Identification and characterization of 2-keto-3-deoxygluconate kinase and 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii
Abstract The halophilic archaeon Haloferax volcanii has been proposed to degrade glucose via the semi-phosphorylative Entner–Doudoroff pathway, involving 2-keto-3-deoxygluconate kinase (KDGK) as key enzyme. So far, neither the enzyme has been characterized nor the encoding gene has been identified....
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| Veröffentlicht in: | FEMS microbiology letters 2014-12, Vol.361 (1), p.76-83 |
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| creator | Pickl, Andreas Johnsen, Ulrike Archer, Robert M. Schönheit, Peter |
| description | Abstract
The halophilic archaeon Haloferax volcanii has been proposed to degrade glucose via the semi-phosphorylative Entner–Doudoroff pathway, involving 2-keto-3-deoxygluconate kinase (KDGK) as key enzyme. So far, neither the enzyme has been characterized nor the encoding gene has been identified. In the genome of H. volcanii, two genes, HVO_0549 (kdgK1) and HVO_A0328 (kdgK2), are annotated encoding putative KDGK-1 and KDGK-2. To identify the physiological role of both kinases, transcriptional regulation analyses of both genes and growth experiments of the respective deletion mutants were performed on different sugars. Further, recombinant KDGK-1 and KDGK-2 were characterized. Together, the data indicate that KDGK-1 represents the functional constitutively expressed KDG kinase in glucose degradation, whereas KDGK-2 is an inducible 2-keto-3-deoxygalactonate kinase likely involved in d-galactose catabolism.
The paper describes the identification of KDGK-1 as functional 2-keto-3-deoxygluconate kinase in the semi-phosphorylative ED pathway of glucose degradation and of KDGK-2 as 2-keto-3-deoxygalactonate kinase in galactose degradation in H. volcanii. Both enzymes belong to the PFK (phosphofructokinase)-B family of carbohydrate kinases.
The paper describes the identification of KDGK-1 as functional 2-keto-3-deoxygluconate kinase in the semi-phosphorylative ED pathway of glucose degradation and of KDGK-2 as 2-keto-3-deoxygalactonate kinase in galactose degradation in H. volcanii. Both enzymes belong to the PFK (phosphofructokinase)-B family of carbohydrate kinases. |
| doi_str_mv | 10.1111/1574-6968.12617 |
| format | Article |
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The halophilic archaeon Haloferax volcanii has been proposed to degrade glucose via the semi-phosphorylative Entner–Doudoroff pathway, involving 2-keto-3-deoxygluconate kinase (KDGK) as key enzyme. So far, neither the enzyme has been characterized nor the encoding gene has been identified. In the genome of H. volcanii, two genes, HVO_0549 (kdgK1) and HVO_A0328 (kdgK2), are annotated encoding putative KDGK-1 and KDGK-2. To identify the physiological role of both kinases, transcriptional regulation analyses of both genes and growth experiments of the respective deletion mutants were performed on different sugars. Further, recombinant KDGK-1 and KDGK-2 were characterized. Together, the data indicate that KDGK-1 represents the functional constitutively expressed KDG kinase in glucose degradation, whereas KDGK-2 is an inducible 2-keto-3-deoxygalactonate kinase likely involved in d-galactose catabolism.
The paper describes the identification of KDGK-1 as functional 2-keto-3-deoxygluconate kinase in the semi-phosphorylative ED pathway of glucose degradation and of KDGK-2 as 2-keto-3-deoxygalactonate kinase in galactose degradation in H. volcanii. Both enzymes belong to the PFK (phosphofructokinase)-B family of carbohydrate kinases.
