Characterization and mutagenesis of two novel iron–sulphur cluster pentonate dehydratases
We describe here the identification and characterization of two novel enzymes belonging to the IlvD/EDD protein family, the D-xylonate dehydratase from Caulobacter crescentus , Cc XyDHT, (EC 4.2.1.82), and the L-arabonate dehydratase from Rhizobium leguminosarum bv . trifolii , Rl ArDHT (EC 4.2.1.25...
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creator | Andberg, Martina Aro-Kärkkäinen, Niina Carlson, Paul Oja, Merja Bozonnet, Sophie Toivari, Mervi Hakulinen, Nina O’Donohue, Michael Penttilä, Merja Koivula, Anu |
description | We describe here the identification and characterization of two novel enzymes belonging to the IlvD/EDD protein family, the D-xylonate dehydratase from
Caulobacter crescentus
,
Cc
XyDHT, (EC 4.2.1.82), and the L-arabonate dehydratase from
Rhizobium leguminosarum
bv
. trifolii
,
Rl
ArDHT (EC 4.2.1.25), that produce the corresponding 2-keto-3-deoxy-sugar acids. There is only a very limited amount of characterization data available on pentonate dehydratases, even though the enzymes from these oxidative pathways have potential applications with plant biomass pentose sugars. The two bacterial enzymes share 41 % amino acid sequence identity and were expressed and purified from
Escherichia coli
as homotetrameric proteins. Both dehydratases were shown to accept pentonate and hexonate sugar acids as their substrates and require Mg
2+
for their activity.
Cc
XyDHT displayed the highest activity on D-xylonate and D-gluconate, while
Rl
ArDHT functioned best on D-fuconate, L-arabonate and D-galactonate. The configuration of the OH groups at C2 and C3 position of the sugar acid were shown to be critical, and the C4 configuration also contributed substantially to the substrate recognition. The two enzymes were also shown to contain an iron–sulphur [Fe–S] cluster. Our phylogenetic analysis and mutagenesis studies demonstrated that the three conserved cysteine residues in the aldonic acid dehydratase group of IlvD/EDD family members, those of C60, C128 and C201 in
Cc
XyDHT, and of C59, C127 and C200 in
Rl
ArDHT, are needed for coordination of the [Fe–S] cluster. The iron–sulphur cluster was shown to be crucial for the catalytic activity (k
cat
) but not for the substrate binding (K
m
) of the two pentonate dehydratases. |
doi_str_mv | 10.1007/s00253-016-7530-8 |
format | Article |
fullrecord | <record><control><sourceid>gale_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_01886409v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A470454181</galeid><sourcerecordid>A470454181</sourcerecordid><originalsourceid>FETCH-LOGICAL-c717t-e7d467f58051639f300f70c9f11f3c4f2dfd5ec5418939e3c3295c36c1aaf6c3</originalsourceid><addsrcrecordid>eNp1ksFu1DAQhiMEokvhAbigSFzoIWUmTuzkuFpRWmklJOiNg2Wc8W6qrL3YTqE98Q68IU-Co5TCIpAPlma-f-x_9GfZc4RTBBCvA0BZswKQF6JmUDQPsgVWrCyAY_UwWwCKOnXa5ih7EsIVAJYN54-zo1IglFjyRfZxtVVe6Ui-v1WxdzZXtst3Y1QbshT6kDuTxy8ut-6ahrz3zv749j2Mw347-lwPY0jSfE82Oqsi5R1tbzqvogoUnmaPjBoCPbu7j7PLszeXq_Ni_e7txWq5LrRAEQsSXcWFqRuokbPWMAAjQLcG0TBdmbIzXU26rrBpWUtMs7KtNeMalTJcs-PsZB67VYPc-36n_I10qpfny7WcaoBNwytorzGxr2Z2793nkUKUuz5oGgZlyY1BYoO1AMZ5ndCXf6FXbvQ2GZko4Iyxqv1NbdRAsrfGxbTOaahcVgKq6dfTs6f_oNLpaNdrZ8n0qX4gODkQJCbS17hRYwjy4sP7QxZnVnsXgidzvwQEOeVEzjlJe-ByyolskubFnbnx0466e8WvYCSgnIGQWnZD_g_3_536E64IxhU</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1810633349</pqid></control><display><type>article</type><title>Characterization and mutagenesis of two novel iron–sulphur cluster pentonate dehydratases</title><source>MEDLINE</source><source>SpringerLink Journals - AutoHoldings</source><creator>Andberg, Martina ; Aro-Kärkkäinen, Niina ; Carlson, Paul ; Oja, Merja ; Bozonnet, Sophie ; Toivari, Mervi ; Hakulinen, Nina ; O’Donohue, Michael ; Penttilä, Merja ; Koivula, Anu</creator><creatorcontrib>Andberg, Martina ; Aro-Kärkkäinen, Niina ; Carlson, Paul ; Oja, Merja ; Bozonnet, Sophie ; Toivari, Mervi ; Hakulinen, Nina ; O’Donohue, Michael ; Penttilä, Merja ; Koivula, Anu</creatorcontrib><description>We describe here the identification and characterization of two novel enzymes belonging to the IlvD/EDD protein family, the D-xylonate dehydratase from
