the D-altronate dehydratase/galactarate dehydratase protein family.</description><subject>Bacteria - metabolism</subject><subject>Fucose - metabolism</subject><subject>Hydro-Lyases - genetics</subject><subject>Phylogeny</subject><issn>1347-6947</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>TOX</sourceid><sourceid>EIF</sourceid><recordid>eNp9kMtLxDAQh4Movk_eJScRpJr0kWyPsviCBS_ey6SZ0Erb1CRdWY_-5Ua6iicPw8zhm2-YHyFnnF1zVmY3SqmbDwWaC75DDnmWy0SUudz9Mx-QI-9fGWMlL_g-OcgWjEuRykPyuWzAQR3QtR8QWjtQayjQwa6xo6vETLUdICDV2Gy0gwAeaTusbbdGHQcaGozwkIyN9bHcpou0piOE5h0237JZEtd6DKBs1_qeGmd7quazcEL2DHQeT7f9mLzc370sH5PV88PT8naV1BkvQpIvUPI8PgkSgTMjEGUhy9RwJUxhGM8Esix-y9TCIJNSaK1YpFNR6kxnx-Ry1o7Ovk3oQ9W3vsaugwHt5Kt0URap4HkuI3o1o7Wz3js01ejaHtym4qz6zryKmVfbzCN9vhVPqkf9y_6EHIGLGbDT-K_pCwzijPo</recordid><startdate>20240124</startdate><enddate>20240124</enddate><creator>Watanabe, Seiya</creator><general>Oxford University Press</general><scope>TOX</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-6530-9047</orcidid></search><sort><creationdate>20240124</creationdate><title>Characterization of a novel L-fuconate dehydratase involved in the non-phosphorylated pathway of L-fucose metabolism from bacteria</title><author>Watanabe, Seiya</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c315t-48e714161a7ea10f6ee75792f1b6f5f0136e036940b8fe0776ddb01a7269d3d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Bacteria - metabolism</topic><topic>Fucose - metabolism</topic><topic>Hydro-Lyases - genetics</topic><topic>Phylogeny</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Watanabe, Seiya</creatorcontrib><collection>Access via Oxford University Press (Open Access Collection)</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watanabe, Seiya</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a novel L-fuconate dehydratase involved in the non-phosphorylated pathway of L-fucose metabolism from bacteria</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2024-01-24</date><risdate>2024</risdate><volume>88</volume><issue>2</issue><spage>177</spage><epage>180</epage><pages>177-180</pages><issn>1347-6947</issn><eissn>1347-6947</eissn><abstract>ABSTRACT
A sugar acid dehydratase from Paraburkholderia mimosarum, potentially involved in the non-phosphorylated L-fucose pathway, was functionally characterized. A biochemical analysis revealed its unique heterodimeric structure and higher specificity toward L-fuconate than D-arabinonate, D-altronate, and L-xylonate, which differed from homomeric homologs. This unique L-fuconate dehydratase has a poor phylogenetic relationship with other functional members of the D-altronate dehydratase/galactarate dehydratase protein family.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>38017627</pmid><doi>10.1093/bbb/zbad161</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-6530-9047</orcidid><oa>free_for_read</oa></addata></record> |
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subjects | Bacteria - metabolism Fucose - metabolism Hydro-Lyases - genetics Phylogeny |
title | Characterization of a novel L-fuconate dehydratase involved in the non-phosphorylated pathway of L-fucose metabolism from bacteria |
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