One Protein, Two Enzymes
Two enzymes, designated, E-2 and E-2â², catalyze different oxidation reactions of an aci-reductone intermediate in the methionine salvage pathway. E-2 and E-2â², overproduced in Escherichia coli from the same gene, have the same protein component. E-2 and E-2â² are separable on an anion exchange...
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| Veröffentlicht in: | The Journal of biological chemistry 1999-01, Vol.274 (3), p.1193-1195 |
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| container_title | The Journal of biological chemistry |
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| creator | Dai, Y Wensink, P C Abeles, R H |
| description | Two enzymes, designated, E-2 and E-2â², catalyze different oxidation reactions of an aci-reductone intermediate in the methionine
salvage pathway. E-2 and E-2â², overproduced in Escherichia coli from the same gene, have the same protein component. E-2 and E-2â² are separable on an anion exchange column or a hydrophobic
column. Their distinct catalytic and chromatographic properties result from binding different metals. The apo-enzyme, obtained
after metal is removed from either enzyme, is catalytically inactive. Addition of Ni 2+ or Co 2+ to the apo-protein yields E-2 activity. E-2â² activity is obtained when Fe 2+ is added. Production in intact E. coli of E-2 and E-2â² depends on the availability of the corresponding metals. These observations suggest that the metal component
dictates reaction specificity. |
| doi_str_mv | 10.1074/jbc.274.3.1193 |
| format | Article |
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salvage pathway. E-2 and E-2â², overproduced in Escherichia coli from the same gene, have the same protein component. E-2 and E-2â² are separable on an anion exchange column or a hydrophobic
column. Their distinct catalytic and chromatographic properties result from binding different metals. The apo-enzyme, obtained
after metal is removed from either enzyme, is catalytically inactive. Addition of Ni 2+ or Co 2+ to the apo-protein yields E-2 activity. E-2â² activity is obtained when Fe 2+ is added. Production in intact E. coli of E-2 and E-2â² depends on the availability of the corresponding metals. These observations suggest that the metal component
dictates reaction specificity.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.3.1193</identifier><identifier>PMID: 9880484</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Catalytic Domain ; Chromatography, Gel ; Chromatography, Ion Exchange ; Cobalt - metabolism ; Dioxygenases ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli ; Ferrous Compounds - metabolism ; Klebsiella pneumoniae - enzymology ; Klebsiella pneumoniae - genetics ; Methionine - analogs & derivatives ; Methionine - metabolism ; Molecular Sequence Data ; Nickel - metabolism ; Oxygenases - genetics ; Oxygenases - metabolism ; Recombinant Proteins - metabolism</subject><ispartof>The Journal of biological chemistry, 1999-01, Vol.274 (3), p.1193-1195</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-be340f3593b2193ec02c4ce7ea9a5fd099b6238aa5e45a6061b511ed6cf922d23</citedby><cites>FETCH-LOGICAL-c357t-be340f3593b2193ec02c4ce7ea9a5fd099b6238aa5e45a6061b511ed6cf922d23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9880484$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Dai, Y</creatorcontrib><creatorcontrib>Wensink, P C</creatorcontrib><creatorcontrib>Abeles, R H</creatorcontrib><title>One Protein, Two Enzymes</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Two enzymes, designated, E-2 and E-2â², catalyze different oxidation reactions of an aci-reductone intermediate in the methionine
salvage pathway. E-2 and E-2â², overproduced in Escherichia coli from the same gene, have the same protein component. E-2 and E-2â² are separable on an anion exchange column or a hydrophobic
column. Their distinct catalytic and chromatographic properties result from binding different metals. The apo-enzyme, obtained
after metal is removed from either enzyme, is catalytically inactive. Addition of Ni 2+ or Co 2+ to the apo-protein yields E-2 activity. E-2â² activity is obtained when Fe 2+ is added. Production in intact E. coli of E-2 and E-2â² depends on the availability of the corresponding metals. These observations suggest that the metal component