Caulobacter crescentus
,
Cc
XyDHT, (EC 4.2.1.82), and the L-arabonate dehydratase from
Rhizobium leguminosarum
bv
. trifolii
,
Rl
ArDHT (EC 4.2.1.25), that produce the corresponding 2-keto-3-deoxy-sugar acids. There is only a very limited amount of characterization data available on pentonate dehydratases, even though the enzymes from these oxidative pathways have potential applications with plant biomass pentose sugars. The two bacterial enzymes share 41 % amino acid sequence identity and were expressed and purified from
Escherichia coli
as homotetrameric proteins. Both dehydratases were shown to accept pentonate and hexonate sugar acids as their substrates and require Mg
2+
for their activity.
Cc
XyDHT displayed the highest activity on D-xylonate and D-gluconate, while
Rl
ArDHT functioned best on D-fuconate, L-arabonate and D-galactonate. The configuration of the OH groups at C2 and C3 position of the sugar acid were shown to be critical, and the C4 configuration also contributed substantially to the substrate recognition. The two enzymes were also shown to contain an iron–sulphur [Fe–S] cluster. Our phylogenetic analysis and mutagenesis studies demonstrated that the three conserved cysteine residues in the aldonic acid dehydratase group of IlvD/EDD family members, those of C60, C128 and C201 in
Cc
XyDHT, and of C59, C127 and C200 in
Rl
ArDHT, are needed for coordination of the [Fe–S] cluster. The iron–sulphur cluster was shown to be crucial for the catalytic activity (k
cat
) but not for the substrate binding (K
m
) of the two pentonate dehydratases.</description><identifier>ISSN: 0175-7598</identifier><identifier>EISSN: 1432-0614</identifier><identifier>DOI: 10.1007/s00253-016-7530-8</identifier><identifier>PMID: 27102126</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Amino Acid Sequence ; Amino acids ; Arabinose - metabolism ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biomedical and Life Sciences ; Biotechnologically Relevant Enzymes and Proteins ; Biotechnology ; Caulobacter ; Caulobacter crescentus ; Caulobacter crescentus - enzymology ; Cloning ; Cloning, Molecular ; Dehydrogenases ; E coli ; Enzymes ; Escherichia coli ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Genes ; Gluconates - metabolism ; Health aspects ; Hydrates ; Hydro-Lyases - genetics ; Hydro-Lyases - metabolism ; Iron ; Life Sciences ; Microbial Genetics and Genomics ; Microbiology ; Mutagenesis ; Observations ; Phylogenetics ; Plant biomass ; Proteins ; Rhizobium leguminosarum ; Rhizobium leguminosarum - enzymology ; Sequence Alignment ; Studies ; Sugar ; Sulfur ; Xylose - metabolism</subject><ispartof>Applied microbiology and biotechnology, 2016-09, Vol.100 (17), p.7549-7563</ispartof><rights>Springer-Verlag Berlin Heidelberg 2016</rights><rights>COPYRIGHT 2016 Springer</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c717t-e7d467f58051639f300f70c9f11f3c4f2dfd5ec5418939e3c3295c36c1aaf6c3</citedby><cites>FETCH-LOGICAL-c717t-e7d467f58051639f300f70c9f11f3c4f2dfd5ec5418939e3c3295c36c1aaf6c3</cites><orcidid>0000-0003-4246-3938</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00253-016-7530-8$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00253-016-7530-8$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,780,784,885,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27102126$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01886409$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Andberg, Martina</creatorcontrib><creatorcontrib>Aro-Kärkkäinen, Niina</creatorcontrib><creatorcontrib>Carlson, Paul</creatorcontrib><creatorcontrib>Oja, Merja</creatorcontrib><creatorcontrib>Bozonnet, Sophie</creatorcontrib><creatorcontrib>Toivari, Mervi</creatorcontrib><creatorcontrib>Hakulinen, Nina</creatorcontrib><creatorcontrib>O’Donohue, Michael</creatorcontrib><creatorcontrib>Penttilä, Merja</creatorcontrib><creatorcontrib>Koivula, Anu</creatorcontrib><title>Characterization and mutagenesis of two novel iron–sulphur cluster pentonate dehydratases</title><title>Applied microbiology and biotechnology</title><addtitle>Appl Microbiol Biotechnol</addtitle><addtitle>Appl Microbiol Biotechnol</addtitle><description>We describe here the identification and characterization of two novel enzymes belonging to the IlvD/EDD protein family, the D-xylonate dehydratase from
