Characterization of oxime metabolizing enzymes in a cyanobacterium Phormidium uncinatum, utilizing ethyl acetohydroximate as sole nitrogen source
Ethyl acetohydroximate-adapted phototrophic cultures of Phormidium uncinatum metabolized this oxime via hydrolysis/oxidation and dismutation of resulting hydroxylamine to nitrite and ammonia. Participating enzymes were bound to thylakoid membranes, which were solubilized and purified by conventional...
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| Veröffentlicht in: | Indian journal of experimental biology 1999-10, Vol.37 (10), p.990-994 |
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| container_title | Indian journal of experimental biology |
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| creator | Bagchi, S N Shakila, T M |
| description | Ethyl acetohydroximate-adapted phototrophic cultures of Phormidium uncinatum metabolized this oxime via hydrolysis/oxidation and dismutation of resulting hydroxylamine to nitrite and ammonia. Participating enzymes were bound to thylakoid membranes, which were solubilized and purified by conventional techniques using QAE-Sephadex and DEAE-Cellulose columns. Specific activity of bound enzymes increased in the range of 25-75 folds. With partially purified enzymes, apparent Km values of hydrolase and oxidase for oxime and dismutase for hydroxylamine were 180, 15 and 36 mu M respectively. |
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Participating enzymes were bound to thylakoid membranes, which were solubilized and purified by conventional techniques using QAE-Sephadex and DEAE-Cellulose columns. Specific activity of bound enzymes increased in the range of 25-75 folds. 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With partially purified enzymes, apparent Km values of hydrolase and oxidase for oxime and dismutase for hydroxylamine were 180, 15 and 36 mu M respectively.</description><subject>ammonia</subject><subject>ethyl acetohydroximate</subject><subject>hydroxylamine</subject><subject>nitrite</subject><subject>Phormidium uncinatum</subject><issn>0019-5189</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><recordid>eNo1jLtOwzAYRjOARCm8gycmIjkXJ_aIIm5SJRi6V3_s341RbBdfJNK34I2hKkzf-YZzLooVpZUoWcXFVXEd4welHROCrorvYYIAMmEwR0jGO-I18V_GIrGYYPSzORq3J-iOi8VIjCNA5ALOj2crW_I--WCNOmF20jhI2d6TnMy_m6ZlJiAx-WlR4VSHhAQiiX5G4kwKfo_u9-Ug8aa41DBHvP3bdbF9etwOL-Xm7fl1eNiUByFSKTuqWQ9KKKWB6R4550ClamutO9lpziqoRS8UZ33TSGSjUMgr7FvWjrVizbq4O2cPwX9mjGlnTZQ4z-DQ57ir-o5S1tLmB-6DZtI</recordid><startdate>19991001</startdate><enddate>19991001</enddate><creator>Bagchi, S N</creator><creator>Shakila, T M</creator><scope>M7N</scope></search><sort><creationdate>19991001</creationdate><title>Characterization of oxime metabolizing enzymes in a cyanobacterium Phormidium uncinatum, utilizing ethyl acetohydroximate as sole nitrogen source</title><author>Bagchi, S N ; Shakila, T M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p99t-c60f57ad9ddfa5f7e888a0cd42ff6c6f851a2979d85733ce5b9de81e7454b2d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>ammonia</topic><topic>ethyl acetohydroximate</topic><topic>hydroxylamine</topic><topic>nitrite</topic><topic>Phormidium uncinatum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bagchi, S N</creatorcontrib><creatorcontrib>Shakila, T M</creatorcontrib><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>Indian journal of experimental biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bagchi, S N</au><au>Shakila, T M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of oxime metabolizing enzymes in a cyanobacterium Phormidium uncinatum, utilizing ethyl acetohydroximate as sole nitrogen source</atitle><jtitle>Indian journal of experimental biology</jtitle><date>1999-10-01</date><risdate>1999</risdate><volume>37</volume><issue>10</issue><spage>990</spage><epage>994</epage><pages>990-994</pages><issn>0019-5189</issn><abstract>Ethyl acetohydroximate-adapted phototrophic cultures of Phormidium uncinatum metabolized this oxime via hydrolysis/oxidation and dismutation of resulting hydroxylamine to nitrite and ammonia. Participating enzymes were bound to thylakoid membranes, which were solubilized and purified by conventional techniques using QAE-Sephadex and DEAE-Cellulose columns. Specific activity of bound enzymes increased in the range of 25-75 folds. With partially purified enzymes, apparent Km values of hydrolase and oxidase for oxime and dismutase for hydroxylamine were 180, 15 and 36 mu M respectively.</abstract><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0019-5189 |
| ispartof | Indian journal of experimental biology, 1999-10, Vol.37 (10), p.990-994 |
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| language | eng |
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| source | DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | ammonia ethyl acetohydroximate hydroxylamine nitrite Phormidium uncinatum |
| title | Characterization of oxime metabolizing enzymes in a cyanobacterium Phormidium uncinatum, utilizing ethyl acetohydroximate as sole nitrogen source |
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