Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica
3-Isopropylmalate dehydrogenase (IPMDH) catalyzes oxidative decarboxylation of (2R, 3S)-3-isopropylmalate to 2-oxoisocaproate in leucine biosynthesis. In this study, recombinant IPMDH (HjIPMDH) from an extremely halophilic archaeon, Haloarcula japonica TR-1, was characterized. Activity of HjIPMDH in...
Gespeichert in:
| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2021-08, Vol.85 (9), p.1986-1994 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1994 |
|---|---|
| container_issue | 9 |
| container_start_page | 1986 |
| container_title | Bioscience, biotechnology, and biochemistry |
| container_volume | 85 |
| creator | Nagaoka, Shintaro Sugiyama, Noriko Yatsunami, Rie Nakamura, Satoshi |
| description | 3-Isopropylmalate dehydrogenase (IPMDH) catalyzes oxidative decarboxylation of (2R, 3S)-3-isopropylmalate to 2-oxoisocaproate in leucine biosynthesis. In this study, recombinant IPMDH (HjIPMDH) from an extremely halophilic archaeon, Haloarcula japonica TR-1, was characterized. Activity of HjIPMDH increased as KCl concentration increased, and the maximum activity was observed at 3.0 m KCl. Analytical ultracentrifugation revealed that HjIPMDH formed a homotetramer at high KCl concentrations, and it dissociated to a monomer at low KCl concentrations. Additionally, HjIPMDH was thermally stabilized by higher KCl concentrations. This is the first report on haloarchaeal IPMDH. |
| doi_str_mv | 10.1093/bbb/zbab122 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2548417912</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2548417912</sourcerecordid><originalsourceid>FETCH-LOGICAL-c247t-c8963ed540205f02b88647b6c424be1027678d8e73957bab4eba49efda5e01aa3</originalsourceid><addsrcrecordid>eNpNkM9LwzAYhoMobk5P3qVHQeqSNG3aowx1wsCLnsuX9KvNSJuadGD311vZFE_fDx5eeB9Crhm9Z7RIlkqp5V6BYpyfkDlLhIyzQsjTf_uMXISwpZQWLGXnZJYIztJcyjnZrhrwoAf0Zg-DcV3k6iiJTXC9d_1oW7AwYFRhM1befWAHAaPauzbCr8Fji3aMGrCub4w1OgKvG8ApZT39pmNnIdpC7zqj4ZKc1WADXh3ngrw_Pb6t1vHm9fll9bCJNRdyiHVeZAlWqaCcpjXlKs8zIVWmBRcKGeUyk3mVo0yKVE61BSoQBdYVpEgZQLIgt4fcqcHnDsNQtiZotBY6dLtQ8lTkgsmC8Qm9O6DauxA81mXvTQt-LBktf-SWk9zyKHeib47BO9Vi9cf-2ky-AZvReMM</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2548417912</pqid></control><display><type>article</type><title>Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica</title><source>MEDLINE</source><source>Oxford University Press Journals All Titles (1996-Current)</source><creator>Nagaoka, Shintaro ; Sugiyama, Noriko ; Yatsunami, Rie ; Nakamura, Satoshi</creator><creatorcontrib>Nagaoka, Shintaro ; Sugiyama, Noriko ; Yatsunami, Rie ; Nakamura, Satoshi</creatorcontrib><description>3-Isopropylmalate dehydrogenase (IPMDH) catalyzes oxidative decarboxylation of (2R, 3S)-3-isopropylmalate to 2-oxoisocaproate in leucine biosynthesis. In this study, recombinant IPMDH (HjIPMDH) from an extremely halophilic archaeon, Haloarcula japonica TR-1, was characterized. Activity of HjIPMDH increased as KCl concentration increased, and the maximum activity was observed at 3.0 m KCl. Analytical ultracentrifugation revealed that HjIPMDH formed a homotetramer at high KCl concentrations, and it dissociated to a monomer at low KCl concentrations. Additionally, HjIPMDH was thermally stabilized by higher KCl concentrations. This is the first report on haloarchaeal IPMDH.</description><identifier>ISSN: 1347-6947</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1093/bbb/zbab122</identifier><identifier>PMID: 34215877</identifier><language>eng</language><publisher>England</publisher><subject>3-Isopropylmalate Dehydrogenase - chemistry ; 3-Isopropylmalate Dehydrogenase - metabolism ; Amino Acid Sequence ; Archaeal Proteins - metabolism ; Biopolymers - chemistry ; Genome, Archaeal ; Halobacteriales - enzymology ; Halobacteriales - genetics ; Hydrogen-Ion Concentration ; Potassium Chloride - analysis ; Temperature</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2021-08, Vol.85 (9), p.1986-1994</ispartof><rights>The Author(s) 2021. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c247t-c8963ed540205f02b88647b6c424be1027678d8e73957bab4eba49efda5e01aa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34215877$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nagaoka, Shintaro</creatorcontrib><creatorcontrib>Sugiyama, Noriko</creatorcontrib><creatorcontrib>Yatsunami, Rie</creatorcontrib><creatorcontrib>Nakamura, Satoshi</creatorcontrib><title>Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>3-Isopropylmalate dehydrogenase (IPMDH) catalyzes oxidative decarboxylation of (2R, 3S)-3-isopropylmalate to 2-oxoisocaproate in leucine biosynthesis. In this study, recombinant IPMDH (HjIPMDH) from an extremely halophilic archaeon, Haloarcula japonica TR-1, was characterized. Activity of HjIPMDH increased as KCl concentration increased, and the maximum activity was observed at 3.0 m KCl. Analytical ultracentrifugation revealed that HjIPMDH formed a homotetramer at high KCl concentrations, and it dissociated to a monomer at low KCl concentrations. Additionally, HjIPMDH was thermally stabilized by higher KCl concentrations. This is the first report on haloarchaeal IPMDH.