Caulobacter crescentus
,
Cc
XyDHT, (EC 4.2.1.82), and the L-arabonate dehydratase from
Rhizobium leguminosarum
bv
. trifolii
,
Rl
ArDHT (EC 4.2.1.25), that produce the corresponding 2-keto-3-deoxy-sugar acids. There is only a very limited amount of characterization data available on pentonate dehydratases, even though the enzymes from these oxidative pathways have potential applications with plant biomass pentose sugars. The two bacterial enzymes share 41 % amino acid sequence identity and were expressed and purified from
Escherichia coli
as homotetrameric proteins. Both dehydratases were shown to accept pentonate and hexonate sugar acids as their substrates and require Mg
2+
for their activity.
Cc
XyDHT displayed the highest activity on D-xylonate and D-gluconate, while
Rl
ArDHT functioned best on D-fuconate, L-arabonate and D-galactonate. The configuration of the OH groups at C2 and C3 position of the sugar acid were shown to be critical, and the C4 configuration also contributed substantially to the substrate recognition. The two enzymes were also shown to contain an iron–sulphur [Fe–S] cluster. Our phylogenetic analysis and mutagenesis studies demonstrated that the three conserved cysteine residues in the aldonic acid dehydratase group of IlvD/EDD family members, those of C60, C128 and C201 in
Cc
XyDHT, and of C59, C127 and C200 in
Rl
ArDHT, are needed for coordination of the [Fe–S] cluster. The iron–sulphur cluster was shown to be crucial for the catalytic activity (k
cat
) but not for the substrate binding (K
m
) of the two pentonate dehydratases.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Arabinose - metabolism</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnologically Relevant Enzymes and Proteins</subject><subject>Biotechnology</subject><subject>Caulobacter</subject><subject>Caulobacter crescentus</subject><subject>Caulobacter crescentus - enzymology</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Dehydrogenases</subject><subject>E coli</subject><subject>Enzymes</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Genes</subject><subject>Gluconates - metabolism</subject><subject>Health aspects</subject><subject>Hydrates</subject><subject>Hydro-Lyases - genetics</subject><subject>Hydro-Lyases - metabolism</subject><subject>Iron</subject><subject>Life Sciences</subject><subject>Microbial Genetics and Genomics</subject><subject>Microbiology</subject><subject>Mutagenesis</subject><subject>Observations</subject><subject>Phylogenetics</subject><subject>Plant biomass</subject><subject>Proteins</subject><subject>Rhizobium leguminosarum</subject><subject>Rhizobium leguminosarum - enzymology</subject><subject>Sequence Alignment</subject><subject>Studies</subject><subject>Sugar</subject><subject>Sulfur</subject><subject>Xylose - metabolism</subject><issn>0175-7598</issn><issn>1432-0614</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1ksFu1DAQhiMEokvhAbigSFzoIWUmTuzkuFpRWmklJOiNg2Wc8W6qrL3YTqE98Q68IU-Co5TCIpAPlma-f-x_9GfZc4RTBBCvA0BZswKQF6JmUDQPsgVWrCyAY_UwWwCKOnXa5ih7EsIVAJYN54-zo1IglFjyRfZxtVVe6Ui-v1WxdzZXtst3Y1QbshT6kDuTxy8ut-6ahrz3zv749j2Mw347-lwPY0jSfE82Oqsi5R1tbzqvogoUnmaPjBoCPbu7j7PLszeXq_Ni_e7txWq5LrRAEQsSXcWFqRuokbPWMAAjQLcG0TBdmbIzXU26rrBpWUtMs7KtNeMalTJcs-PsZB67VYPc-36n_I10qpfny7WcaoBNwytorzGxr2Z2793nkUKUuz5oGgZlyY1BYoO1AMZ5ndCXf6FXbvQ2GZko4Iyxqv1NbdRAsrfGxbTOaahcVgKq6dfTs6f_oNLpaNdrZ8n0qX4gODkQJCbS17hRYwjy4sP7QxZnVnsXgidzvwQEOeVEzjlJe-ByyolskubFnbnx0466e8WvYCSgnIGQWnZD_g_3_536E64IxhU</recordid><startdate>20160901</startdate><enddate>20160901</enddate><creator>Andberg, Martina</creator><creator>Aro-Kärkkäinen, Niina</creator><creator>Carlson, Paul</creator><creator>Oja, Merja</creator><creator>Bozonnet, Sophie</creator><creator>Toivari, Mervi</creator><creator>Hakulinen, Nina</creator><creator>O’Donohue, Michael</creator><creator>Penttilä, Merja</creator><creator>Koivula, Anu</creator><general>Springer