Inactivation of rat muscle 5'-adenylate aminohydrolase by tyrosine nitration with tetranitromethane
Reaction of rat muscle AMP deaminase with low molar excess of tetranitromethane results in a rapid loss of free thiol groups and a concomitant decrease in enzyme activity at high, but not at low, AMP concentration. This modification appears to be limited to the same non-essential thiol groups reacti...
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| Veröffentlicht in: | Biochemical journal 1981-03, Vol.193 (3), p.853-859 |
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| container_title | Biochemical journal |
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| creator | Ranieri-Raggi, M Bergamini, C Montali, U Raggi, A |
| description | Reaction of rat muscle AMP deaminase with low molar excess of tetranitromethane results in a rapid loss of free thiol groups and a concomitant decrease in enzyme activity at high, but not at low, AMP concentration. This modification appears to be limited to the same non-essential thiol groups reactive towards specific reagents in non-denaturing conditions. On incubation with higher molar excess of tetranitromethane, a loss of enzyme activity is observed, which correlates with nitration of tyrosine residues. By amino acid analysis, approximately there tyrosine residues per subunit are estimated to be nitrated in the completely inactivated enzyme. The kinetic properties of the partially inactivated AMP deaminase reveal a negative co-operatively behaviour at approximately half saturation. This suggests that modification of tyrosine residues is also responsible for alteration of the binding properties of the hypothesized activating site of AMP deaminase. |
| doi_str_mv | 10.1042/bj1930853 |
| format | Article |
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This modification appears to be limited to the same non-essential thiol groups reactive towards specific reagents in non-denaturing conditions. On incubation with higher molar excess of tetranitromethane, a loss of enzyme activity is observed, which correlates with nitration of tyrosine residues. By amino acid analysis, approximately there tyrosine residues per subunit are estimated to be nitrated in the completely inactivated enzyme. The kinetic properties of the partially inactivated AMP deaminase reveal a negative co-operatively behaviour at approximately half saturation. This suggests that modification of tyrosine residues is also responsible for alteration of the binding properties of the hypothesized activating site of AMP deaminase.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj1930853</identifier><identifier>PMID: 7305963</identifier><language>eng</language><publisher>England</publisher><subject>AMP Deaminase - antagonists & inhibitors ; Animals ; Binding Sites ; Enzyme Activation - drug effects ; Kinetics ; Methane - analogs & derivatives ; Muscles - enzymology ; Nucleotide Deaminases - antagonists & inhibitors ; Rats ; Tetranitromethane - pharmacology ; Tyrosine - metabolism</subject><ispartof>Biochemical journal, 1981-03, Vol.193 (3), p.853-859</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1162677/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1162677/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7305963$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ranieri-Raggi, M</creatorcontrib><creatorcontrib>Bergamini, C</creatorcontrib><creatorcontrib>Montali, U</creatorcontrib><creatorcontrib>Raggi, A</creatorcontrib><title>Inactivation of rat muscle 5'-adenylate aminohydrolase by tyrosine nitration with tetranitromethane</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Reaction of rat muscle AMP deaminase with low molar excess of tetranitromethane results in a rapid loss of free thiol groups and a concomitant decrease in enzyme activity at high, but not at low, AMP concentration. This modification appears to be limited to the same non-essential thiol groups reactive towards specific reagents in non-denaturing conditions. On incubation with higher molar excess of tetranitromethane, a loss of enzyme activity is observed, which correlates with nitration of tyrosine residues. By amino acid analysis, approximately there tyrosine residues per subunit are estimated to be nitrated in the completely inactivated enzyme. The kinetic properties of the partially inactivated AMP deaminase reveal a negative co-operatively behaviour at approximately half saturation. This suggests that modification of tyrosine residues is also responsible for alteration of the binding properties of the hypothesized activating site of AMP deaminase.