Purification and Characterization of Citrate Synthase from Streptomyces hygroscopicus SF-1293 and Comparison of Its Properties with Those of 2-Phosphinomethylmalic Acid Synthase
To study the relationship between citrate synthase and 2-phosphinomethylmalic acid (PMM) synthase, which catalyzes a very similar reaction comparable to citrate formation in the biosynthesis of a herbicide, bialaphos, citrate synthase was purified from the mycelium of Streptomyces hygroscopicus SF-1...
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| Veröffentlicht in: | Agricultural and biological chemistry 1990-02, Vol.54 (2), p.463-470 |
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| creator | Shimotohno, Kumiko W. Imai, Satoshi Murakami, Takeshi Seto, Haruo |
| description | To study the relationship between citrate synthase and 2-phosphinomethylmalic acid (PMM) synthase, which catalyzes a very similar reaction comparable to citrate formation in the biosynthesis of a herbicide, bialaphos, citrate synthase was purified from the mycelium of Streptomyces hygroscopicus SF-1293, a bialaphos-producing organism. The overall purification was 440-fold with a yield of 4.4% from cell-free extract. Based on comparison with PMM synthase, it has been concluded that citrate synthase of S. hygroscopicus is quite different from PMM synthase in several aspects such as enzymatic properties, amino acid composition. N-terminal amino acid sequence, and stereo-chemical reaction mechanism. |
| doi_str_mv | 10.1080/00021369.1990.10869949 |
| format | Article |
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The overall purification was 440-fold with a yield of 4.4% from cell-free extract. Based on comparison with PMM synthase, it has been concluded that citrate synthase of S. hygroscopicus is quite different from PMM synthase in several aspects such as enzymatic properties, amino acid composition. N-terminal amino acid sequence, and stereo-chemical reaction mechanism.</description><identifier>ISSN: 0002-1369</identifier><identifier>DOI: 10.1080/00021369.1990.10869949</identifier><identifier>PMID: 1368511</identifier><language>eng</language><publisher>Japan: Taylor & Francis</publisher><subject>2-phosphinomethylmalic acid synthase ; Amino Acid Sequence ; Base Sequence ; Biotechnology ; Citrate (si)-Synthase - genetics ; Citrate (si)-Synthase - isolation & purification ; Citrate (si)-Synthase - metabolism ; citrate synthase ; Cloning, Molecular ; DNA, Bacterial - genetics ; Kinetics ; Molecular Sequence Data ; Oxo-Acid-Lyases - genetics ; Oxo-Acid-Lyases - metabolism ; Restriction Mapping ; Streptomyces - enzymology ; Streptomyces - genetics</subject><ispartof>Agricultural and biological chemistry, 1990-02, Vol.54 (2), p.463-470</ispartof><rights>Copyright, 1990, by the Japan Society for Bioscience, Biotechnology, and Agrochemistry. 1990</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c346t-aeb7490d2d125940fa3c7463eaecd1bfd2f9e7168c635a6982be840fb17d4b713</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1368511$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shimotohno, Kumiko W.</creatorcontrib><creatorcontrib>Imai, Satoshi</creatorcontrib><creatorcontrib>Murakami, Takeshi</creatorcontrib><creatorcontrib>Seto, Haruo</creatorcontrib><title>Purification and Characterization of Citrate Synthase from Streptomyces hygroscopicus SF-1293 and Comparison of Its Properties with Those of 2-Phosphinomethylmalic Acid Synthase</title><title>Agricultural and biological chemistry</title><addtitle>Agric Biol Chem</addtitle><description>To study the relationship between citrate synthase and 2-phosphinomethylmalic acid (PMM) synthase, which catalyzes a very similar reaction comparable to citrate formation in the biosynthesis of a herbicide, bialaphos, citrate synthase was purified from the mycelium of Streptomyces hygroscopicus SF-1293, a bialaphos-producing organism. The overall purification was 440-fold with a yield of 4.4% from cell-free extract. Based on comparison with PMM synthase, it has been concluded that citrate synthase of S. hygroscopicus is quite different from PMM synthase in several aspects such as enzymatic properties, amino acid composition. N-terminal amino acid sequence, and stereo-chemical reaction mechanism.