Berlin Heidelberg</general><general>Springer</general><general>Springer Nature B.V</general><general>Springer 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and mutagenesis of two novel iron–sulphur cluster pentonate dehydratases</title><author>Andberg, Martina ; Aro-Kärkkäinen, Niina ; Carlson, Paul ; Oja, Merja ; Bozonnet, Sophie ; Toivari, Mervi ; Hakulinen, Nina ; O’Donohue, Michael ; Penttilä, Merja ; Koivula, Anu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c717t-e7d467f58051639f300f70c9f11f3c4f2dfd5ec5418939e3c3295c36c1aaf6c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Arabinose - metabolism</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnologically Relevant Enzymes and Proteins</topic><topic>Biotechnology</topic><topic>Caulobacter</topic><topic>Caulobacter crescentus</topic><topic>Caulobacter crescentus - enzymology</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>Dehydrogenases</topic><topic>E coli</topic><topic>Enzymes</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Genes</topic><topic>Gluconates - metabolism</topic><topic>Health aspects</topic><topic>Hydrates</topic><topic>Hydro-Lyases - genetics</topic><topic>Hydro-Lyases - metabolism</topic><topic>Iron</topic><topic>Life Sciences</topic><topic>Microbial Genetics and Genomics</topic><topic>Microbiology</topic><topic>Mutagenesis</topic><topic>Observations</topic><topic>Phylogenetics</topic><topic>Plant biomass</topic><topic>Proteins</topic><topic>Rhizobium leguminosarum</topic><topic>Rhizobium leguminosarum - enzymology</topic><topic>Sequence Alignment</topic><topic>Studies</topic><topic>Sugar</topic><topic>Sulfur</topic><topic>Xylose - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Andberg, Martina</creatorcontrib><creatorcontrib>Aro-Kärkkäinen, Niina</creatorcontrib><creatorcontrib>Carlson, Paul</creatorcontrib><creatorcontrib>Oja, Merja</creatorcontrib><creatorcontrib>Bozonnet, Sophie</creatorcontrib><creatorcontrib>Toivari, Mervi</creatorcontrib><creatorcontrib>Hakulinen, Nina</creatorcontrib><creatorcontrib>O’Donohue, Michael</creatorcontrib><creatorcontrib>Penttilä, Merja</creatorcontrib><creatorcontrib>Koivula, Anu</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied 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Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Business Premium Collection</collection><collection>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>Business Premium Collection (Alumni)</collection><collection>Health Research Premium Collection</collection><collection>ABI/INFORM Global (Corporate)</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Business Collection (Alumni Edition)</collection><collection>ProQuest Business Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ABI/INFORM Professional Advanced</collection><collection>ProQuest Biological Science Collection</collection><collection>ABI/INFORM Global</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Business</collection><collection>ProQuest One Business (Alumni)</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>Biotechnology Research Abstracts</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Applied microbiology and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Andberg, Martina</au><au>Aro-Kärkkäinen, Niina</au><au>Carlson, Paul</au><au>Oja, Merja</au><au>Bozonnet, Sophie</au><au>Toivari, Mervi</au><au>Hakulinen, Nina</au><au>O’Donohue, Michael</au><au>Penttilä, Merja</au><au>Koivula, Anu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and mutagenesis of two novel iron–sulphur cluster pentonate dehydratases</atitle><jtitle>Applied microbiology and biotechnology</jtitle><stitle>Appl Microbiol Biotechnol</stitle><addtitle>Appl Microbiol Biotechnol</addtitle><date>2016-09-01</date><risdate>2016</risdate><volume>100</volume><issue>17</issue><spage>7549</spage><epage>7563</epage><pages>7549-7563</pages><issn>0175-7598</issn><eissn>1432-0614</eissn><abstract>We describe here the identification and characterization of two novel enzymes belonging to the IlvD/EDD protein family, the D-xylonate dehydratase from
