Some properties of glutamine synthetase from Anabaena cylindrica
Some properties of the biosynthetic and γ-glutamyltransferase activities of glutamine synthetase (EC 6.3.1.2) from Anabaena cylindrica are described, including requirement for divalent cations, pH optimum and Km for substrates. The γ-glutamyltransferase reaction was inhibited by L-glutamate, ammonia...
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| Veröffentlicht in: | Planta 1978, Vol.139 (3), p.289-299 |
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| creator | Sawhney, S.K Nicholas, D.J.D |
| description | Some properties of the biosynthetic and γ-glutamyltransferase activities of glutamine synthetase (EC 6.3.1.2) from Anabaena cylindrica are described, including requirement for divalent cations, pH optimum and Km for substrates. The γ-glutamyltransferase reaction was inhibited by L-glutamate, ammonia and ATP. The inhibition by L-glutamate and ammonia was competitive for L-glutamine and non-competitive for hydroxylamine. Both the biosynthetic and the γ-glutamyltransferase activities of the desalted enzyme were much more sensitive to inactivarion by treatments such as urea, hydroxylamine and incubation at 50° C than the preparation which contained a divalent cation. The effects of some substrates of these reactions on protection against thermal denaturation and hydroxylamine were examined. An interpretation of these results in terms of the sequence of binding of substrates both in the biosynthetic and the γ-glutamyltransferase reactions are discussed. |
| doi_str_mv | 10.1007/BF00388643 |
| format | Article |
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The γ-glutamyltransferase reaction was inhibited by L-glutamate, ammonia and ATP. The inhibition by L-glutamate and ammonia was competitive for L-glutamine and non-competitive for hydroxylamine. Both the biosynthetic and the γ-glutamyltransferase activities of the desalted enzyme were much more sensitive to inactivarion by treatments such as urea, hydroxylamine and incubation at 50° C than the preparation which contained a divalent cation. The effects of some substrates of these reactions on protection against thermal denaturation and hydroxylamine were examined. An interpretation of these results in terms of the sequence of binding of substrates both in the biosynthetic and the γ-glutamyltransferase reactions are discussed.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/BF00388643</identifier><identifier>PMID: 24414273</identifier><language>eng</language><publisher>Germany: Springer-Verlag</publisher><subject>Algae ; Ammonia ; Arsenates ; Biosynthesis ; Chlorides ; Divalent cations ; Enzyme activity ; Enzyme preparations ; Enzymes ; Quaternary ammonium compounds ; Sodium</subject><ispartof>Planta, 1978, Vol.139 (3), p.289-299</ispartof><rights>Springer-Verlag 1978</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c331t-482f1169bdca57cbb60affc411a83a5e1ed1bae6c6af777eabec6a18bd2a7f0b3</citedby><cites>FETCH-LOGICAL-c331t-482f1169bdca57cbb60affc411a83a5e1ed1bae6c6af777eabec6a18bd2a7f0b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23373351$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23373351$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,4010,27902,27903,27904,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24414273$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sawhney, S.K</creatorcontrib><creatorcontrib>Nicholas, D.J.D</creatorcontrib><title>Some properties of glutamine synthetase from Anabaena cylindrica</title><title>Planta</title><addtitle>Planta</addtitle><description>Some properties of the biosynthetic and γ-glutamyltransferase activities of glutamine synthetase (EC 6.3.1.2) from Anabaena cylindrica are described, including requirement for divalent cations, pH optimum and Km for substrates. The γ-glutamyltransferase reaction was inhibited by L-glutamate, ammonia and ATP. The inhibition by L-glutamate and ammonia was competitive for L-glutamine and non-competitive for hydroxylamine. Both the biosynthetic and the γ-glutamyltransferase activities of the desalted enzyme were much more sensitive to inactivarion by treatments such as urea, hydroxylamine and incubation at 50° C than the preparation which contained a divalent cation. The effects of some substrates of these reactions on protection against thermal denaturation and hydroxylamine were examined. An interpretation of these results in terms of the sequence of binding of substrates both in the biosynthetic and the γ-glutamyltransferase reactions are discussed.