</description><subject>2-phosphinomethylmalic acid synthase</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biotechnology</subject><subject>Citrate (si)-Synthase - genetics</subject><subject>Citrate (si)-Synthase - isolation & purification</subject><subject>Citrate (si)-Synthase - metabolism</subject><subject>citrate synthase</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial - genetics</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Oxo-Acid-Lyases - genetics</subject><subject>Oxo-Acid-Lyases - metabolism</subject><subject>Restriction Mapping</subject><subject>Streptomyces - enzymology</subject><subject>Streptomyces - genetics</subject><issn>0002-1369</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUctu1DAUzaKoLS2fAPKKXYod52EvRyMKlSox0rRr68YPYhTHwXZUhb_iD_GQFpZd2TpP6Z6i-EDwDcEMf8IYV4S2_IZw_hdqOa_5WXF5IsoTc1G8jfEHxg2mGJ8X5xljDSGXxe_DEqyxEpL1E4JJof0AAWTSwf7aQG_Q3qYASaPjOqUBokYmeIeOKeg5ebdKHdGwfg8-Sj9buUR0vC1JxekW6N0MwcYt6i5FdAh-1iHZbHuyaUAPg8-ZmazKQ_7Og52802lYRwejlWgnrfrXfV28MTBG_e75vSoebz8_7L-W99--3O1396WkdZtK0H1Xc6wqRaqG19gAlV3dUg1aKtIbVRmuO9Iy2dIGWs6qXrMs60mn6r4j9Kr4uOXOwf9cdEzC2Sj1OMKk_RJFx3lOZuxVIWlYx0jTZGG7CWW-VAzaiDlYB2EVBIvTkOJlSHEaUrwMmY3vnxuW3mn137atmPndxtvJ-ODgyYdRiQTr6IMJMEkbBX2l4w9tNLMM</recordid><startdate>199002</startdate><enddate>199002</enddate><creator>Shimotohno, Kumiko W.</creator><creator>Imai, Satoshi</creator><creator>Murakami, Takeshi</creator><creator>Seto, Haruo</creator><general>Taylor & Francis</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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>199002</creationdate><title>Purification and Characterization of Citrate Synthase from Streptomyces hygroscopicus SF-1293 and Comparison of Its Properties with Those of 2-Phosphinomethylmalic Acid Synthase</title><author>Shimotohno, Kumiko W. ; 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The overall purification was 440-fold with a yield of 4.4% from cell-free extract. Based on comparison with PMM synthase, it has been concluded that citrate synthase of S. hygroscopicus is quite different from PMM synthase in several aspects such as enzymatic properties, amino acid composition. N-terminal amino acid sequence, and stereo-chemical reaction mechanism.</abstract><cop>Japan</cop><pub>Taylor & Francis</pub><pmid>1368511</pmid><doi>10.1080/00021369.1990.10869949</doi><tpages>8</tpages></addata></record> |
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| ispartof | Agricultural and biological chemistry, 1990-02, Vol.54 (2), p.463-470 |
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| language | eng |
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| source | J-STAGE Free; MEDLINE; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | 2-phosphinomethylmalic acid synthase Amino Acid Sequence Base Sequence Biotechnology Citrate (si)-Synthase - genetics Citrate (si)-Synthase - isolation & purification Citrate (si)-Synthase - metabolism citrate synthase Cloning, Molecular DNA, Bacterial - genetics Kinetics Molecular Sequence Data Oxo-Acid-Lyases - genetics Oxo-Acid-Lyases - metabolism Restriction Mapping Streptomyces - enzymology Streptomyces - genetics |
| title | Purification and Characterization of Citrate Synthase from Streptomyces hygroscopicus SF-1293 and Comparison of Its Properties with Those of 2-Phosphinomethylmalic Acid Synthase |
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