Mitochondrial Isocitrate Dehydrogenases from Yeast
A polarographic technique suitable for kinetic studies of either isolated or bound pyridine nucleotide-linked dehydrogenases was used to investigate the isocitrate dehydrogenases of yeast mitochondria. Intact mitochondria were found to contain both triphosphopyridine nucleotide- and diphosphopyridin...
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| Veröffentlicht in: | The Journal of biological chemistry 1966-11, Vol.241 (22), p.5461-5466 |
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| container_issue | 22 |
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| container_title | The Journal of biological chemistry |
| container_volume | 241 |
| creator | Bernofsky, C Utter, M F |
| description | A polarographic technique suitable for kinetic studies of either isolated or bound pyridine nucleotide-linked dehydrogenases
was used to investigate the isocitrate dehydrogenases of yeast mitochondria. Intact mitochondria were found to contain both
triphosphopyridine nucleotide- and diphosphopyridine nucleotide-linked isocitrate dehydrogenases with properties very similar
to those which have been reported for the isolated dehydrogenases. The DPN-linked enzyme in situ exhibits a nonclassical, sigmoid substrate against activity relationship with respect to isocitrate and is activated by adenosine
5'-monophosphate. The TPN-linked enzyme in situ exhibits a hyperbolic substrate against activity relationship which is unaffected by AMP.
The DPN-linked dehydrogenase also shows another non-classical increase in activity that occurs in response to high isocitrate
concentrations or to heat treatment. This activation is characteristic only of untreated, intact mitochondria and may be secondary
to an alteration of the mitochondria themselves. |
| doi_str_mv | 10.1016/S0021-9258(18)96452-5 |
| format | Article |
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was used to investigate the isocitrate dehydrogenases of yeast mitochondria. Intact mitochondria were found to contain both
triphosphopyridine nucleotide- and diphosphopyridine nucleotide-linked isocitrate dehydrogenases with properties very similar
to those which have been reported for the isolated dehydrogenases. The DPN-linked enzyme in situ exhibits a nonclassical, sigmoid substrate against activity relationship with respect to isocitrate and is activated by adenosine
5'-monophosphate. The TPN-linked enzyme in situ exhibits a hyperbolic substrate against activity relationship which is unaffected by AMP.
The DPN-linked dehydrogenase also shows another non-classical increase in activity that occurs in response to high isocitrate
concentrations or to heat treatment. This activation is characteristic only of untreated, intact mitochondria and may be secondary
to an alteration of the mitochondria themselves.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(18)96452-5</identifier><identifier>PMID: 4380945</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Adenine Nucleotides - metabolism ; Isocitrate Dehydrogenase - metabolism ; Kinetics ; Mitochondria - enzymology ; NAD - metabolism ; NADP - metabolism ; Polarography ; Saccharomyces - cytology ; Saccharomyces - enzymology</subject><ispartof>The Journal of biological chemistry, 1966-11, Vol.241 (22), p.5461-5466</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c379t-bc2c47ad8beb4b5cf4f67cbba1b54351ac420ed7d5a9be16c4cda694be84af93</citedby><cites>FETCH-LOGICAL-c379t-bc2c47ad8beb4b5cf4f67cbba1b54351ac420ed7d5a9be16c4cda694be84af93</cites></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/4380945$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bernofsky, C</creatorcontrib><creatorcontrib>Utter, M F</creatorcontrib><title>Mitochondrial Isocitrate Dehydrogenases from Yeast</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A polarographic technique suitable for kinetic studies of either isolated or bound pyridine nucleotide-linked dehydrogenases
was used to investigate the isocitrate dehydrogenases of yeast mitochondria. Intact mitochondria were found to contain both
triphosphopyridine nucleotide- and diphosphopyridine nucleotide-linked isocitrate dehydrogenases with properties very similar
to those which have been reported for the isolated dehydrogenases. The DPN-linked enzyme in situ exhibits a nonclassical, sigmoid substrate against activity relationship with respect to isocitrate and is activated by adenosine
5'-monophosphate. The TPN-linked enzyme in situ exhibits a hyperbolic substrate against activity relationship which is unaffected by AMP.