</description><subject>Algae</subject><subject>Ammonia</subject><subject>Arsenates</subject><subject>Biosynthesis</subject><subject>Chlorides</subject><subject>Divalent cations</subject><subject>Enzyme activity</subject><subject>Enzyme preparations</subject><subject>Enzymes</subject><subject>Quaternary ammonium compounds</subject><subject>Sodium</subject><issn>0032-0935</issn><issn>1432-2048</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><recordid>eNpFkE1Lw0AQhhdRbK1evKs5ihCd_Ug2vVmLVaHgofYcJpvZmpKPupse-u9dqdrTDPM8vAwvY5cc7jmAfniaAcgsS5U8YkOupIgFqOyYDcNZxDCWyYCdeb8GCFDrUzYQSnEltByyx0XXULRx3YZcX5GPOhut6m2PTdVS5Hdt_0k9eoqs65po0mKB1GJkdnXVlq4yeM5OLNaeLn7niC1nzx_T13j-_vI2ncxjIyXvY5UJy3k6LkqDiTZFkQJaaxTnmElMiFPJQ3RqUrRaa8KCwsqzohSoLRRyxG73ueHXry35Pm8qb6iusaVu63OuxqBBpaCCerdXjeu8d2TzjasadLucQ_7TWH5oLMjXv7nboqHyX_2rKAhXe2Ht-84duJQBJjzwmz232OW4cpXPlwsBXIJQAIlW8humH3lK</recordid><startdate>1978</startdate><enddate>1978</enddate><creator>Sawhney, S.K</creator><creator>Nicholas, D.J.D</creator><general>Springer-Verlag</general><scope>FBQ</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1978</creationdate><title>Some properties of glutamine synthetase from Anabaena cylindrica</title><author>Sawhney, S.K ; Nicholas, D.J.D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c331t-482f1169bdca57cbb60affc411a83a5e1ed1bae6c6af777eabec6a18bd2a7f0b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Algae</topic><topic>Ammonia</topic><topic>Arsenates</topic><topic>Biosynthesis</topic><topic>Chlorides</topic><topic>Divalent cations</topic><topic>Enzyme activity</topic><topic>Enzyme preparations</topic><topic>Enzymes</topic><topic>Quaternary ammonium compounds</topic><topic>Sodium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sawhney, S.K</creatorcontrib><creatorcontrib>Nicholas, D.J.D</creatorcontrib><collection>AGRIS</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Planta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sawhney, S.K</au><au>Nicholas, D.J.D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Some properties of glutamine synthetase from Anabaena cylindrica</atitle><jtitle>Planta</jtitle><addtitle>Planta</addtitle><date>1978</date><risdate>1978</risdate><volume>139</volume><issue>3</issue><spage>289</spage><epage>299</epage><pages>289-299</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><abstract>Some properties of the biosynthetic and γ-glutamyltransferase activities of glutamine synthetase (EC 6.3.1.2) from Anabaena cylindrica are described, including requirement for divalent cations, pH optimum and Km for substrates. The γ-glutamyltransferase reaction was inhibited by L-glutamate, ammonia and ATP. The inhibition by L-glutamate and ammonia was competitive for L-glutamine and non-competitive for hydroxylamine. Both the biosynthetic and the γ-glutamyltransferase activities of the desalted enzyme were much more sensitive to inactivarion by treatments such as urea, hydroxylamine and incubation at 50° C than the preparation which contained a divalent cation. The effects of some substrates of these reactions on protection against thermal denaturation and hydroxylamine were examined. An interpretation of these results in terms of the sequence of binding of substrates both in the biosynthetic and the γ-glutamyltransferase reactions are discussed.</abstract><cop>Germany</cop><pub>Springer-Verlag</pub><pmid>24414273</pmid><doi>10.1007/BF00388643</doi><tpages>11</tpages></addata></record> |
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| ispartof | Planta, 1978, Vol.139 (3), p.289-299 |
| issn | 0032-0935 1432-2048 |
| language | eng |
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| source | Jstor Complete Legacy; SpringerLink Journals - AutoHoldings |
| subjects | Algae Ammonia Arsenates Biosynthesis Chlorides Divalent cations Enzyme activity Enzyme preparations Enzymes Quaternary ammonium compounds Sodium |
| title | Some properties of glutamine synthetase from Anabaena cylindrica |
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