</description><subject>3-Isopropylmalate Dehydrogenase - chemistry</subject><subject>3-Isopropylmalate Dehydrogenase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Archaeal Proteins - metabolism</subject><subject>Biopolymers - chemistry</subject><subject>Genome, Archaeal</subject><subject>Halobacteriales - enzymology</subject><subject>Halobacteriales - genetics</subject><subject>Hydrogen-Ion Concentration</subject><subject>Potassium Chloride - analysis</subject><subject>Temperature</subject><issn>1347-6947</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkM9LwzAYhoMobk5P3qVHQeqSNG3aowx1wsCLnsuX9KvNSJuadGD311vZFE_fDx5eeB9Crhm9Z7RIlkqp5V6BYpyfkDlLhIyzQsjTf_uMXISwpZQWLGXnZJYIztJcyjnZrhrwoAf0Zg-DcV3k6iiJTXC9d_1oW7AwYFRhM1befWAHAaPauzbCr8Fji3aMGrCub4w1OgKvG8ApZT39pmNnIdpC7zqj4ZKc1WADXh3ngrw_Pb6t1vHm9fll9bCJNRdyiHVeZAlWqaCcpjXlKs8zIVWmBRcKGeUyk3mVo0yKVE61BSoQBdYVpEgZQLIgt4fcqcHnDsNQtiZotBY6dLtQ8lTkgsmC8Qm9O6DauxA81mXvTQt-LBktf-SWk9zyKHeib47BO9Vi9cf-2ky-AZvReMM</recordid><startdate>20210825</startdate><enddate>20210825</enddate><creator>Nagaoka, Shintaro</creator><creator>Sugiyama, Noriko</creator><creator>Yatsunami, Rie</creator><creator>Nakamura, Satoshi</creator><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></search><sort><creationdate>20210825</creationdate><title>Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica</title><author>Nagaoka, Shintaro ; Sugiyama, Noriko ; Yatsunami, Rie ; Nakamura, Satoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c247t-c8963ed540205f02b88647b6c424be1027678d8e73957bab4eba49efda5e01aa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>3-Isopropylmalate Dehydrogenase - chemistry</topic><topic>3-Isopropylmalate Dehydrogenase - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Archaeal Proteins - metabolism</topic><topic>Biopolymers - chemistry</topic><topic>Genome, Archaeal</topic><topic>Halobacteriales - enzymology</topic><topic>Halobacteriales - genetics</topic><topic>Hydrogen-Ion Concentration</topic><topic>Potassium Chloride - analysis</topic><topic>Temperature</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagaoka, Shintaro</creatorcontrib><creatorcontrib>Sugiyama, Noriko</creatorcontrib><creatorcontrib>Yatsunami, Rie</creatorcontrib><creatorcontrib>Nakamura, Satoshi</creatorcontrib><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>Nagaoka, Shintaro</au><au>Sugiyama, Noriko</au><au>Yatsunami, Rie</au><au>Nakamura, Satoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2021-08-25</date><risdate>2021</risdate><volume>85</volume><issue>9</issue><spage>1986</spage><epage>1994</epage><pages>1986-1994</pages><issn>1347-6947</issn><eissn>1347-6947</eissn><abstract>3-Isopropylmalate dehydrogenase (IPMDH) catalyzes oxidative decarboxylation of (2R, 3S)-3-isopropylmalate to 2-oxoisocaproate in leucine biosynthesis. In this study, recombinant IPMDH (HjIPMDH) from an extremely halophilic archaeon, Haloarcula japonica TR-1, was characterized. Activity of HjIPMDH increased as KCl concentration increased, and the maximum activity was observed at 3.0 m KCl. Analytical ultracentrifugation revealed that HjIPMDH formed a homotetramer at high KCl concentrations, and it dissociated to a monomer at low KCl concentrations. Additionally, HjIPMDH was thermally stabilized by higher KCl concentrations. This is the first report on haloarchaeal IPMDH.</abstract><cop>England</cop><pmid>34215877</pmid><doi>10.1093/bbb/zbab122</doi><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1347-6947 |
| ispartof | Bioscience, biotechnology, and biochemistry, 2021-08, Vol.85 (9), p.1986-1994 |
| issn | 1347-6947 1347-6947 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_2548417912 |
| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current) |
| subjects | 3-Isopropylmalate Dehydrogenase - chemistry 3-Isopropylmalate Dehydrogenase - metabolism Amino Acid Sequence Archaeal Proteins - metabolism Biopolymers - chemistry Genome, Archaeal Halobacteriales - enzymology Halobacteriales - genetics Hydrogen-Ion Concentration Potassium Chloride - analysis Temperature |
| title | Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-25T11%3A44%3A06IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20of%203-isopropylmalate%20dehydrogenase%20from%20extremely%20halophilic%20archaeon%20Haloarcula%20japonica&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=Nagaoka,%20Shintaro&rft.date=2021-08-25&rft.volume=85&rft.issue=9&rft.spage=1986&rft.epage=1994&rft.pages=1986-1994&rft.issn=1347-6947&rft.eissn=1347-6947&rft_id=info:doi/10.1093/bbb/zbab122&rft_dat=%3Cproquest_cross%3E2548417912%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2548417912&rft_id=info:pmid/34215877&rfr_iscdi=true |