The DPN-linked dehydrogenase also shows another non-classical increase in activity that occurs in response to high isocitrate
concentrations or to heat treatment. This activation is characteristic only of untreated, intact mitochondria and may be secondary
to an alteration of the mitochondria themselves.</description><subject>Adenine Nucleotides - metabolism</subject><subject>Isocitrate Dehydrogenase - metabolism</subject><subject>Kinetics</subject><subject>Mitochondria - enzymology</subject><subject>NAD - metabolism</subject><subject>NADP - metabolism</subject><subject>Polarography</subject><subject>Saccharomyces - cytology</subject><subject>Saccharomyces - enzymology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1966</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtLAzEQx4MotVY_QmFBED2sJtlkNzlKfRUqHuxBTyHJznYju01Ntki_vdsHncsc_o8ZfgiNCb4nmOQPnxhTkkrKxS0RdzJnnKb8BA0JFlmacfJ1ioZHyzm6iPEH98MkGaABywSWjA8RfXedt7VflsHpJplGb10XdAfJE9SbMvgFLHWEmFTBt8k36NhdorNKNxGuDnuE5i_P88lbOvt4nU4eZ6nNCtmlxlLLCl0KA4YZbitW5YU1RhPDWf-ftoxiKIuSa2mA5JbZUueSGRBMVzIboZt97Sr43zXETrUuWmgavQS_jkowymVRZL2R7402-BgDVGoVXKvDRhGstqjUDpXaclBEqB0qxfvc-HBgbVooj6kDm16_3uu1W9R_LoAyrkcFraKMKNpXsJxk__VZcTg</recordid><startdate>19661125</startdate><enddate>19661125</enddate><creator>Bernofsky, C</creator><creator>Utter, M F</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>19661125</creationdate><title>Mitochondrial Isocitrate Dehydrogenases from Yeast</title><author>Bernofsky, C ; Utter, M F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c379t-bc2c47ad8beb4b5cf4f67cbba1b54351ac420ed7d5a9be16c4cda694be84af93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1966</creationdate><topic>Adenine Nucleotides - metabolism</topic><topic>Isocitrate Dehydrogenase - metabolism</topic><topic>Kinetics</topic><topic>Mitochondria - enzymology</topic><topic>NAD - metabolism</topic><topic>NADP - metabolism</topic><topic>Polarography</topic><topic>Saccharomyces - cytology</topic><topic>Saccharomyces - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bernofsky, C</creatorcontrib><creatorcontrib>Utter, M F</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>Bernofsky, C</au><au>Utter, M F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mitochondrial Isocitrate Dehydrogenases from Yeast</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1966-11-25</date><risdate>1966</risdate><volume>241</volume><issue>22</issue><spage>5461</spage><epage>5466</epage><pages>5461-5466</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>A polarographic technique suitable for kinetic studies of either isolated or bound pyridine nucleotide-linked dehydrogenases
was used to investigate the isocitrate dehydrogenases of yeast mitochondria. Intact mitochondria were found to contain both
triphosphopyridine nucleotide- and diphosphopyridine nucleotide-linked isocitrate dehydrogenases with properties very similar
to those which have been reported for the isolated dehydrogenases. The DPN-linked enzyme in situ exhibits a nonclassical, sigmoid substrate against activity relationship with respect to isocitrate and is activated by adenosine
5'-monophosphate. The TPN-linked enzyme in situ exhibits a hyperbolic substrate against activity relationship which is unaffected by AMP.
The DPN-linked dehydrogenase also shows another non-classical increase in activity that occurs in response to high isocitrate
concentrations or to heat treatment. This activation is characteristic only of untreated, intact mitochondria and may be secondary
to an alteration of the mitochondria themselves.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>4380945</pmid><doi>10.1016/S0021-9258(18)96452-5</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 1966-11, Vol.241 (22), p.5461-5466 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Adenine Nucleotides - metabolism Isocitrate Dehydrogenase - metabolism Kinetics Mitochondria - enzymology NAD - metabolism NADP - metabolism Polarography Saccharomyces - cytology Saccharomyces - enzymology |
| title | Mitochondrial Isocitrate Dehydrogenases from Yeast |
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