The paper describes the identification of KDGK-1 as functional 2-keto-3-deoxygluconate kinase in the semi-phosphorylative ED pathway of glucose degradation and of KDGK-2 as 2-keto-3-deoxygalactonate kinase in galactose degradation in H. volcanii. Both enzymes belong to the PFK (phosphofructokinase)-B family of carbohydrate kinases.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/1574-6968.12617</identifier><identifier>PMID: 25287957</identifier><language>eng</language><publisher>England: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Galactose - metabolism ; Glucose - metabolism ; glucose degradation ; Glycolysis ; Haloarchaea ; Haloferax volcanii - enzymology ; Haloferax volcanii - genetics ; Microbiology ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor) - genetics ; Phosphotransferases (Alcohol Group Acceptor) - metabolism ; semi‐phosphorylative Entner–Doudoroff pathway ; Sequence Alignment ; substrate promiscuity</subject><ispartof>FEMS microbiology letters, 2014-12, Vol.361 (1), p.76-83</ispartof><rights>2014 Federation of European Microbiological Societies. 2014</rights><rights>2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved</rights><rights>2014 Federation of European Microbiological Societies.</rights><rights>Copyright © 2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4067-970f3222ef78e54c6c2078b15db8029510ef238ebb66feec6a3856bdbcacba303</citedby><cites>FETCH-LOGICAL-c4067-970f3222ef78e54c6c2078b15db8029510ef238ebb66feec6a3856bdbcacba303</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2F1574-6968.12617$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2F1574-6968.12617$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25287957$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pickl, Andreas</creatorcontrib><creatorcontrib>Johnsen, Ulrike</creatorcontrib><creatorcontrib>Archer, Robert M.</creatorcontrib><creatorcontrib>Schönheit, Peter</creatorcontrib><title>Identification and characterization of 2-keto-3-deoxygluconate kinase and 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
The halophilic archaeon Haloferax volcanii has been proposed to degrade glucose via the semi-phosphorylative Entner–Doudoroff pathway, involving 2-keto-3-deoxygluconate kinase (KDGK) as key enzyme. So far, neither the enzyme has been characterized nor the encoding gene has been identified. In the genome of H. volcanii, two genes, HVO_0549 (kdgK1) and HVO_A0328 (kdgK2), are annotated encoding putative KDGK-1 and KDGK-2. To identify the physiological role of both kinases, transcriptional regulation analyses of both genes and growth experiments of the respective deletion mutants were performed on different sugars. Further, recombinant KDGK-1 and KDGK-2 were characterized. Together, the data indicate that KDGK-1 represents the functional constitutively expressed KDG kinase in glucose degradation, whereas KDGK-2 is an inducible 2-keto-3-deoxygalactonate kinase likely involved in d-galactose catabolism.
The paper describes the identification of KDGK-1 as functional 2-keto-3-deoxygluconate kinase in the semi-phosphorylative ED pathway of glucose degradation and of KDGK-2 as 2-keto-3-deoxygalactonate kinase in galactose degradation in H. volcanii. Both enzymes belong to the PFK (phosphofructokinase)-B family of carbohydrate kinases.
The paper describes the identification of KDGK-1 as functional 2-keto-3-deoxygluconate kinase in the semi-phosphorylative ED pathway of glucose degradation and of KDGK-2 as 2-keto-3-deoxygalactonate kinase in galactose degradation in H. volcanii. Both enzymes belong to the PFK (phosphofructokinase)-B family of carbohydrate kinases.</description><subject>Amino Acid Sequence</subject><subject>Galactose - metabolism</subject><subject>Glucose - metabolism</subject><subject>glucose degradation</subject><subject>Glycolysis</subject><subject>Haloarchaea</subject><subject>Haloferax volcanii - enzymology</subject><subject>Haloferax volcanii - genetics</subject><subject>Microbiology</subject><subject>Phosphorylation</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - genetics</subject><subject>Phosphotransferases (Alcohol Group Acceptor) - metabolism</subject><subject>semi‐phosphorylative Entner–Doudoroff pathway</subject><subject>Sequence Alignment</subject><subject>substrate promiscuity</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFLHDEYhkOp1NX23FsZ6KUI0SQzk2SOIrUKK17sOWQyX7rR2WSbzKjrv_AfN-uoWBHMJeTjeZ988CL0lZJ9ms8BrUWFecPlPmWcig9o9jz5iGakFBJT0ohttJPSJSGkYoR_QtusZlI0tZih-9MO_OCsM3pwwRfad4VZ6KjNANHdTcNgC4avYAi4xB2E2_WffjTB6wGKK-d1gofYK0T32fEf5HwxLKBY6D7omD-BrD7JDwtR3xbXoTfaO_cZbVndJ_jyeO-i38c_L45O8Pz81-nR4RybinCBG0FsyRgDKyTUleGGESFbWnetJKypKQHLSglty7kFMFyXsuZt1xptWl2Schf9mLyrGP6OkAa1dMlA32sPYUyKSsY5KSu6Qb-_Qi_DGH3eTlGeCS4lEZk6mCgTQ0oRrFpFt9RxrShRm7bUphu16UY9tJUT3x69Y7uE7pl_qicD9QTcuB7W7_nU8dn8Sbw35cK4ejOFX2zxD0K0rNM</recordid><startdate>20141201</startdate><enddate>20141201</enddate><creator>Pickl, Andreas</creator><creator>Johnsen, Ulrike</creator><creator>Archer, Robert M.