Occurrence of old yellow enzyme in Gluconobacter suboxydans, and the cyclic regeneration of NADP
Old yellow enzyme system has been found in the cytosol fraction of Gluconobacter suboxydans. This is the first time that the enzyme has been found in organisms other than yeast cells. Old yellow enzyme [EC 1.6.99.1], D-glucose-6-phosphate dehydrogenase [EC 1.1.1.49], and catalase were isolated and c...
Gespeichert in:
| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1979-09, Vol.86 (3), p.699-709 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 709 |
|---|---|
| container_issue | 3 |
| container_start_page | 699 |
| container_title | Journal of biochemistry (Tokyo) |
| container_volume | 86 |
| creator | Adachi, O Matsushita, K Shinagawa, E Ameyama, M. (Yamaguchi Univ. (Japan). Faculty of Agriculture) |
| description | Old yellow enzyme system has been found in the cytosol fraction of Gluconobacter suboxydans. This is the first time that the enzyme has been found in organisms other than yeast cells. Old yellow enzyme [EC 1.6.99.1], D-glucose-6-phosphate dehydrogenase [EC 1.1.1.49], and catalase were isolated and crystallized separately from the organism. The old yellow enzyme from G. suboxydans showed catalytic and physicochemical properties almost identical with those of the enzyme from yeast cells. NADPH was specifically oxidized by the old yellow enzyme and the reduced enzyme was spontaneously reoxidized by atmospheric oxygen. The old yellow enzyme from G. suboxydans also contained FMN as a prosthetic group, and two mol of FMN were found per mol of enzyme (molecular weight, 88,000 as determined by gel filtration). In the oxidation of D-glucose-6-phosphate to 6-phospho-D-gluconate, cyclic regeneration of NADP occurred smoothly in the presence of D-glucose-6-phosphate dehydrogenase and catalase, even when a limited amount of NADP or NADPH was present in the reaction mixture. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a132574 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_74791600</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>74791600</sourcerecordid><originalsourceid>FETCH-LOGICAL-c510t-83229a11d612976488ba037eb89dcf23bbdd7952d89bafdf248b7386d183f8263</originalsourceid><addsrcrecordid>eNpVkEtv1DAUhS1EBUPLH4CNN7Aigx-J7SxYVH3MgCraSiBGbIyfbYbELnYiJvx6MmRUidXV1Tn3cT4A3mC0xKim7-POx2S3cUhBtXm51ebedUuFKal4-QQsMK9YQViFn4IFQgQXNSk3z8GLnLf7llD6DByVWFCxAD-ujRlScsE4GD2MrYWja9v4G7rwZ-wcbAJctYOJIWplepdgHnTcjVaF_A6qYGF_76AZTdsYmNydCy6pvolhv-3z6fnNCTjy05fu5aEeg6-XF1_O1sXV9erj2elVYSqM-kJQQmqFsWWY1JyVQmiFKHda1NZ4QrW2ltcVsaLWyltPSqE5FcxOMbwgjB6Dt_PehxR_DS73smuymaKo4OKQJS95jRlCk_HDbDQp5pyclw-p6VQaJUZyz1f-z1fOfOWB7zT_-nBo0J2zj9P_gE5qMatN7t3uUVTpp2Sc8kquN9_l-tv6ckXYrdxM_lez36so1V1qsvx0IxDCFCP6F84mloE</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>74791600</pqid></control><display><type>article</type><title>Occurrence of old yellow enzyme in Gluconobacter suboxydans, and the cyclic regeneration of NADP</title><source>J-STAGE Free</source><source>MEDLINE</source><source>Free Full-Text Journals in Chemistry</source><source>Oxford University Press Journals Digital Archive Legacy</source><creator>Adachi, O ; Matsushita, K ; Shinagawa, E ; Ameyama, M. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</creator><creatorcontrib>Adachi, O ; Matsushita, K ; Shinagawa, E ; Ameyama, M. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</creatorcontrib><description>Old yellow enzyme system has been found in the cytosol fraction of Gluconobacter suboxydans. This is the first time that the enzyme has been found in organisms other than yeast cells. Old yellow enzyme [EC 1.6.99.1], D-glucose-6-phosphate dehydrogenase [EC 1.1.1.49], and catalase were isolated and crystallized separately from the organism. The old yellow enzyme from G. suboxydans showed catalytic and physicochemical properties almost identical with those of the enzyme from yeast cells. NADPH was specifically oxidized by the old yellow enzyme and the reduced enzyme was spontaneously reoxidized by atmospheric oxygen. The old yellow enzyme from G. suboxydans also contained FMN as a prosthetic group, and two mol of FMN were found per mol of enzyme (molecular weight, 88,000 as determined by gel filtration). In the oxidation of D-glucose-6-phosphate to 6-phospho-D-gluconate, cyclic regeneration of NADP occurred smoothly in the presence of D-glucose-6-phosphate dehydrogenase and catalase, even when a limited amount of NADP or NADPH was present in the reaction mixture.