</description><subject>AMP Deaminase - antagonists & inhibitors</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Enzyme Activation - drug effects</subject><subject>Kinetics</subject><subject>Methane - analogs & derivatives</subject><subject>Muscles - enzymology</subject><subject>Nucleotide Deaminases - antagonists & inhibitors</subject><subject>Rats</subject><subject>Tetranitromethane - pharmacology</subject><subject>Tyrosine - metabolism</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1981</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUMtOwzAQtBColMKBD0DyDXEI-BUnviChikelSlzgHNnOhrhK7Cpxi_L3TdWqgtO-ZmZ3B6FbSh4pEezJrKjiJE_5GZpSkZEkz1h-jqaESZFIwugluur7FSFUEEEmaJJxkirJp8guvLbRbXV0weNQ4U5H3G562wBO7xNdgh8aHQHr1vlQD2UXGt0DNgOOQxd65wF7F7sD_9fFGkcYy30vtBBr7eEaXVS66eHmGGfo--31a_6RLD_fF_OXZWKZUjHhFoQAk1NGoLImA6VA55JokhprJE-ZpFVqZF7KlApurMoZG_MKuFCZqvgMPR901xvTQmnBj4c0xbpzre6GImhX_J94Vxc_YVtQKpnMslHg4SBgx8_6DqoTl5Jib3RxMnrE3v1ddkIeneU7-RB8Kg</recordid><startdate>19810301</startdate><enddate>19810301</enddate><creator>Ranieri-Raggi, M</creator><creator>Bergamini, C</creator><creator>Montali, U</creator><creator>Raggi, A</creator><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>5PM</scope></search><sort><creationdate>19810301</creationdate><title>Inactivation of rat muscle 5'-adenylate aminohydrolase by tyrosine nitration with tetranitromethane</title><author>Ranieri-Raggi, M ; Bergamini, C ; Montali, U ; Raggi, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c299t-3ce44eb8120efcb7e99ea860a05bcb635261f5b68d65143bc9822d65fe34979f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1981</creationdate><topic>AMP Deaminase - antagonists & inhibitors</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Enzyme Activation - drug effects</topic><topic>Kinetics</topic><topic>Methane - analogs & derivatives</topic><topic>Muscles - enzymology</topic><topic>Nucleotide Deaminases - antagonists & inhibitors</topic><topic>Rats</topic><topic>Tetranitromethane - pharmacology</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ranieri-Raggi, M</creatorcontrib><creatorcontrib>Bergamini, C</creatorcontrib><creatorcontrib>Montali, U</creatorcontrib><creatorcontrib>Raggi, A</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ranieri-Raggi, M</au><au>Bergamini, C</au><au>Montali, U</au><au>Raggi, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Inactivation of rat muscle 5'-adenylate aminohydrolase by tyrosine nitration with tetranitromethane</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1981-03-01</date><risdate>1981</risdate><volume>193</volume><issue>3</issue><spage>853</spage><epage>859</epage><pages>853-859</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Reaction of rat muscle AMP deaminase with low molar excess of tetranitromethane results in a rapid loss of free thiol groups and a concomitant decrease in enzyme activity at high, but not at low, AMP concentration. This modification appears to be limited to the same non-essential thiol groups reactive towards specific reagents in non-denaturing conditions. On incubation with higher molar excess of tetranitromethane, a loss of enzyme activity is observed, which correlates with nitration of tyrosine residues. By amino acid analysis, approximately there tyrosine residues per subunit are estimated to be nitrated in the completely inactivated enzyme. The kinetic properties of the partially inactivated AMP deaminase reveal a negative co-operatively behaviour at approximately half saturation. This suggests that modification of tyrosine residues is also responsible for alteration of the binding properties of the hypothesized activating site of AMP deaminase.</abstract><cop>England</cop><pmid>7305963</pmid><doi>10.1042/bj1930853</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 1981-03, Vol.193 (3), p.853-859 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | AMP Deaminase - antagonists & inhibitors Animals Binding Sites Enzyme Activation - drug effects Kinetics Methane - analogs & derivatives Muscles - enzymology Nucleotide Deaminases - antagonists & inhibitors Rats Tetranitromethane - pharmacology Tyrosine - metabolism |
| title | Inactivation of rat muscle 5'-adenylate aminohydrolase by tyrosine nitration with tetranitromethane |
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