dictates reaction specificity.</description><subject>Catalytic Domain</subject><subject>Chromatography, Gel</subject><subject>Chromatography, Ion Exchange</subject><subject>Cobalt - metabolism</subject><subject>Dioxygenases</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli</subject><subject>Ferrous Compounds - metabolism</subject><subject>Klebsiella pneumoniae - enzymology</subject><subject>Klebsiella pneumoniae - genetics</subject><subject>Methionine - analogs & derivatives</subject><subject>Methionine - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Nickel - metabolism</subject><subject>Oxygenases - genetics</subject><subject>Oxygenases - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkE1Lw0AQhhdRaq1exYtQPHgycT-T3aOU-gGFeqjgbdndTExKk9TdllJ_vVtSxLnMYd55hnkQuiY4JTjnj0vrUprzlKWEKHaChgRLljBBPk_REGNKEkWFPEcXISxxLK7IAA2UlJhLPkQ38xbG777bQN0-jBe7bjxtf_YNhEt0VppVgKtjH6GP5-li8prM5i9vk6dZ4pjIN4kFxnHJhGKWxvvgMHXcQQ5GGVEWWCmbUSaNEcCFyXBGrCAEisyVitKCshG677lr331vIWx0UwcHq5VpodsGnSnBZcTHYNoHne9C8FDqta8b4_eaYH1QoaMKHVVopg8q4sLtkby1DRR_8ePvcX7Xz6v6q9rVHrStO1dB8x_yC6MIYv0</recordid><startdate>19990115</startdate><enddate>19990115</enddate><creator>Dai, Y</creator><creator>Wensink, P C</creator><creator>Abeles, R H</creator><general>American Society for Biochemistry and Molecular Biology</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>7X8</scope></search><sort><creationdate>19990115</creationdate><title>One Protein, Two Enzymes</title><author>Dai, Y ; Wensink, P C ; Abeles, R H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c357t-be340f3593b2193ec02c4ce7ea9a5fd099b6238aa5e45a6061b511ed6cf922d23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Catalytic Domain</topic><topic>Chromatography, Gel</topic><topic>Chromatography, Ion Exchange</topic><topic>Cobalt - metabolism</topic><topic>Dioxygenases</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli</topic><topic>Ferrous Compounds - metabolism</topic><topic>Klebsiella pneumoniae - enzymology</topic><topic>Klebsiella pneumoniae - genetics</topic><topic>Methionine - analogs & derivatives</topic><topic>Methionine - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Nickel - metabolism</topic><topic>Oxygenases - genetics</topic><topic>Oxygenases - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Dai, Y</creatorcontrib><creatorcontrib>Wensink, P C</creatorcontrib><creatorcontrib>Abeles, R H</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>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Dai, Y</au><au>Wensink, P C</au><au>Abeles, R H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>One Protein, Two Enzymes</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1999-01-15</date><risdate>1999</risdate><volume>274</volume><issue>3</issue><spage>1193</spage><epage>1195</epage><pages>1193-1195</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Two enzymes, designated, E-2 and E-2â², catalyze different oxidation reactions of an aci-reductone intermediate in the methionine
salvage pathway. E-2 and E-2â², overproduced in Escherichia coli from the same gene, have the same protein component. E-2 and E-2â² are separable on an anion exchange column or a hydrophobic
column. Their distinct catalytic and chromatographic properties result from binding different metals. The apo-enzyme, obtained
after metal is removed from either enzyme, is catalytically inactive. Addition of Ni 2+ or Co 2+ to the apo-protein yields E-2 activity. E-2â² activity is obtained when Fe 2+ is added. Production in intact E. coli of E-2 and E-2â² depends on the availability of the corresponding metals. These observations suggest that the metal component
dictates reaction specificity.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9880484</pmid><doi>10.1074/jbc.274.3.1193</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1999-01, Vol.274 (3), p.1193-1195 |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Catalytic Domain Chromatography, Gel Chromatography, Ion Exchange Cobalt - metabolism Dioxygenases Electrophoresis, Polyacrylamide Gel Escherichia coli Ferrous Compounds - metabolism Klebsiella pneumoniae - enzymology Klebsiella pneumoniae - genetics Methionine - analogs & derivatives Methionine - metabolism Molecular Sequence Data Nickel - metabolism Oxygenases - genetics Oxygenases - metabolism Recombinant Proteins - metabolism |
| title | One Protein, Two Enzymes |
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