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a132574</identifier><identifier>PMID: 41838</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Catalase - isolation & purification ; Chromatography, Gel ; Crystallization ; Electrophoresis, Polyacrylamide Gel ; Flavin Mononucleotide - analysis ; Glucosephosphate Dehydrogenase - isolation & purification ; NADH, NADPH Oxidoreductases - isolation & purification ; NADP - metabolism ; NADPH Dehydrogenase - isolation & purification ; Oxygen - metabolism ; Pseudomonadaceae - enzymology ; Ultracentrifugation</subject><ispartof>Journal of biochemistry (Tokyo), 1979-09, Vol.86 (3), p.699-709</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c510t-83229a11d612976488ba037eb89dcf23bbdd7952d89bafdf248b7386d183f8263</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/41838$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Adachi, O</creatorcontrib><creatorcontrib>Matsushita, K</creatorcontrib><creatorcontrib>Shinagawa, E</creatorcontrib><creatorcontrib>Ameyama, M. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</creatorcontrib><title>Occurrence of old yellow enzyme in Gluconobacter suboxydans, and the cyclic regeneration of NADP</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Old yellow enzyme system has been found in the cytosol fraction of Gluconobacter suboxydans. This is the first time that the enzyme has been found in organisms other than yeast cells. Old yellow enzyme [EC 1.6.99.1], D-glucose-6-phosphate dehydrogenase [EC 1.1.1.49], and catalase were isolated and crystallized separately from the organism. The old yellow enzyme from G. suboxydans showed catalytic and physicochemical properties almost identical with those of the enzyme from yeast cells. NADPH was specifically oxidized by the old yellow enzyme and the reduced enzyme was spontaneously reoxidized by atmospheric oxygen. The old yellow enzyme from G. suboxydans also contained FMN as a prosthetic group, and two mol of FMN were found per mol of enzyme (molecular weight, 88,000 as determined by gel filtration). In the oxidation of D-glucose-6-phosphate to 6-phospho-D-gluconate, cyclic regeneration of NADP occurred smoothly in the presence of D-glucose-6-phosphate dehydrogenase and catalase, even when a limited amount of NADP or NADPH was present in the reaction mixture.</description><subject>Catalase - isolation & purification</subject><subject>Chromatography, Gel</subject><subject>Crystallization</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Flavin Mononucleotide - analysis</subject><subject>Glucosephosphate Dehydrogenase - isolation & purification</subject><subject>NADH, NADPH Oxidoreductases - isolation & purification</subject><subject>NADP - metabolism</subject><subject>NADPH Dehydrogenase - isolation & purification</subject><subject>Oxygen - metabolism</subject><subject>Pseudomonadaceae - enzymology</subject><subject>Ultracentrifugation</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkEtv1DAUhS1EBUPLH4CNN7Aigx-J7SxYVH3MgCraSiBGbIyfbYbELnYiJvx6MmRUidXV1Tn3cT4A3mC0xKim7-POx2S3cUhBtXm51ebedUuFKal4-QQsMK9YQViFn4IFQgQXNSk3z8GLnLf7llD6DByVWFCxAD-ujRlScsE4GD2MrYWja9v4G7rwZ-wcbAJctYOJIWplepdgHnTcjVaF_A6qYGF_76AZTdsYmNydCy6pvolhv-3z6fnNCTjy05fu5aEeg6-XF1_O1sXV9erj2elVYSqM-kJQQmqFsWWY1JyVQmiFKHda1NZ4QrW2ltcVsaLWyltPSqE5FcxOMbwgjB6Dt_PehxR_DS73smuymaKo4OKQJS95jRlCk_HDbDQp5pyclw-p6VQaJUZyz1f-z1fOfOWB7zT_-nBo0J2zj9P_gE5qMatN7t3uUVTpp2Sc8kquN9_l-tv6ckXYrdxM_lez36so1V1qsvx0IxDCFCP6F84mloE</recordid><startdate>197909</startdate><enddate>197909</enddate><creator>Adachi, O</creator><creator>Matsushita, K</creator><creator>Shinagawa, E</creator><creator>Ameyama, M. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</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></search><sort><creationdate>197909</creationdate><title>Occurrence of old yellow enzyme in Gluconobacter suboxydans, and the cyclic regeneration of NADP</title><author>Adachi, O ; Matsushita, K ; Shinagawa, E ; Ameyama, M. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c510t-83229a11d612976488ba037eb89dcf23bbdd7952d89bafdf248b7386d183f8263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Catalase - isolation & purification</topic><topic>Chromatography, Gel</topic><topic>Crystallization</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Flavin Mononucleotide - analysis</topic><topic>Glucosephosphate Dehydrogenase - isolation & purification</topic><topic>NADH, NADPH Oxidoreductases - isolation & purification</topic><topic>NADP - metabolism</topic><topic>NADPH Dehydrogenase - isolation & purification</topic><topic>Oxygen - metabolism</topic><topic>Pseudomonadaceae - enzymology</topic><topic>Ultracentrifugation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Adachi, O</creatorcontrib><creatorcontrib>Matsushita, K</creatorcontrib><creatorcontrib>Shinagawa, E</creatorcontrib><creatorcontrib>Ameyama, M. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</creatorcontrib><collection>AGRIS</collection><collection>Istex</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>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Adachi, O</au><au>Matsushita, K</au><au>Shinagawa, E</au><au>Ameyama, M. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Occurrence of old yellow enzyme in Gluconobacter suboxydans, and the cyclic regeneration of NADP</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1979-09</date><risdate>1979</risdate><volume>86</volume><issue>3</issue><spage>699</spage><epage>709</epage><pages>699-709</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>Old yellow enzyme system has been found in the cytosol fraction of Gluconobacter suboxydans. This is the first time that the enzyme has been found in organisms other than yeast cells. Old yellow enzyme [EC 1.6.99.1], D-glucose-6-phosphate dehydrogenase [EC 1.1.1.49], and catalase were isolated and crystallized separately from the organism. The old yellow enzyme from G. suboxydans showed catalytic and physicochemical properties almost identical with those of the enzyme from yeast cells. NADPH was specifically oxidized by the old yellow enzyme and the reduced enzyme was spontaneously reoxidized by atmospheric oxygen. The old yellow enzyme from G. suboxydans also contained FMN as a prosthetic group, and two mol of FMN were found per mol of enzyme (molecular weight, 88,000 as determined by gel filtration). In the oxidation of D-glucose-6-phosphate to 6-phospho-D-gluconate, cyclic regeneration of NADP occurred smoothly in the presence of D-glucose-6-phosphate dehydrogenase and catalase, even when a limited amount of NADP or NADPH was present in the reaction mixture.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>41838</pmid><doi>10.1093/oxfordjournals.jbchem.a132574</doi><tpages>11</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-924X |
| ispartof | Journal of biochemistry (Tokyo), 1979-09, Vol.86 (3), p.699-709 |
| issn | 0021-924X 1756-2651 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_74791600 |
| source | J-STAGE Free; MEDLINE; Free Full-Text Journals in Chemistry; Oxford University Press Journals Digital Archive Legacy |
| subjects | Catalase - isolation & purification Chromatography, Gel Crystallization Electrophoresis, Polyacrylamide Gel Flavin Mononucleotide - analysis Glucosephosphate Dehydrogenase - isolation & purification NADH, NADPH Oxidoreductases - isolation & purification NADP - metabolism NADPH Dehydrogenase - isolation & purification Oxygen - metabolism Pseudomonadaceae - enzymology Ultracentrifugation |
| title | Occurrence of old yellow enzyme in Gluconobacter suboxydans, and the cyclic regeneration of NADP |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T08%3A15%3A19IST&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=Occurrence%20of%20old%20yellow%20enzyme%20in%20Gluconobacter%20suboxydans,%20and%20the%20cyclic%20regeneration%20of%20NADP&rft.jtitle=Journal%20of%20biochemistry%20(Tokyo)&rft.au=Adachi,%20O&rft.date=1979-09&rft.volume=86&rft.issue=3&rft.spage=699&rft.epage=709&rft.pages=699-709&rft.issn=0021-924X&rft.eissn=1756-2651&rft_id=info:doi/10.1093/oxfordjournals.jbchem.a132574&rft_dat=%3Cproquest_cross%3E74791600%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=74791600&rft_id=info:pmid/41838&rfr_iscdi=true |