Caulobacter crescentus
,
Cc
XyDHT, (EC 4.2.1.82), and the L-arabonate dehydratase from
Rhizobium leguminosarum
bv
. trifolii
,
Rl
ArDHT (EC 4.2.1.25), that produce the corresponding 2-keto-3-deoxy-sugar acids. There is only a very limited amount of characterization data available on pentonate dehydratases, even though the enzymes from these oxidative pathways have potential applications with plant biomass pentose sugars. The two bacterial enzymes share 41 % amino acid sequence identity and were expressed and purified from
Escherichia coli
as homotetrameric proteins. Both dehydratases were shown to accept pentonate and hexonate sugar acids as their substrates and require Mg
2+
for their activity.
Cc
XyDHT displayed the highest activity on D-xylonate and D-gluconate, while
Rl
ArDHT functioned best on D-fuconate, L-arabonate and D-galactonate. The configuration of the OH groups at C2 and C3 position of the sugar acid were shown to be critical, and the C4 configuration also contributed substantially to the substrate recognition. The two enzymes were also shown to contain an iron–sulphur [Fe–S] cluster. Our phylogenetic analysis and mutagenesis studies demonstrated that the three conserved cysteine residues in the aldonic acid dehydratase group of IlvD/EDD family members, those of C60, C128 and C201 in
Cc
XyDHT, and of C59, C127 and C200 in
Rl
ArDHT, are needed for coordination of the [Fe–S] cluster. The iron–sulphur cluster was shown to be crucial for the catalytic activity (k
cat
) but not for the substrate binding (K
m
) of the two pentonate dehydratases.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>27102126</pmid><doi>10.1007/s00253-016-7530-8</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0003-4246-3938</orcidid></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0175-7598 |
ispartof | Applied microbiology and biotechnology, 2016-09, Vol.100 (17), p.7549-7563 |
issn | 0175-7598 1432-0614 |
language | eng |
recordid | cdi_hal_primary_oai_HAL_hal_01886409v1 |
source | MEDLINE; SpringerLink Journals - AutoHoldings |
subjects | Amino Acid Sequence Amino acids Arabinose - metabolism Bacterial Proteins - genetics Bacterial Proteins - metabolism Biomedical and Life Sciences Biotechnologically Relevant Enzymes and Proteins Biotechnology Caulobacter Caulobacter crescentus Caulobacter crescentus - enzymology Cloning Cloning, Molecular Dehydrogenases E coli Enzymes Escherichia coli Escherichia coli - genetics Escherichia coli - metabolism Genes Gluconates - metabolism Health aspects Hydrates Hydro-Lyases - genetics Hydro-Lyases - metabolism Iron Life Sciences Microbial Genetics and Genomics Microbiology Mutagenesis Observations Phylogenetics Plant biomass Proteins Rhizobium leguminosarum Rhizobium leguminosarum - enzymology Sequence Alignment Studies Sugar Sulfur Xylose - metabolism |
title | Characterization and mutagenesis of two novel iron–sulphur cluster pentonate dehydratases |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-25T02%3A31%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Characterization%20and%20mutagenesis%20of%20two%20novel%20iron%E2%80%93sulphur%20cluster%20pentonate%20dehydratases&rft.jtitle=Applied%20microbiology%20and%20biotechnology&rft.au=Andberg,%20Martina&rft.date=2016-09-01&rft.volume=100&rft.issue=17&rft.spage=7549&rft.epage=7563&rft.pages=7549-7563&rft.issn=0175-7598&rft.eissn=1432-0614&rft_id=info:doi/10.1007/s00253-016-7530-8&rft_dat=%3Cgale_hal_p%3EA470454181%3C/gale_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1810633349&rft_id=info:pmid/27102126&rft_galeid=A470454181&rfr_iscdi=true |