</creator><creator>Schönheit, Peter</creator><general>Blackwell Publishing Ltd</general><general>Oxford University Press</general><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>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20141201</creationdate><title>Identification and characterization of 2-keto-3-deoxygluconate kinase and 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii</title><author>Pickl, Andreas ; Johnsen, Ulrike ; Archer, Robert M. ; Schönheit, Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4067-970f3222ef78e54c6c2078b15db8029510ef238ebb66feec6a3856bdbcacba303</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Galactose - metabolism</topic><topic>Glucose - metabolism</topic><topic>glucose degradation</topic><topic>Glycolysis</topic><topic>Haloarchaea</topic><topic>Haloferax volcanii - enzymology</topic><topic>Haloferax volcanii - genetics</topic><topic>Microbiology</topic><topic>Phosphorylation</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - genetics</topic><topic>Phosphotransferases (Alcohol Group Acceptor) - metabolism</topic><topic>semi‐phosphorylative Entner–Doudoroff pathway</topic><topic>Sequence Alignment</topic><topic>substrate promiscuity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pickl, Andreas</creatorcontrib><creatorcontrib>Johnsen, Ulrike</creatorcontrib><creatorcontrib>Archer, Robert M.</creatorcontrib><creatorcontrib>Schönheit, Peter</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pickl, Andreas</au><au>Johnsen, Ulrike</au><au>Archer, Robert M.</au><au>Schönheit, Peter</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification and characterization of 2-keto-3-deoxygluconate kinase and 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2014-12-01</date><risdate>2014</risdate><volume>361</volume><issue>1</issue><spage>76</spage><epage>83</epage><pages>76-83</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><abstract>Abstract
The halophilic archaeon Haloferax volcanii has been proposed to degrade glucose via the semi-phosphorylative Entner–Doudoroff pathway, involving 2-keto-3-deoxygluconate kinase (KDGK) as key enzyme. So far, neither the enzyme has been characterized nor the encoding gene has been identified. In the genome of H. volcanii, two genes, HVO_0549 (kdgK1) and HVO_A0328 (kdgK2), are annotated encoding putative KDGK-1 and KDGK-2. To identify the physiological role of both kinases, transcriptional regulation analyses of both genes and growth experiments of the respective deletion mutants were performed on different sugars. Further, recombinant KDGK-1 and KDGK-2 were characterized. Together, the data indicate that KDGK-1 represents the functional constitutively expressed KDG kinase in glucose degradation, whereas KDGK-2 is an inducible 2-keto-3-deoxygalactonate kinase likely involved in d-galactose catabolism.
The paper describes the identification of KDGK-1 as functional 2-keto-3-deoxygluconate kinase in the semi-phosphorylative ED pathway of glucose degradation and of KDGK-2 as 2-keto-3-deoxygalactonate kinase in galactose degradation in H. volcanii. Both enzymes belong to the PFK (phosphofructokinase)-B family of carbohydrate kinases.
The paper describes the identification of KDGK-1 as functional 2-keto-3-deoxygluconate kinase in the semi-phosphorylative ED pathway of glucose degradation and of KDGK-2 as 2-keto-3-deoxygalactonate kinase in galactose degradation in H. volcanii. Both enzymes belong to the PFK (phosphofructokinase)-B family of carbohydrate kinases.</abstract><cop>England</cop><pub>Blackwell Publishing Ltd</pub><pmid>25287957</pmid><doi>10.1111/1574-6968.12617</doi><tpages>8</tpages></addata></record> |
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| subjects | Amino Acid Sequence Galactose - metabolism Glucose - metabolism glucose degradation Glycolysis Haloarchaea Haloferax volcanii - enzymology Haloferax volcanii - genetics Microbiology Phosphorylation Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism semi‐phosphorylative Entner–Doudoroff pathway Sequence Alignment substrate promiscuity |
| title | Identification and characterization of 2-keto-3-deoxygluconate kinase and 2-keto-3-deoxygalactonate kinase in the haloarchaeon Haloferax volcanii |
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